Influence of In vitro Digestion on Antioxidative Activity of Coconut Meat Protein Hydrolysates
نویسندگان
چکیده
Purpose: To investigate the antioxidative stability of coconut meat protein hydrolysates (CMPHs) in the gastrointestinal tract, and evaluate the changes in antioxidant activity, amino acid composition and molecular weight distribution of CMPHs during gastrointestinal (GI )digestion Methods: A two-stage in vitro digestion model (pepsin treatment for 2 h followed by pancreatin treatment for 2 h, both at 37 °C) was used to simulate the process of GI digestion to determine changes in antioxidant activities, namely, 1,1diphenyl-2-picrylhydrazyl and hydroxyl radical scavenging and reducing power, of CMPHs previously prepared by papain digestion. Results: Based on the in vitro pepsin–pancreatin simulated GI digestion, it was found that there were more free amino acids and smaller oligopeptides with MW < 500 Da in the final GI digests. Compared with blank, enzymatic breakdown of the GI digests increased their hydroxyl (by 11.8 %) and reducing power (by 71.8 %). Conclusion: CMPHs are high value-added antioxidants and possess a potential capacity to resist gastrointestinal digestion, which makes them promising ingredients for formulation of functional foods.
منابع مشابه
Comparison of in vitro digestion characteristics and antioxidant activity of hot- and cold-pressed peanut meals.
Due to the poor protein solubility, hot-pressed peanut meal (HPM) has less value than cold-pressed peanut meal (CPM) in the food industry. The objective of this study was to determine whether the denatured proteins in HPM were suitable for hydrolysis by digestive enzymes. The hydrolysis characteristics and antioxidant activity of HPM and CPM during in vitro digestion were compared. The results ...
متن کاملAntioxidant, Liver Protective and Angiotensin I-converting Enzyme Inhibitory Activities of Old Laying Hen Hydrolysate in Crab Meat Analogue
The purpose of this study was to evaluate the antioxidative activities of Crab meat analogue prepared with protein hydrolysates obtained from mechanically deboned chicken meat (MDCM) from spent laying hens. 2,2-diphenyl-1-picrylhydrazyl hydrate (DPPH) radical-scavenging activity was increased by adding MDCM hydrolysates during storage, and activity correlated with the concentration of DPPH adde...
متن کاملAntioxidant Effect and Water-Holding Capacity of Roselle (Hibiscus sabdariffa L.) Seed Protein Hydrolysates
The aim of this study was to investigate the effect of in-vitro pepsin and pancreatin digestion of proteins extracted from Roselle seed on the production of bioactive peptides. Defatted Roselle seed flour was used to extract different protein fractions namely globulin, albumin and glutelin. The proteins were digested using pepsin (1 h) followed by pancreatin (1 h) in order to produce hydrolysat...
متن کاملAngiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes
The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine enzymes) and ex vivo digestion (with human gastrointestinal enzymes). Secondly, to evaluate the ACE...
متن کاملBioactivity of Cod and Chicken Protein Hydrolysates before and after in vitro Gastrointestinal Digestion.
Bioactivity of cod (Gadus morhua) and chicken (Gallus domesticus) protein hydrolysates before and after in vitro gastrointestinal (GI) digestion was investigated using yeast Saccharomyces cerevisiae as a model organism. Both hydrolysates were exposed to in vitro GI digestion prior to cellular exposure to simulate digestion conditions in the human body and therefore investigate the role of modul...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2015