Identification and characterization of novel α-amylase and α-glucosidase inhibitory peptides from camel whey proteins

Abstract

This study explores the inhibitory properties of camel whey protein hydrolysates (CWPH) toward α-amylase (AAM) and α-glucosidase (AG). A general full factorial design (3 × 3) was applied to study the effect of temperature (30, 37, and 45°C), time (120, 240, and 360 min), and enzyme (pepsin) concentration (E%; 0.5, 1, and 2%). The results showed that maximum degree of hydrolysis was obtained when hydrolysis was carried out at higher temperature (45°C; P < 0.05), compared with lower temperatures of 30 and 37°C. Electrophoretic pattern displays degradation of all protein bands upon hydrolysis by pepsin at various hydrolysis conditions applied. All the 27 CWPH generated showed significant AAM and AG inhibitory potential as indicated by their lower IC 50 values (mg/mL) compared with intact whey proteins. In total 196 peptides were identified from selected hydrolysates and 15 potential peptides (PepSite score > 0.8; http: / / pepsite2 .russelllab .org/ ) were explored via in silico approach. Novel peptides PAGNFLMNGLMHR, PAVACCLPPLPCHM, ML-PLMLPFTMGY, and PAGNFLPPVAAAPVM were identified as potential inhibitors for both AAM and AG due to their high number of binding sites and highest binding probability toward the target enzymes. CCGM and MFE, as well as FCCLGPVPP were identified as AG and AAM inhibitory peptides, respectively. This is the first study that reports novel AG and AAM inhibitory peptides from camel whey proteins. The future direction for this research involves synthesis of these potential AG and AAM inhibitory peptides in a pure form and investigate their antidiabetic properties in the in vitro, as well as in vivo models. Thus, CWPH can be considered for potential applications in glycaemic regulation.

Camel and bovine milk lactoferrins activate insulin receptor and its related AKT and ERK1/2 pathways

“…However, such a beneficial action of CM in diabetes remained for a long time elusive at the molecular and cellular levels because the antidiabetic agent or agents and the molecular mechanisms involved have not been appropriately studied or fully dissected. Recent studies have investigated this aspect, revealing interesting CM whey proteins and their derived hydrolysates and peptides with bioactivity against different components of glucose homeostasis and insulin and glucagon-like peptide-1 (GLP-1) secretion pathways, including insulin and insulin receptors (IR), α-amylase, α-glucosidase, and dipeptidyl peptidase IV (DPP-IV; Abdulrahman et al, 2016;Mudgil et al, 2018;Nongonierma et al, 2018Nongonierma et al, , 2019Ashraf et al, 2021;Baba et al, 2021;. Indeed, crude hydrolysates obtained from in vitro hydrolysis of raw CM whey proteins with various proteases have been shown to inhibit DPP-IV, which is responsible for GLP-1 degradation and, thereby, the decrease of insulin secretion by the β pancreatic cells.…”

Conjoint application of ultrasonication and redox pair mediated free radical method enhances the functional and bioactive properties of camel whey-quercetin conjugates

“…Freeze dried camel whey was produced in the laboratory of Dept. of Food Science, United Arab Emirates University (UAEU) as per the method described by Baba et al [7] . A 20% solution of freeze-dried whey was subjected to dialysis using a dialysis tubing (SnakeSkin®, Thermo Fisher Scientific) with 3.5 KDa molecular weight cut off (MWCO) for 48 h at 4 °C to remove salts and lactose followed by freeze drying.…”

“…The AGI inhibition activity of conjugates was determined according to the method described by Baba et al [7] with slight modifications. Briefly, 50 μL of each sample (5 μg/mL) was mixed with 100 μL of enzyme (0.2 U/mL) in 50 μL of Hepes buffer (0.1 M, pH = 6.8).…”

“…Recently, production of modified whey-polyphenol conjugates with enhanced techno-functional as well as bioactive properties is generating high research interest and has been identified as the hotspot in the field of food science [13] . Moreover, recent research on whey proteins from camel milk is gaining considerable importance in today’s world due to its therapeutic properties [3] , [6] , [7] . Camel whey has been reported for their high techno-functional potential that warrants its use in food industry [32] , [33] , [68] .…”

Cow and camel milk-derived whey and casein protein hydrolysates demonstrated effective antifungal properties against selected Candida species

“…The curd obtained was allowed to settle for 1 h at 4°C and separation of casein (as a pellet) and whey fraction (supernatant) was performed at 10,000 × g, 15 min at 4°C. For the separation of caseins and whey proteins from camel milk, a slightly modified method described by Baba et al (2021) and was followed. Both fractions (casein and whey) thus obtained were frozen at −20°C and freeze-dried (temperature = −80°C, pressure = 0.1 bar) using a Telstar freeze-drier (Telstar), and finally stored at −20°C until further utilization.…”