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Physicochemical properties of house cricket (Acheta domesticus) protein and antioxidant stability of its enzymatic hydrolysate under pH, temperature and in vitro digestion

in Journal of Insects as Food and Feed
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Bung-Orn Hemung School of Applied Sciences, Faculty of Interdisciplinary Studies, Khon Kaen University, Nong Khai 43000, Thailand

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Natteewan Udomsil Division of Food Technology, School of Interdisciplinary Studies, Mahidol University Kanchanaburi Campus, Lumsum, Saiyok, Kanchanaburi 71150, Thailand

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Sumeth Imsoonthornruksa Center for Biomolecular Structure Function and Application, School of Biotechnology, Suranaree University of Technology, 111 University Ave., Nakhon Ratchasima 30000, Thailand

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Ratasark Summart Center for Biomolecular Structure Function and Application, School of Biotechnology, Suranaree University of Technology, 111 University Ave., Nakhon Ratchasima 30000, Thailand

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Mariena Ketudat-Cairns Center for Biomolecular Structure Function and Application, School of Biotechnology, Suranaree University of Technology, 111 University Ave., Nakhon Ratchasima 30000, Thailand

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Online-Publikationsdatum:
01 Apr 2026

Abstract

House cricket (Acheta domesticus) is a sustainable protein source but faces low consumer acceptance for direct consumption. To enhance its usability, cricket protein isolate (CPI) and its enzymatic hydrolysates (CPH) were characterized as potential functional ingredients. Cricket powder contained 71% protein, with an amino acid profile comparable to animal proteins. CPI exhibited favourable functional properties, including high water-binding capacity (4.9 g water/g sample), emulsifying activity (EAI approx. 5.5 m2/g), and stable emulsifying performance (ESI). Protein solubility was lowest at pH 4.0, indicating the isoelectric point (pI), while foaming ability increased under alkaline conditions but decreased near the pI. Hydrolysis with alcalase and flavourzyme achieved higher degrees of hydrolysis and enhanced antioxidant activity. CPH showed thermal-activated and acid-stable antioxidative activity. These results demonstrate the potential of cricket proteins as functional and antioxidant-rich ingredients, supporting the development of innovative, more acceptable insect-based foods.

Schlüsselwörter:antioxidant stability; cricket hydrolysate; emulsifying; foaming; in vitro digestion; protein solubility

1 Introduction

Insects have emerged as promising contributors to global food and feed security due to their high nutritional value, rapid growth rates, and low environmental impact (Tang et al., 2019). They are rich in proteins, essential fatty acids, vitamins, and minerals (Tzompa-Sosa and Fogliano, 2017; Tzompa-Sosa et al., 2014) Although insects are traditionally consumed in many parts of Asia, Africa, and Latin America, negative perceptions such as disgust and reluctance persist in Western societies (de-Magistris, 2015). Interestingly, acceptance is notably higher when insects are incorporated in processed foods in an unrecognizable form (Tan et al., 2015).

In response to growing interest, the edible insect industry in Europe and North America has developed commercial-scale production of insect flours from species such as crickets for use in both human food and animal feed (Baigts-Allende, et al., 2021; Melgar-Lalanne et al., 2019). These products are commonly obtained by drying and milling whole insects. However, to broaden their use and improve consumer acceptability, it is essential to develop alternative forms such as protein isolates and concentrates. Alkaline extraction followed by isoelectric precipitation is a widely used method to recover protein isolates from various sources, including legumes and oilseeds. This technique holds promise for insects as well. Protein isolates derived from crickets have been reported to exhibit limited solubility and poor foaming or gelling properties, particularly when extracted under acidic conditions (Yi et al., 2013). In contrast, functional characteristics of cricket proteins isolated by alkaline precipitation remain underexplored. Characterizing such isolates is crucial for determining their suitability as functional food ingredients, particularly in terms of solubility, emulsifying and foaming properties, and water and oil binding capacities.

Furthermore, enzymatic hydrolysis has been demonstrated to improve the functional properties of insect proteins, especially in enhancing emulsification and foaming capacity (Hall et al., 2017; Xie et al., 2019). Cricket protein hydrolysates have also been investigated for flavour modification through Maillard reactions to improve sensory properties (Grossmann et al., 2021). In addition, hydrolysates generated using enzymes such as alcalase have also shown increased antioxidant activity and higher degrees of hydrolysis in plant protein systems (Liu et al., 2022; Minh, 2015). Despite these advances, limited research has examined the enzymatic hydrolysis of cricket protein isolates, especially using alcalase, flavourzyme, or their combination. The antioxidative properties and stability of these hydrolysates remain unclear.

Therefore, this study aimed to (i) characterize the functional properties of protein isolates obtained from house cricket (Acheta domesticus) via alkaline extraction, and (ii) investigate the effects of enzymatic hydrolysis using alcalase, flavourzyme, or a sequential combination of both enzymes on the degree of hydrolysis, antioxidant activity, and functional properties of the resulting hydrolysates. By comparing the properties of both the native isolate (CPI) and the hydrolysed form (CPH), this research provides comprehensive insights into how enzymatic treatment modifies techno-functional behaviour. The findings offer valuable guidance for the development of insect-based food ingredients with improved functionality and antioxidant potential, supporting wider consumer acceptance and contributing to sustainable food innovation.

2 Materials and methods

Proximate analysis of cricket powder

Cricket powder was purchased from J.R. Unique Foods (Thailand). Its proximate analysis was performed according to AOAC (2000). Moisture content was determined based on oven drying at 105 °C for over 12 h. Protein determination was based on nitrogen content using the Kjeldahl method. An ether extract was used to estimate the crude fat content. Total ash content determination was performed by dry ashing overnight at over 550 °C. Finally, carbohydrate content was calculated from the difference between these quantities and the total composition.

Isolation of cricket protein

Cricket protein isolation was adapted from Föste et al. (2014) and Ganguly et al. (2021). Briefly, cricket powder and distilled water were mixed in a ratio of 1:10 (w/v). The mixture pH was adjusted to 12.0 by adding 2.5 M NaOH and stirring at room temperature for 60 min. The mixture was centrifuged at 4000 × g for 20 min at 4 °C. Supernatant was collected and adjusted to pH 4.0 using 2.5 M HCl with stirring at room temperature for 30 min. Precipitated protein was collected by centrifugation at 4000 × g for 20 min at 4 °C. Cricket protein was then dialyzed in deionized water (DI) at a 1:50 ratio for 24 h followed by lyophilization (Alpha 2-4 LSC, Osterode, Germany). Lyophilized protein was a cricket protein isolate (CPI) and stored at –20 °C until used.

Generation of cricket protein hydrolysate (CPH) by enzymatic hydrolysis

Cricket protein isolate (CPI) suspension (12%, w/v) were subjected to enzymatic hydrolysis under three conditions: (i) alcalase, (ii) flavourzyme, and (iii) a combination of alcalase and flavourzyme. CPI was separately hydrolysed with each enzyme (5%, w/w) at 55 °C for 3 h. For sequential hydrolysis, CPI was first treated with Alcalase 2.4 L® (5%, w/w) at pH 9.0 and incubated at 55 °C for 1, 2 and 3 h. The mixture was then heated at 100 °C for 15 min to inactivate the enzyme. Subsequently, flavourzyme (5%, w/w) was added to the hydrolysate for further digestion under the same conditions. All enzymatic reactions were terminated by heating at 100 °C for 10 min. The hydrolysate was cooled before centrifugation at 9000 × g for 10 min. The supernatant was collected for lyophilization to obtain CPH before string it at –20 °C for further analysis and characterization.

Degree of hydrolysis

The degree of hydrolysis was measured using a trinitroben-zenesulphonic acid (TNBS) method (Adler-Nissen, 1979). For each trial, a 1 ml aliquot was removed. After each hydrolysis (30, 60 and 90 min), samples were centrifuged at 10 000 × g for 5 min. A 50 μl aliquot from the supernatant was mixed with 0.5 ml of 0.2 M sodium borate buffer (pH 8.0) and 0.5 ml of TNBS (0.05%). These solutions were incubated in the dark at 50 °C for 60 min. Then, 1 ml of 0.1 M HCl was added to the mixture and left at room temperature for 30 min. The absorbance of the samples was measured at 420 nm (UV-Visible spectrophotometer, Beckmann, Irvine, CA, USA).

Antioxidant activities of CPH

DPPH radical-scavenging activity: The hydrolysate (1 ml) was mixed with 1 ml of 0.1 mM DPPH dissolved in ethanol. This mixture was kept in the dark at room temperature for 10 min. Its absorbance was monitored at 517 nm (Pharmacia-Biotech Ultrospec 2000 UV-Visible spectrophotometer). The DPPH radical scavenging activity was determined and expressed as a percentage of inhibition, according to the method previously described by Chang et al. (2007).

ABTS radical-scavenging activity: CPH (20 μl; 1 mg/ml) was mixed with 1.98 ml of ABTS. The reaction mixture was incubated for 10 min at room temperature in the dark. Its absorbance at 734 nm was measured. The final results were expressed as a percentage of radical inhibition, following a previously described method (Yu et al., 2013).

Fe2 + chelating activity: Each sample (1 ml) was mixed with 3.7 ml of distilled water (DI). Then, 0.1 ml of 2 mmol/l FeCl2 and 0.2 ml of 5 mmol/l ferrozine were added to the mixture. This was allowed to run at room temperature for 20 min. Its absorbance was measured at 562 nm. DPPH Fe2 + chelating activity was expressed as a percentage of radical inhibition.

Functional properties of CPI and CPH using combined enzyme

Solubility of CPI and CPH as a function of pH: The solubility of the CPI and CPH was determined using a method described by Hall et al. (2017). Briefly, 30 mg of CPI was dispersed in 3 ml of McIlvaine buffer at the pH values of 2.2, 4.0, 6.0, 7.0, 8.0, 10.0, and 12.0. The mixtures were vigorously mixed for 3 min at room temperature using a vortex mixer before centrifugation at 7500 × g for 15 min. The supernatant was collected for protein content determination by a Lowry method using bovine serum albumin as a standard. Protein solubility was expressed as a percentage relative to the original weight of the sample.

Foaming capability: The foaming capability of CPI and CPH was estimated according to the method described by Wang et al. (2024). CPI (0.3 g) was dispersed in 10 ml of McIlvaine buffer at various pH values (6.0, 7.0 and 8.0). Protein mixtures were placed in 50 ml conical tubes and homogenized at 11 000 rpm for 2 min for aeration to generate protein foam. Foam volumes were measured at 0, 30, 60 and 90 min. Foaming capability was expressed as a percentage ratio of foam volume before and after aeration.
Foaming capability ( % ) = ( Volume of foam ∕ Volume of initial solution ) × 100
Water binding capacity: Water binding capacity (WBC) was determined according to Dion-Poulin et al. (2021). Briefly, 0.5 g of CPI was mixed with 5 g of McIlvaine buffer (pH 6.0, 7.0 and 8.0), vortexed for 30 s, and left at room temperature for 10 min. Samples were centrifuged at 10 000 × g for 10 min at 4 °C before decanting the supernatant. The unbound water was drained from the precipitate by placing the centrifugation tube upside-down on a tissue paper before weighing. The WBC was expressed as the percentage of absorbed water to the dried samples as shown in the equation below:
WBC ( % ) = ( ( W 2 − W 1 ) ∕ W 1 ) × 100 ,
where W 1 =weight (g) of dried sample and W 2 =weight (g) of precipitate after removing unbound water.
Oil binding capacity: Soybean oil (5 g) was added to 0.5 g of CPI and placed in a conical tube before vortexing (30 s) 3 times (each interval was 2 min). Samples were centrifuged at 16 000 × g for 10 min at 4 °C. The resulting pellets were immediately weighed after decanting the supernatants Dion-Poulin et al. (2021). The oil binding capacity (OBC) was expressed as the wight percentage of absorbed oil to the dried samples as:
OBC ( % ) = ( ( W 2 − W 1 ) ∕ W 1 ) × 100 ,
where W 1 =weight (g) of dried sample and W2=weight (g) of precipitate after removing unbound oil.
Emulsifying properties: The emulsifying activity index (EAI) and emulsion stability index (ESI) were determined according to Liu et al. (2020) with slight modifications. Samples (15 ml of CP or CPHs at 1 mg/ml in 0.2 M phosphate buffer, pH 7.0) were mixed with 5 ml of soybean oil and homogenized (IKA T25 Ultra-Turrax, 10 000 rpm, 2 min). Emulsions collected at 0 and 30 min were diluted 10–30 times with 0.1% SDS, and absorbance was measured at 500 nm using 0.1% SDS as the blank. EAI and ESI were calculated as described by Dion-Poulin et al. (2020).
EAI ( m 2 ∕ g ) = ( 4.606 × A 0 × DF ) ( c × φ × 10000 ) ESI ( min ) = A 0 A 0 − A 30 × 30 ,
where A 0 and A 30 are the absorbance of the diluted emulsion after homogenization at 0 and 30 min, DF is the dilution factor, c (g/ml) is the concentration of hydrolysates, and φ is the soybean oil volume fraction of the emulsion (0.25).

Total amino acid profile of CPI and CPH

The total amino acid contents of cricket powder, CPI and CPH were determined according to Udomsil et al. (2019). Briefly, 12 M HCl containing 1% phenol was added to the samples and hydrolysed in a microwave oven (Anton Paar, Graz, Austria). Subsequently, the samples were precipitated and filtered through a membrane filter having 0.22-mm pores. Cysteine and methionine contents were hydrolysed after oxidation with performic acid. Tryptophan determination was done after alkaline hydroxylation of the samples with 4.2 M NaOH. Ninhydrin was used for post-column derivatization with spectrophotometric detection at 570 nm. However, proline was measured at 440 nm. Total amino acids were measured using an amino acid analyser (Biochrom 30, Pharmacia Biotech, Amersham, UK) and quantified by comparison with standards (A6282 and A6407, Sigma-Aldrich, St Louis, MO, USA).

Effect of temperature and pH on CPH antioxidant stabilities

The stability of antioxidative capability was evaluated using DPPH radical scavenging activity due to its predominant mode of action. Each sample (0.25 mg/ml, IC50 value, 1 ml) was heated for 30 min at temperatures of 37, 50, 70, 100 and 121 °C. The effect of pH (2, 4, 5, 7, 10 and 12) was determined by incubating samples at room temperature for 30 min. After heating or pH treatment, all samples were cooled in an ice-water bath for 5 min. The DPPH radical scavenging activities of the samples were determined. A control sample was stored at room temperature (RT) for 30 min before being placed in an ice water bath for 5 min (Chaijan et al., 2021).

Effect of gastrointestinal digestion on CPH antioxidant stabilities

Simulated gastrointestinal (GI) digestion was performed using a pepsin-pancreatin method (Chaijan et al., 2021). The pH of a CPI solution (0.25 mg/ml, IC50 value, 1 ml) was adjusted to 2.0 using 2 M HCl before adding PS to a final concentration of 4%. This was done to evaluate sample stability in the presence of pepsin (PS). The reaction mixture was shaken constantly at 37 °C for 1 h. The same process was repeated and followed by pH adjustment to 7.5 using 1 M NaOH before adding 2% of pancreatin (PC). This was done to separately determine the sample stability in the presence of PS and PC. The mixture was incubated at 37 °C for 3 h with constant shaking. During digestion, samples were taken at various times between 0 and 240 min. The sample was halted by heating at 100 °C for 10 min to inhibit enzyme activity. These samples were used for determination of DPPH radical scavenging activity.

Statistical analysis

Chemical experiments were done in triplicate. Statistical analysis was performed using SPSS 13.0 software (SPSS, Chicago, IL, USA). Analysis of variance was used to evaluate significant differences between samples, and mean differences were determined by Duncan’s multiple range test at p < 0.05.

3 Results

Chemical composition of cricket powder

The nutritional composition of cricket powder was determined, and these values are presented in Table 1. Protein content of cricket powder was 71.69%, fat 9.88%, fibre 8.63%, ash 6.3%, moisture 2.65%, and carbohydrate content was negligible. The results indicated that cricket powder has a high protein content. The total fibre was about 8.63%, derived from the chitin residue. Cricket powders tested in the present study have relatively high crude protein. If protein quality is high in terms of human nutritional requirements, insect powders may serve as raw food materials to formulate high-quality protein concentrates/isolates.

Chemical composition of whole cricket (\textit{Acheta domesticus} ) powder
Table 1

Chemical composition of whole cricket (Acheta domesticus) powder

Citation: Journal of Insects as Food and Feed 2026; 10.1163/23524588-bja10397

Degree of hydrolysis and DPPH radical scavenging activity of CPH

Alcalase, a widely used endoprotease derived from Bacillus licheniformis, is known for its broad substrate specificity and high hydrolysis efficiency, often resulting in a high yield of bioactive peptides (Kristinsson and Rasco, 2000). In contrast, Flavourzyme, produced by Aspergillus oryzae, possesses both endo- and exopeptidase activities, which further hydrolyse peptides generated by Alcalase into shorter peptides or free amino acids. This dual activity not only reduces bitterness but also improves the flavour and overall functional properties of the resulting hydrolysate (Guo et al., 2013). Therefore, the combination of alcalase and flavourzyme was selected to efficiently produce short-chain peptides with enhanced bioactivity and favourable sensory characteristics from cricket protein.

Hydrolysis of CPI by alcalase provided a degree of hydrolysis of about 33% with a digestion time of 3 h (Table 2). Hydrolysis of CPI by flavourzyme was more effective than by alcalase, as it exhibited comparable antioxidant activity ( p > 0.05). Although flavourzyme showed less capability to hydrolyse CPI, a synergistic effect was observed after combining it with alcalase. The DH values obtained from sequential hydrolysis (AF2–AF6) were higher than those from individual enzyme hydrolysis (Table 2). The antioxidant activity of cricket peptides, assessed by DPPH radical scavenging ability, increased proportionally with DH (Table 2). Sequential hydrolysis with combined enzymes showed higher antioxidant activity than single enzymes ( p < 0.05). However, hydrolysis of CPI with the combined enzymes for 6 hours did not significantly increase DPPH radical scavenging activity ( p > 0.05), although it resulted in a significantly higher DH value ( p < 0.05). The antioxidant activity of AF2 was comparable to that of AF4 and AF6 ( p > 0.05). Therefore, AF2 was selected as the optimal condition for evaluating the functional properties of CPH, as well as the stability of its antioxidant activity under various conditions. These findings suggest that enzyme combinations can provide more effective protein hydrolysis than single enzymes.

Degree of hydrolysis (DH) and DPPH$\cdot $ radical scavenging of CPI hydrolysate and cricket protein hydrolysate (CPH) prepared using individual and combined enzymes
Table 2

Degree of hydrolysis (DH) and DPPH⋅ radical scavenging of CPI hydrolysate and cricket protein hydrolysate (CPH) prepared using individual and combined enzymes

Citation: Journal of Insects as Food and Feed 2026; 10.1163/23524588-bja10397

Functionalities of CPI and CPH

Solubility of CPI and CPH: The solubility of CPI and CPH across a pH range of 2.0 to 12.0 was shown in Figure 1. CPI exhibited the lowest solubility at pH 4.0, indicating the isoelectric point (pI) of the protein, where precipitation was most pronounced. Solubility gradually increased with increasing pH, particularly from pH 6 to 12, reaching a maximum of approximately 60.5% at pH 12.0. This solubility trend reflects the enhanced solubility of CPI under alkaline conditions. In contrast, CPH showed consistently higher solubility than CPI across all tested pH values. The solubility of CPH ranged from approximately 44.2% at pH 2.0 to 56.8% at pH 12.0, with only minor fluctuations, and no clear isoelectric precipitation was observed. The high solubility of CPH across the entire pH range may be attributed to its smaller peptide size and increased hydrophilicity following enzymatic hydrolysis.

Protein solubility of cricket protein isolate (CPI) and cricket protein hydrolysate (CPH) using alcalase combined with flavourzyme for 2~h as a function of pH (2--12).
Figure 1

Protein solubility of cricket protein isolate (CPI) and cricket protein hydrolysate (CPH) using alcalase combined with flavourzyme for 2 h as a function of pH (2–12).

Citation: Journal of Insects as Food and Feed 2026; 10.1163/23524588-bja10397

Foaming properties: CPH showed enhanced foaming capacity across all pH conditions when compared to CPI, as shown in Table 3 ( p < 0.05). The highest foam capacity of CPH was observed at pH 8 and pH 7, with values of 58.00 and 57.83%, respectively. These values were significantly higher than that of CPI at the same pH levels. Foam stability of CPH was also higher than CPI and remained relatively stable over time. At pH 7, CPH showed the highest stability, maintaining over 90% foam after 30, 60 and 90 min (93.65, 93.19 and 90.23%, respectively), with no significant decrease ( p > 0.05). Foam stability at pH 6 and 8 was also high, with values above 80% across all time points. Notably, foam stability remained consistent from 30 to 90 minutes, ranging from 85.27 to 84.36% at pH 6. These results indicate that CPH possesses superior foam-forming and foam-stabilizing abilities compared to CPI, particularly at neutral to slightly alkaline pH. This could be attributed to the presence of smaller peptides with increased surface activity and solubility resulting from enzymatic hydrolysis.

Foaming capacity (%) and foam stability (%) of CPI and cricket protein hydrolysate (CPH) prepared using combined enzymes, measured at different pH values and time intervals
Table 3

Foaming capacity (%) and foam stability (%) of CPI and cricket protein hydrolysate (CPH) prepared using combined enzymes, measured at different pH values and time intervals

Citation: Journal of Insects as Food and Feed 2026; 10.1163/23524588-bja10397

WBC, OBC and emulsifying properties: The functional properties of CPI and CPH, including water-binding capacity (WBC), oil-binding capacity (OBC), emulsifying activity index (EAI), and emulsion stability index (ESI), were evaluated at pH 6, 7 and 8 (Table 4). CPI showed significantly higher WBC values compared to CPH across all pH levels. The WBC of CPI increased from 3.41 g water/g sample at pH 6 to 4.93 g/g at pH 8, while CPH showed no significant differences in WBC across pH levels ( p > 0.05). Similarly, CPI exhibited higher OBC (5.5 g oil/g sample) compared to CPH ( p < 0.05). In terms of emulsifying properties, CPI had a higher EAI (52.45 m2/g) than CPH (31.67 m2/g). However, CPH showed a significantly higher ESI than that of CPI ( p < 0.05).

Water binding capacity (WBC) at various pH values, oil binding capacity (OBC), emulsifying activity index (EAI) and emulsion stability index (ESI) at pH 7 of crude protein isolate (CPI) and cricket protein hydrolysate (CPH) prepared using combined enzymes
Table 4

Water binding capacity (WBC) at various pH values, oil binding capacity (OBC), emulsifying activity index (EAI) and emulsion stability index (ESI) at pH 7 of crude protein isolate (CPI) and cricket protein hydrolysate (CPH) prepared using combined enzymes

Citation: Journal of Insects as Food and Feed 2026; 10.1163/23524588-bja10397

Total amino acid contents of CPI and CPH

Cricket powder, CPI, and CPH were analysed for their total amino acid contents. The combination of alcalase and flavourzyme hydrolysis for 2 h was selected for the preparation of cricket protein hydrolysate, as it exhibited potent DPPH radical scavenging activity (Table 4), with no statistically significant improvement observed with longer hydrolysis times (4 and 6 h) ( p > 0.05). The total amount of amino acids in whole cricket powder and CPI was 661.85 mg/g and 416.86 mg/g of sample, respectively (Table 5). Glutamic was the most abundant amino acid (58.6 mg/g), followed by aspartic acid (45 mg/g), alanine (27.7 mg/g%), and leucine (25 mg/g). Leucine was the most commonly found essential amino acid in whole cricket powder and CPI, 45.83 and 31.03 mg/g of sample, followed by lysine and valine. Depending on the source and type of protein, lysine is typically considered a limiting essential amino acid for protein synthesis in humans. Therefore, it is of critical nutritional/physiological significance. Among the non-essential amino acids, glutamic acid in whole cricket protein powder and CPI was 72.77 and 57.19 mg/g, respectively. Amount of aspartic acid in whole cricket powder and CPI was 62.03 and 47.79 mg/g, respectively. Arginine in whole cricket powder was abundant (Table 5).

Total amino acid profile of whole cricket powder, crude protein isolate (CPI) and cricket protein hydrolysate (CPH) prepared using combined enzymes
Table 5

Total amino acid profile of whole cricket powder, crude protein isolate (CPI) and cricket protein hydrolysate (CPH) prepared using combined enzymes

Citation: Journal of Insects as Food and Feed 2026; 10.1163/23524588-bja10397

Effect of temperature, pH and gastrointestinal enzyme on antioxidant activity of CPH

CPH derived from combined enzyme treatment for 2 h was selected for antioxidant activity analysis. The antioxidant capacity of CPH was evaluated through its DPPH radical scavenging, ABTS radical scavenging, and metal-chelating activities, as depicted in Figure 2. As shown in Figure 2a, CPH demonstrated a concentration-dependent DPPH radical scavenging activity. The scavenging percentage linearly increased with an escalation in CPH concentration. At a concentration of 0.05 mg/ml, the activity was approx. 7%, which progressively rose to about 85% at the highest tested concentration of 0.4 mg/ml. Similar to the DPPH assay, the ABTS radical scavenging activity of CPH also exhibited a positive correlation with its concentration (Figure 2b). The lowest concentration of 0.05 mg/ml showed an approximate scavenging activity of 1%, increasing steadily to about 12.5% at 0.4 mg/ml. The metal-chelating activity of CPH is presented in Figure 2c. A clear concentration-dependent increase was observed, with the activity ranging from approximately 2% at 0.05 mg/ml to around 14% at a concentration of 0.4 mg/ml. This indicates CPH’s capacity to chelate metal ions at varying concentrations.

Free radical scavenging activity based on 2,2-diphenyl-1-picrylhydrazyl (DPPH) (A) and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) (B) and Fe2\tsup{$+$} chelating capability (C) of cricket protein hydrolysate (CPH) using alcalase combined with flavourzyme for 2~h.
Figure 2

Free radical scavenging activity based on 2,2-diphenyl-1-picrylhydrazyl (DPPH) (A) and 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) (B) and Fe2+ chelating capability (C) of cricket protein hydrolysate (CPH) using alcalase combined with flavourzyme for 2 h.

Citation: Journal of Insects as Food and Feed 2026; 10.1163/23524588-bja10397

DPPH radical scavenging activity was studied to determine the stability of cricket protein hydrolysate, since DPPH is the most effective method for measuring antioxidant activity. Temperature effects (Figure 3a) were evaluated at 37–121 °C to simulate food heat treatment and compared to a control that was left at room temperature. The control sample exhibited an activity of approx. 52%. Exposure to temperatures of 37, 50 and 70 °C did not significantly alter the scavenging activity, with values remaining around 50–51%. According to these results, the DPPH radical scavenging activity slightly increased with temperature up to 100 °C and decreased at 121 °C ( p < 0.05). Likewise, the crude peptides produced in this study showed antioxidant stability in the acid condition with maximal activity at pH 2.0. A reduction of antioxidant activity was observed upon increasing pH which drastically decreased when the pH reached about 10 and slightly increased at pH 12 (Figure 3b). The stability of crude peptides exposed to a digestive enzyme, pepsin (PS) for 60 min, was evidenced by observation of similar results between the control and PS (Figure 3c). This indicated that pepsin did not digest antioxidant peptides and therefore they could remain active during digestion. This result is concomitant with the high antioxidant stability of these peptides under acid conditions rather than in an alkaline environment (Figure 3b).

Effect of temperature (a), pH (b), and \textit{in vitro} digestion (c) on 2,2-diphenyl-1-picrylhydrazyl (DPPH$\cdot $) scavenging activity of cricket protein hydrolysate upon pepsin (PS) and pancreatin (PC) treatment at 60--240~min. Different letters indicate significant differences ($p<0.05$).
Figure 3

Effect of temperature (a), pH (b), and in vitro digestion (c) on 2,2-diphenyl-1-picrylhydrazyl (DPPH⋅) scavenging activity of cricket protein hydrolysate upon pepsin (PS) and pancreatin (PC) treatment at 60–240 min. Different letters indicate significant differences ( p < 0.05).

Citation: Journal of Insects as Food and Feed 2026; 10.1163/23524588-bja10397

4 Discussion

The proximate analysis confirmed that the cricket powder used in this study is a rich protein source (Table 1). The crude protein content (approx. 72%) was comparable to that reported for Acheta domesticus by Brogan et al. (2021), but higher than the value (approx. 50%) reported for commercial domestic cricket powder (Hirsch et al., 2025). Such differences may be attributed to variations in processing methods (e.g. full-fat versus partially defatted powders), drying conditions, and farming practices. The samples in this study were processed under controlled laboratory conditions, which may have contributed to the relatively high protein recovery. It is recognized that proximate composition within the same species may vary depending on rearing diet, gut content at harvest, developmental stage, and environmental conditions. The crickets were obtained from a commercial producer; however, detailed information regarding feed formulation was not available. Therefore, the potential influence of diet on nutrient composition cannot be excluded and should be considered a limitation of this study.

Among edible cricket species, A. domesticus is widely cultivated in Thailand and commonly used for commercial cricket powder production due to its relatively higher protein and lower lipid content compared to other farmed species such as Gryllus bimaculatus (Udomsil et al., 2019). Since the objective of the present study was to evaluate cricket protein as a substrate for enzymatic hydrolysis, a species with a favourable protein-to-lipid ratio was intentionally selected to improve protein extraction efficiency and enzymatic accessibility. Future studies should further investigate interspecies variation and the influence of rearing diet on hydrolysate yield and bioactivity.

The protein quality of Acheta domesticus has been reported to be comparable to that of conventional animal and plant protein sources. This species typically contains 60–77% crude protein on a dry matter basis, which exceeds most plant proteins such as soybean (approx. 35–40% on a dry matter basis) and is comparable to animal-derived proteins, including beef, egg, and milk, when expressed on a dry weight basis (Rumpold and Schlüter, 2013; Yi et al., 2013). Furthermore, its essential amino acid profile is well balanced and has been shown to be comparable to those of casein and soy protein isolates (Payne et al., 2016). These findings are consistent with the protein levels observed in the present study and further support the potential of A. domesticus as a high-quality alternative protein source.

Solubility variation as a function of pH is useful for developing strategies to purify protein from crickets. CPI behaves favorably at pH 12 (Fig. 1). This is consistent with the general behaviour of insect proteins, which exhibit low solubility near their isoelectric point (pI), typically between pH 4.5 and 5.5. These findings suggest that CPI is poorly soluble under acidic conditions but can be selectively solubilized under alkaline conditions. This characteristic enables the use of an alkaline solubilization–acid precipitation technique to obtain a purified cricket protein concentrate with reduced non-protein impurities

At pH values far from the pI, solubility increases due to greater electrostatic repulsion and protein unfolding (Hall et al., 2017; Yi et al., 2013). These findings align with Brogan et al. (2021), reported that nearly 70 % of protein from cricket, locust, and silkworm pupae powders dissolved under alkaline conditions (pH 9–11), while solubility dropped to just 7–15% in the acidic range (pH 4–6), highlighting the clear pH-dependent solubility behaviour of insect proteins. Based on the solubility profiles, alkaline solubilization followed by isoelectric precipitation appears to be the most suitable technique for protein isolation in this study. This method not only increases protein yield and purity but also facilitates the removal of non-protein components such as fat and chitin. Consistent with a previous report by Hall et al. (2017), which demonstrated the lowest solubility of tropical banded cricket (G. sigillatus) proteins around pH 3–4.

The foaming properties of both CPI and CPH were strongly influenced by pH and were closely related to their solubility profiles. CPH exhibited significantly higher foaming capacity and foam stability than CPI across all tested pH values, particularly at pH 7 and 8. This superior foaming performance of CPH may be attributed to its higher solubility over the entire pH range, as observed in Figure 1. The enhanced solubility of CPH, resulting from enzymatic hydrolysis, likely led to an increased concentration of surface-active peptides in solution, which facilitated more rapid adsorption at the air–water interface and improved foam formation (Stone et al., 2019). In contrast, CPI displayed lower foaming capacity and reduced stability, particularly near its isoelectric point (pH 4–5), where solubility was minimal. Poor solubility at this pH range reduces the availability of protein molecules in solution, thus limiting their ability to migrate and stabilize interfaces. Although CPI showed improved foam formation at pH 8, its performance remained inferior to that of CPH, possibly due to the larger molecular size and lower mobility of intact protein structures, which may hinder effective interfacial alignment and film formation. Therefore, enzymatic hydrolysis not only improves protein solubility but also contributes to functional enhancements such as foaming, which is desirable in various food applications.

Water and oil holding abilities are important in many food applications for mouthfeel, texture, palatability, and ingredient binding, among other attributes. Adebowale et al. (2005) reported the water absorption capacities of large African crickets (Gryllidae sp.) was 2.38 g/g sample. Our results showed higher water binding capacity (WBC) than previously reported. This might be due to different chemical compositions of the protein preparations (Table 2). Isolation of protein by alkaline precipitation could eliminate impurities, resulting in higher protein concentrations. Materials with higher protein contents could absorb/bind more water. CPI could bind oil indicating hydrophobicity governed by amino acid composition. The difference might be due to extraction and isolation methods resulting in higher protein purity. Zhao et al. (2016) reported cricket protein extracts have higher WHC and OHC than their respective flours. This indicates that CPI could bind with hydrophobic molecules, especially flavor ingredients in oil-based food matrices, e.g. food emulsions. The observed decrease in water and oil binding capacities of the CPH, alongside improved foaming capacity and stability, aligns well with the known structure–function relationships of protein hydrolysates. Enzymatic hydrolysis generally reduces molecular size and disrupts native protein structure, which limits the ability of peptides to retain water or oil. However, the smaller peptides exhibit enhanced surface activity and diffusion rates, contributing to better foam formation and stability (Wouters et al., 2016).

CPI demonstrated stronger emulsifying activity due to the surface-active nature of its intact protein molecules, which are able to migrate to the oil–water interface, unfold, and effectively stabilize emulsions. The amphiphilic characteristics of these proteins, characterized by the presence of both hydrophilic and hydrophobic regions, enable them to align at the interface and lower interfacial tension. This process leads to the formation of a viscoelastic film that supports the stability of emulsion droplets (Liang and Tang, 2013). In contrast, although CPH exhibited lower initial emulsifying activity, it provided enhanced emulsion stability over time. This improved stability can be attributed to the rapid diffusion and structural rearrangement of smaller peptide fragments at the interface. These peptides can form a compact and cohesive interfacial layer, which contributes to greater resistance against coalescence and phase separation during storage. This behavior is commonly observed in peptides that are both highly soluble and structurally flexible, allowing for dynamic adaptation at the interface (Padial-Domı́nguez et al., 2020). Therefore, selecting between native and hydrolysed proteins should be based on the specific functional requirements of the product, such as the need for rapid foaming and emulsification or for enhanced stability during storage.

Whole cricket powder contains 661.85 mg/g (approximately 66.2%) of total amino acid (Table 5), which is lower than the protein content of cricket powder (71.69%, Table 1) since the protein contents in Table 1 were analysed using the Kjeldahl method, which determined the total nitrogen (TN) of sample. Therefore, nitrogen in chitin was included in these results. Thus, the protein content was higher than the total amino acid level. Total amino acid content of CPI and CPH was 416.86 and 342.60 mg/g (Table 5), since some amino acids were oxidized during sample preparation by acid and high temperature. The amino acid composition of cricket powder, CPI and CPH revealed marked differences associated with the protein extraction and hydrolysis processes. Cricket powder exhibited the highest total amino acid content, reflecting its unprocessed and complete matrix that includes both soluble and insoluble protein fractions. In contrast, CPI and CPH showed significantly lower total amino acid levels. This reduction is likely due to selective loss of certain protein fractions during the alkaline extraction and isoelectric precipitation steps, which may exclude insoluble structural proteins, such as cuticular or muscle-associated proteins, from the final isolate. Additionally, peptides and amino acids that are highly soluble or of low molecular weight may be lost during washing or centrifugation. The further decrease in amino acid content in CPH relative to CPI suggests that enzymatic hydrolysis may contribute to the degradation or loss of free amino acids and small peptides during processing or sample cleanup. This is consistent with previous studies showing that some amino acids may be unstable or lost during proteolysis, filtration, or post-hydrolysis treatment (Padial-Domı́nguez et al., 2020). Despite the reduction in total content, the amino acid profile of CPI and CPH still retains essential amino acids, though in lower concentrations, which supports their continued nutritional relevance in functional food applications.

The comparable DPPH radical scavenging ability was observed in samples digested with either alcalase or flavourzyme although the DH was slightly different. This suggested that different DHs might not govern the antioxidant activity of the peptides. Additionally, different digestive enzymes provide various peptide fragments with distinct amino acid composition, governing antioxidant activity (Liu et al., 2022). In this study, peptides derived from an enzyme combination (alcalase and flavourzyme) were more effective than those digested by single enzymes (alcalase or flavourzyme). An increased activity was partly explained by the different DHs since the enzyme combination produced shorter peptides. This indicated that low molecular peptides facilitate free radical scavenging to a greater extent than high molecular weight peptides. Peptides with lower molecular weights are more effective in hindering free radical reactions (Fan et al., 2012). A non-hydrolysed control was included in the DPPH assay to establish the baseline antioxidant activity of the unprocessed sample. The untreated sample demonstrated 28% radical scavenging activity, whereas the enzymatic hydrolysates exhibited significantly higher values, ranging from 35 to 41% (Table 2). This marked increase following hydrolysis suggests that the generation of bioactive peptides was a primary contributor to the enhanced antioxidant activity. Although the potential contribution of other endogenous or feed-derived compounds cannot be entirely excluded, the relative increase observed in comparison to the non-hydrolysed control indicates that protein hydrolysis was the principal factor responsible for the improved DPPH radical scavenging activity.

In this study, the DPPH radical scavenging activity of CPI heated to 100 °C was slightly increased to 55% and decreased to 52% at 121 °C. Heating can cause the hydrogen bonds between a peptide’s side chains and the water molecule to break, exposing the reactive side chains and allowing free radicals to bind. Furthermore, while short-chain and low-molecular-weight peptides lack tertiary/quaternary structures, they can still create secondary structures (Du et al., 2020; Zhu et al., 2014). The highest DPPH activity was found when those crude peptides were incubated at 100 °C followed by 121 °C (Figure 3a). Heating at 100 °C slightly enhanced the antioxidant activity of the protein hydrolysate, likely due to increased release of low-molecular-weight peptides. However, further heating at 121 °C caused a modest decline, consistent with previous findings that high temperatures can induce oxidation or aggregation of antioxidant peptides, thereby reducing their radical-scavenging capacity (Fashakin et al., 2023; López-Sánchez et al., 2016; Mirzaei et al., 2020; Singh et al., 2018).

Stability of crude peptides at different pH values (Figure 3b), the maximum activity was found at the pH value of 2.0. It has been hypothesized that more protons are attracted to carbonyl oxygen with increased solution acidity, resulting in more positive charges. Thus, this positive charge is partially delocalized onto carbonyl carbon, which becomes more electron-deficient and susceptible to attack by nucleophiles (Sun et al., 2019). Zhu et al. (2014) reported that exposure of amino acids to extremely alkaline conditions causes racemization and deamination, resulting in a reduction of antioxidant activity. A similar phenomenon was reported for peptides purified from fermented fish (Chaijan et al., 2021). This suggested that our crude peptides are suitable for using in acidic food products rather than in low-acid foods. This pH-dependent activity is a common phenomenon for many natural antioxidants, particularly those with ionizable groups (e.g. carboxyl, amino, hydroxyl groups). The protonation state of these functional groups is crucial for their ability to donate hydrogen atoms or electrons to neutralize free radicals or chelate metal ions. Under acidic conditions, these groups may be in a more favourable protonated or deprotonated state for radical scavenging, while alkaline conditions can lead to their deprotonation, altering their redox potential or rendering them less effective (Yi et al., 2013).

Moreover, high stability under acidic conditions would favour peptide stability in the digestive tract (Figure 3c). The result of digestive enzyme stability tests showed the highest stability under pepsin (PS) digestion. Similar stability of antioxidant peptides from semi-dry fermented catfish under acidic conditions was reported (Chaijan et al., 2021b). A reduced antioxidant activity of these crude peptides was observed when pancreatic enzymes (PC) were incorporated into the digestion system. These crude peptides might be partly digested in the intestine and lose their ability to scavenge the DPPH radicals. Peptides derived from dry-cured ham exhibited diminished capacity to scavenge DPPH radicals when subjected to simulated digestion by gastrointestinal system enzymes (Gallego et al., 2023). However, a rate reduction did not progress with increased digestion time. This suggests that antioxidant activity was maintained. The present study aimed to comprehensively evaluate the antioxidant activity of CPH and its stability under various environmental and processing conditions. Our findings provide valuable insights into the potential applicability and limitations of CPH as a natural antioxidant.

5 Conclusions

This study demonstrates the potential of cricket protein isolate (CPI) and its hydrolysates (CPH) as functional and antioxidant-rich ingredients for food applications. CPI exhibited favourable water and oil binding capacities and emulsifying properties due to its intact protein structure, while CPH showed enhanced solubility, foaming ability, and emulsion stability as a result of enzymatic hydrolysis. Sequential hydrolysis using alcalase and flavourzyme improved the degree of hydrolysis and produced peptides with significant DPPH radical scavenging activity. These antioxidant peptides remained thermally stable and retained activity under acidic conditions and simulated gastric digestion, suggesting their suitability for incorporation into heat-processed or low-pH food systems. However, antioxidant activity declined under highly alkaline conditions or with pancreatic digestion, highlighting the need for targeted formulation strategies. This study demonstrates the potential of crickets as a sustainable source of both high-quality protein and bioactive peptides. The derived hydrolysates exhibit notable functional properties and biological activities, highlighting their applicability in the development of functional foods, nutraceuticals, and other value-added products.

*

Corresponding author; e-mail: natteewan.udo@mahidol.ac.th

#

The authors are equal contributors to this work and designated as co-first authors.

Acknowledgements

This research project was funded by Mahidol University (Fundamental Fund: fiscal year 2024 by National Science Research and Innovation Fund (NSRF)) [FF-146/2567] and was partially supported by the National Research Council of Thailand (NRCT) [Grant No. NRCT.MHESI.A208/2021].

Author contributions

Bung-Orn Hemung: Writing (original draft, review and editing), formal analysis, visualization. Sumeth Imsoonthornruksa: Writing (review and editing), software, data analysis. Ratasark Summart: Writing (review and editing), data analysis. Mariena Ketudat-Cairns: Writing (review and editing), supervision, resources. Natteewan Udomsil: Writing (original draft, review and editing), funding acquisition, conceptualization, methodology, validation, supervision.

Conflict of interest

The authors declared that they have no conflicts of interest in this work. We declare that we do not have any commercial or associative interest that represents a conflict of interest in connection with the submitted manuscript.

Data availability

The data that support this study are available from the corresponding author upon reasonable request.

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Titel:
Physicochemical properties of house cricket (Acheta domesticus) protein and antioxidant stability of its enzymatic hydrolysate under pH, temperature and in vitro digestion
Artikelkategorie:
Research Article
DOI:
https://doi.org/10.1163/23524588-bja10397
Sprache:
Englisch
Seiten:
1–15
Keywords:
antioxidant stability; cricket hydrolysate; emulsifying; foaming; in vitro digestion; protein solubility
Quelltitel:
Journal of Insects as Food and Feed
Band/Ausgabe:
Artikelvorabzugriff
Received:
21 Nov 2025
Accepted:
10 Mar 2026
Verleger:
Wageningen Academic
eISSN:
2352-4588
Fachgebiete:
Allgemein, Biowissenschaften, Ernährung und Gesundheit, Tiere und Veterinärmedizin, Entomologie, Biologie

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