Structural properties of native and conjugated black soldier fly (Hermetia illucens) larvae protein via Maillard reaction and classification by SIMCA

Abstract

Black soldier fly (Hermetia illucens) has received considerable interest as an alternative protein source. Aqueous solutions of black soldier fly larvae (BSFL) protein and glucose (2:1 w.w À1 , pH 9) were heated at 50, 70 and 90 C, for 2-10 h at 2 h intervals, respectively. The zeta-potential (ζ) of BSFL-Glu conjugates heat-treated at 70 C ranged from -10.25 to -25.25 mV while the native BSFL protein ranged from -12.84 to -16.70 mV. The ζ-potential analysis revealed that the glycation reaction modified the surface charge density of the BSFL protein as a function of reaction time and temperature. In addition, an increase in thermal stability of the BSFL-Glu conjugates was observed by means of Thermo-gravimetric analysis (TGA) and differential scanning calorimetry (DSC). Fourier transform infrared spectroscopy (FT-IR) analysis indicated that the most apparent structural changes in the BSFL protein were in the amide I and amide II region. Well-separated clusters permitting differentiation between native BSFL and BSFL-Glu conjugates were observed by using principal component analysis (PCA) on FT-IR spectra. At 50, 70 and 90 C the first two principal components (PC1 and PC2) showed an accumulated total variance of 91, 96 and 95%, respectively. A classification efficiency of 91% was obtained when using soft independent modelling of class analogy (SIMCA). Infrared spectroscopy combined with SIMCA is a powerful tool to monitor the formation of edible insect protein-sugar conjugates by Maillard reaction. As a result, combining FT-IR spectroscopy with multivariate techniques (PCA and SIMCA) exhibited a strong potential to differentiate between native and glycated protein samples from black soldier fly larvae.

Pamuk Çeki̇rdeği̇ Protei̇n Konsantresi̇ni̇n Karakteri̇sti̇k Özelli̇kleri̇ni̇n Beli̇rlenmesi̇

“…A mass loss of approximately 83% was reported in this phase. Thermal changes occurring in this range may be associated with the degradation or decomposition of polypeptide chains in the protein (Mshayisa et al, 2021). Similar curves for plant-based proteins were noted in previous studies (Yu et al, 2015;Timilsena et al, 2016;Başyiğit et al, 2022a;Başyiğit et al, 2022b).…”

Nutritional, Techno-Functional and Structural Properties of Black Soldier Fly (Hermetia illucens) Larvae Flours and Protein Concentrates

“…The ζ-Potential of the protein concentrates (BSFL-PC1 and BSFL-PC2) were determined using a Zetasizer Nano Series (Malvern Instruments, Malvern, Worcestershire, UK) as described by Ladjal-Ettoumi et al [ 25 ] and Mshayisa et al [ 26 ], respectively. The protein powders were diluted to 1% ( w / v ) with Milli-Q water.…”

“…The edible insect powders were placed onto double-sided carbon adhesive tape attached to the specimen stubs, respectively. The sample’s surface structure was observed at 320× magnification and in the secondary electron mode at 15.0 kV following the procedure described by Mshayisa et al [ 26 ].…”

“…All flour and protein concentrate samples were analysed using a Perkin Elmer Fourier transform infrared spectroscope (FT-IR) equipped with a universal attenuated total reflectance (UATR) polarisation accessory for spectra as described by Mshayisa et al [ 26 ]. A background spectrum was collected prior to data collection of each sample, and then the sample powders obtained by grinding in a mortar were placed directly, covering the surface of the ATR crystal.…”

Enhancing Zinc Uptake through Dual-Modification of Cicer arietinum Protein

“…Te onset temperature of NCP-Zn is recorded at 53.27 °C which signifes the initiation of thermal degradation or decomposition in the protein. Te unfolding of the protein's native structure is induced by the application of heat, leading to disruptions that afect its solubility and functional properties [95]. In addition, the peak temperature of decomposition is observed at 294.51 °C.…”