» Articles » PMID: 32121110

Anti-Hyperglycemic Effects of Green Crab Hydrolysates Derived by Commercially Available Enzymes

Overview
Journal Foods
Specialty Biotechnology
Date 2020 Mar 4
PMID 32121110
Citations 4
Authors
Affiliations
Soon will be listed here.
Abstract

The predation and burrowing activity of invasive green crabs have had detrimental effects on important marine resources and habitats. Our objective is to develop bioactive hydrolysates by enzymatic proteolysis of underutilized green crab. Mechanically separated mince was hydrolyzed with Alcalase, Protamex, Flavourzyme, and Papain (1%) for 60 min. Subsequently, the hydrolysates were introduced to a simulated gastrointestinal digestion model. Selected samples were fractionated by ultrafiltration, and their anti-hyperglycemic effects including α-glucosidase, α-amylase, and dipeptidyl peptidase-IV (DPP-IV) inhibitory activities and glucagon-like 1 (GLP-1) secretory activity were evaluated. The Protamex treatment showed the highest α-glucosidase inhibitory activity (IC 1.38 ± 0.19 mg/mL) compared to other enzyme treatments and the crab mince control, and its α-amylase inhibitory activity (IC 11.02 ± 0.69 mg/mL) was lower than its α-glucosidase inhibitory activity. Its GLP-1 secretory activity was approximately four times higher than the positive control (10 mM glutamine). The <3 kD fraction contributed significantly to the anti-hyperglycemic activity of Protamex-derived hydrolysates, and this activity was stable after simulated digestion. Our results suggest that green crab hydrolysates obtained by Protamex treatment have the potential for type 2 diabetes management and could be incorporated in food products as a health-promoting ingredient.

Citing Articles

Integration of Deep Learning and Sequential Metabolism to Rapidly Screen Dipeptidyl Peptidase (DPP)-IV Inhibitors from .

Liu H, Yu S, Li X, Wang X, Qi D, Pan F Molecules. 2023; 28(21).

PMID: 37959800 PMC: 10649927. DOI: 10.3390/molecules28217381.


Hatched Eggshell Membrane Can Be a Novel Source of Antioxidant Hydrolysates to Protect against HO-Induced Oxidative Stress in Human Chondrocytes.

Zhu L, Ma M, Ahn D, Guyonnet V, Wang L, Zheng Y Antioxidants (Basel). 2022; 11(12).

PMID: 36552636 PMC: 9774709. DOI: 10.3390/antiox11122428.


Preparation, Characterization, and Mechanism of Antifreeze Peptides from Defatted Antarctic Krill () on .

Liu Y, Yu X, Zhu Y, Yang W, Zeng Y, Hu Y Molecules. 2022; 27(9).

PMID: 35566118 PMC: 9104330. DOI: 10.3390/molecules27092771.


Introduction to the Special Issue: "Advance in Recovery and Application of Bioactive Compounds from Seafood".

Jacobsen C, Holdt S Foods. 2021; 10(2).

PMID: 33525691 PMC: 7912078. DOI: 10.3390/foods10020266.

References
1.
Matsui T, Oki T, Osajima Y . Isolation and identification of peptidic alpha-glucosidase inhibitors derived from sardine muscle hydrolyzate. Z Naturforsch C J Biosci. 1999; 54(3-4):259-63. DOI: 10.1515/znc-1999-3-417. View

2.
Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

3.
Deacon C, Nauck M, Pridal L, Willms B, Holst J . Both subcutaneously and intravenously administered glucagon-like peptide I are rapidly degraded from the NH2-terminus in type II diabetic patients and in healthy subjects. Diabetes. 1995; 44(9):1126-31. DOI: 10.2337/diab.44.9.1126. View

4.
Reimann F, Williams L, da Silva Xavier G, Rutter G, Gribble F . Glutamine potently stimulates glucagon-like peptide-1 secretion from GLUTag cells. Diabetologia. 2004; 47(9):1592-601. DOI: 10.1007/s00125-004-1498-0. View

5.
Hildebrandt M, REUTTER W, Arck P, Rose M, Klapp B . A guardian angel: the involvement of dipeptidyl peptidase IV in psychoneuroendocrine function, nutrition and immune defence. Clin Sci (Lond). 2000; 99(2):93-104. View