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Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update.

ABSTRACT: Diabetes, a glucose metabolic disorder, is considered one of the biggest challenges associated with a complex complication of health crises in the modern lifestyle. Inhibition or reduction of the dipeptidyl peptidase IV (DPP-IV), alpha-glucosidase, and protein-tyrosine phosphatase 1B (PTP-1B) enzyme activities or expressions are notably considered as the promising therapeutic strategies for the management of type 2 diabetes (T2D). Various food protein-derived antidiabetic bioactive peptides have been isolated and verified. This review provides an overview of the DPP-IV, PTP-1B, and α-glucosidase inhibitors, and updates on the methods for the discovery of DPP-IV inhibitory peptides released from food-protein hydrolysate. The finding of novel bioactive peptides involves studies about the strategy of separation fractionation, the identification of peptide sequences, and the evaluation of peptide characteristics in vitro, in silico, in situ, and in vivo. The potential of bioactive peptides suggests useful applications in the prevention and management of diabetes. Furthermore, evidence of clinical studies is necessary for the validation of these peptides' efficiencies before commercial applications.

SUBMITTER: Nong NTP

PROVIDER: S-EPMC8431147 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:The demand for healthy food items with a high nutrient value of bioavailability and bioaccessibility has created a need for continuous development of technology and food ingredients like bioactive peptides. This study aimed to investigate seven proteolytic lactic acid bacteria (PLABs) isolated from the plaa-som (fermented fish) sample originated from silver BARB species for production of proteolytic enzymes. Proteolytic enzymes produced by (PLABs) were used further to create potent bioactive peptides by hydrolyzing proteins throughout PLAB-probiotics enhancer. Protein derived-bioactive peptides was tested the proteolytic activity on different protein sources and examined bioactivities including antioxidative and antimicrobial effect for further use in functional foods. Results of screened-PLAB strains showed high proteolytic activity namely Streptococcus thermophilus strains (KKUPA22 and KKUPK13). These strains have proteolytic system consisting of extracellular and cell-bound enzymes that used for degrading protein in fish flesh protein (FFP) and skim milk (SKM) broth media. Proteolytic activity of tested bacterial enzymes was estimated after incubation at 45, 37, and 50 °C. Furthermore, FFP hydrolysates were formed with various peptides and has small molecular weights (checked by SDS-PAGE) in the range of10.5 to 22 kDa), exhibiting strong activity. Data revealed that S. thermophilus strains (KKUPA22 and KKUPK13) had high antioxidant activity in term of 2,2-diphenyl-1-picrylhydrazyl (DPPH), 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS) radical-scavenging inhibition, and ferric reducing antioxidant power (FRAP) reducing power capacity. Both strains (KKUPA22 and KKUPK13) of S. thermophilus have higher antimicrobial activity against Gram-negative bacteria than against Gram-positive bacteria. We have confirmed presence of proteolytic (prt) gene regions in S. thermophilus strains using specific primers via PCR amplification. Results showed highest homology (100%) with the prtS gene of S. thermophillus located on the cell envelope proteolytic enzymes (CEPEs) such as serine proteinase. Therefore, it concluded that the proteolytic system of tested PLAB strains able to generate bioactive peptides-derived proteins having active biological property, good mechanism of degradability, and bioaccessibility for further use in catalyzing protein of functional foods.

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Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update.

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