In vitro inhibition of glucose gastro-intestinal enzymes and antioxidant activity of hydrolyzed collagen peptides from different species.

Autor: Gaspardi ALA; Centro de Ciência e Qualidade de Alimentos (CCQA), Instituto de Tecnologia de Alimentos (ITAL), Campinas, Brazil., da Silva DC; Centro de Ciência e Qualidade de Alimentos (CCQA), Instituto de Tecnologia de Alimentos (ITAL), Campinas, Brazil., Ponte LGS; Laboratório Multidisciplinar em Alimentos e Saúde (LABMAS), Faculdade de Ciências Aplicadas (FCA), Universidade de Campinas (UNICAMP), Limeira, Brazil., Galland F; Centro de Ciência e Qualidade de Alimentos (CCQA), Instituto de Tecnologia de Alimentos (ITAL), Campinas, Brazil., da Silva VSN; Centro de Ciência e Qualidade de Alimentos (CCQA), Instituto de Tecnologia de Alimentos (ITAL), Campinas, Brazil., Simabuco FM; Laboratório Multidisciplinar em Alimentos e Saúde (LABMAS), Faculdade de Ciências Aplicadas (FCA), Universidade de Campinas (UNICAMP), Limeira, Brazil., Bezerra RMN; Laboratório Multidisciplinar em Alimentos e Saúde (LABMAS), Faculdade de Ciências Aplicadas (FCA), Universidade de Campinas (UNICAMP), Limeira, Brazil., Pacheco MTB; Centro de Ciência e Qualidade de Alimentos (CCQA), Instituto de Tecnologia de Alimentos (ITAL), Campinas, Brazil.
Jazyk: angličtina
Zdroj: Journal of food biochemistry [J Food Biochem] 2022 Dec; Vol. 46 (12), pp. e14383. Date of Electronic Publication: 2022 Oct 01.
DOI: 10.1111/jfbc.14383
Abstrakt: The growing value of industrial collagen by-products has given rise to interest in extracting them from different species of animals. Intrinsic protein structure variation of collagen sources and its hydrolysis can bring about different bioactivities. This study aimed to characterize and evaluate the differences in vitro biological potential of commercial bovine (BH), fish (FH), and porcine hydrolysates (PH) regarding their antioxidant and hypoglycemic activities. All samples showed percentages above 90% of protein content, with high levels of amino acids (glycine, proline, and hydroxyproline), responsible for the specific structure of collagen. The BH sample showed a higher degree of hydrolysis (DH) (8.7%) and a higher percentage of smaller than 2 kDa peptides (74.1%). All collagens analyzed in vitro showed inhibition of pancreatic enzymes (α-amylase and α-glucosidase), with the potential to prevent diabetes mellitus. The PH sample showed higher antioxidant activities measured by ORAC (67.08 ± 4.23 μmol Trolox Eq./g) and ABTS radical scavenging (65.69 ± 3.53 μmol Trolox Eq./g) methods. For the first time, DNA protection was analyzed to hydrolyzed collagen peptides, and the FH sample showed a protective antioxidant action to supercoiled DNA both in the presence (39.51%) and in the absence (96.36%) of AAPH (reagent 2,2'-azobis(2-amidinopropane)). The results confirmed that the source of native collagen reflects on the bioactivity of hydrolyzed collagen peptides, probably due to its amino acid composition. PRACTICAL APPLICATIONS: Our data provide new application for collagen hydrolysates with hypoglycemiant and antioxidant activity. These data open discussion for future studies on the additional benefits arising from collagen peptide consumption for the prevention of aging complications or hyperglycemic conditions as observed in chronic diseases such as diabetes mellitus type II (DM 2). The confirmation of these results can open new market areas for the use of collagen with pharmacological applications or to produce new supplements. Furthermore, provides a solution for waste collagen from meat industries and adds value to the product.
(© 2022 Wiley Periodicals LLC.)
Databáze: MEDLINE
Externí odkaz:
Nepřihlášeným uživatelům se plný text nezobrazuje