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

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Autor(es):
Gaspardi, Ana Lais Andrade ; da Silva, Daniele Cristina ; Ponte, Luis Gustavo Saboia ; Galland, Fabiana ; da Silva, Vera Sonia Nunes ; Simabuco, Fernando Moreira ; Bezerra, Rosangela Maria Neves ; Pacheco, Maria Teresa Bertoldo
Número total de Autores: 8
Tipo de documento: Artigo Científico
Fonte: JOURNAL OF FOOD BIOCHEMISTRY; v. 46, n. 12, p. 14-pg., 2022-10-01.
Resumo

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 (alpha-amylase and alpha-glucosidase), with the potential to prevent diabetes mellitus. The PH sample showed higher antioxidant activities measured by ORAC (67.08 +/- 4.23 mu mol Trolox Eq./g) and ABTS radical scavenging (65.69 +/- 3.53 mu mol 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. (AU)

Processo FAPESP: 19/11200-7 - Prospecção de bioatividade de peptídeos provenientes de hidrolisados de colágeno
Beneficiário:Ana Lais Andrade Gaspardi
Modalidade de apoio: Bolsas no Brasil - Mestrado
Processo FAPESP: 17/50349-0 - Plano de desenvolvimento institucional em pesquisa do Instituto de Tecnologia de Alimentos - ITAL (PDIp)
Beneficiário:Claire Isabel Grígoli de Luca Sarantópoulos
Modalidade de apoio: Auxílio à Pesquisa - Programa Modernização de Institutos Estaduais de Pesquisa