Functional properties and biological activities of perilla seed meal protein hydrolysates obtained by using different proteolytic enzymes

• Published in: Food science and biotechnology Vol. 29; no. 11; pp. 1553 - 1562
• Main Authors: Kim, Ja Min, Yoon, Kyung Young
• Format: Journal Article
• Language: English
• Published: Singapore Springer Singapore 01.11.2020; Springer Nature B.V; 한국식품과학회
• Subjects: Angiotensin; Angiotensin I; Anti-inflammatory agents; Biological properties; Chemistry; Chemistry and Materials Science; Food Science; Hydrolysates; Inflammation; Nutrition; Oils & fats; Oilseeds; Pepsin; Peptidyl-dipeptidase A; Proteins; Proteolysis; Proteolytic enzymes; Radicals; Scavenging; Seed meal; Seeds; Sulfonic acid; Trypsin; 식품과학; Protein hydrolysate; Functional property; Agricultural by-product; Perilla seed meal; Enzymatic hydrolysis; Biological activity
• ISSN: 1226-7708; 2092-6456
• DOI: 10.1007/s10068-020-00810-x

In this study, we aimed to determine the potential functional properties and biological activities of the hydrolysates of perilla seed meal (PSM), which is a by-product of perilla seed oil extraction. PSM protein was hydrolyzed independently by using five proteases, and their functional and biological properties were analyzed. PSM protein hydrolysate exhibited high solubility at most of the tested pH values, and the trypsin-treated hydrolysate exhibited the highest water and oil absorption capacity. The neutrase-treated hydrolysate was most effective in scavenging the 1,1-diphenyl-2-picrylhydrazine radicals, whereas the pepsin-treated hydrolysate showed the highest angiotensin I-converting enzyme inhibitory effect, and anti-inflammatory activity. Trypsin-treated hydrolysate exhibited the highest scavenging activity against of 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid radicals with the IC 50 of 109.72 µg/mL. The results of the present study suggest that the type of protease used for the treatment significantly influences the functional properties and biological activities of the resulting PSM protein hydrolysates.