Characterisation of black soldier fly larva protein before and after conjugation by the Maillard reaction
In: Journal of Insects as Food and Feed
Authors:
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,
, and
B. Zozo
https://orcid.org/0000-0001-5707-8042
B. Zozo
Department of Chemistry, Cape Peninsula University of Technology, Bellville, 7535, South Africa.
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M.M. Wicht
https://orcid.org/0000-0003-3344-6933
M.M. Wicht
Department of Chemistry, Cape Peninsula University of Technology, Bellville, 7535, South Africa.
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V.V. Mshayisa
https://orcid.org/0000-0002-1946-859X
V.V. Mshayisa
Department of Food Science and Technology, Cape Peninsula University of Technology, Bellville, 7535, South Africa.
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J. van Wyk
https://orcid.org/0000-0003-1885-0321
J. van Wyk
Department of Food Science and Technology, Cape Peninsula University of Technology, Bellville, 7535, South Africa.
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Black soldier fly has been proposed as an alternative protein source sustainable for both food and feed due to its nutritional composition. The functional properties of this protein can be improved by inducing the Maillard reaction (MR) in protein-sugar mixtures. This study focused on the conjugation and characterisation of black soldier fly larvae (BSFL) proteins and conjugates. The defatted BSFL larvae were subjected to protein extraction at an alkaline pH. The protein extract was then conjugated with glucose. The BSFL protein and glucose were mixed at (2:1 w/w, pH 9), incubated at 50, 70, and 90 °C for 30, 60, 90 and 120 min. The products obtained were then characterised and compared. The changes were confirmed by universal attenuated total reflectance Fourier-transform infrared spectroscopy (UATR-FTIR), scanning electron microscopy, thermal gravimetric analysis and differential scanning calorimetry. UATR-FTIR combined with principal component analysis monitored the protein-sugar conjugates, to show the structural difference among heated proteins and conjugates. The heating treatments resulted in the unfolding and reduction of the protein molecule aggregation. The protein extract from the larvae was rich in protein content (67±0.78%) and displayed good essential amino acids (EAA) in sufficient quantities to meet the dietary requirements for humans. The EAA quantities of the conjugates decreased due to the MR treatment. The conjugates showed a significant decrease in the lysine content as a function of reaction temperature and time at 90 °C and 120 min, respectively. FTIR indicated that the amide I and II bands of the protein were altered by the MR. The increased Tmax (the temperature at which decomposition is completed) demonstrated that the conjugation of the protein with glucose improved the thermal stability, remarkably. These results suggested that MR with glucose can be a promising way to improve the thermal properties of BSFL protein.
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Characterisation of black soldier fly larva protein before and after conjugation by the Maillard reaction
In: Journal of Insects as Food and Feed
Authors:
,
,
, and
B. Zozo
https://orcid.org/0000-0001-5707-8042
B. Zozo
Department of Chemistry, Cape Peninsula University of Technology, Bellville, 7535, South Africa.
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M.M. Wicht
https://orcid.org/0000-0003-3344-6933
M.M. Wicht
Department of Chemistry, Cape Peninsula University of Technology, Bellville, 7535, South Africa.
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V.V. Mshayisa
https://orcid.org/0000-0002-1946-859X
V.V. Mshayisa
Department of Food Science and Technology, Cape Peninsula University of Technology, Bellville, 7535, South Africa.
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J. van Wyk
https://orcid.org/0000-0003-1885-0321
J. van Wyk
Department of Food Science and Technology, Cape Peninsula University of Technology, Bellville, 7535, South Africa.
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Black soldier fly has been proposed as an alternative protein source sustainable for both food and feed due to its nutritional composition. The functional properties of this protein can be improved by inducing the Maillard reaction (MR) in protein-sugar mixtures. This study focused on the conjugation and characterisation of black soldier fly larvae (BSFL) proteins and conjugates. The defatted BSFL larvae were subjected to protein extraction at an alkaline pH. The protein extract was then conjugated with glucose. The BSFL protein and glucose were mixed at (2:1 w/w, pH 9), incubated at 50, 70, and 90 °C for 30, 60, 90 and 120 min. The products obtained were then characterised and compared. The changes were confirmed by universal attenuated total reflectance Fourier-transform infrared spectroscopy (UATR-FTIR), scanning electron microscopy, thermal gravimetric analysis and differential scanning calorimetry. UATR-FTIR combined with principal component analysis monitored the protein-sugar conjugates, to show the structural difference among heated proteins and conjugates. The heating treatments resulted in the unfolding and reduction of the protein molecule aggregation. The protein extract from the larvae was rich in protein content (67±0.78%) and displayed good essential amino acids (EAA) in sufficient quantities to meet the dietary requirements for humans. The EAA quantities of the conjugates decreased due to the MR treatment. The conjugates showed a significant decrease in the lysine content as a function of reaction temperature and time at 90 °C and 120 min, respectively. FTIR indicated that the amide I and II bands of the protein were altered by the MR. The increased Tmax (the temperature at which decomposition is completed) demonstrated that the conjugation of the protein with glucose improved the thermal stability, remarkably. These results suggested that MR with glucose can be a promising way to improve the thermal properties of BSFL protein.
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