ABSTRACT
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 IC50 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.
ABSTRACT
The systematic investigations on the value of social wasps as a food resource are deficient, in spite of the long history of the utilization of social wasps as food and pharmaceutical bioresources. Vespa velutina nigrithorax is an invasive alien wasp species that is currently dominating in East Asia and Europe, bringing huge economic damages. As a control over alien species is made when the valuable utilization of the invasive species as a potential resource are discovered, investigations on the potential of V. v. nigrithorax as a useful bioresource are also in demand. Nutritional and heavy metal analyses of the larvae revealed their balanced and rich nutritional value and safety as a food resource. The larval saliva amino acid composition was investigated for further study on amino acid supplementation and exercise enhancement.
ABSTRACT
This study aimed to obtain antioxidant peptides from perilla seed meal (PSM), which is normally discarded as an industrial waste during seed oil extraction. PSM protein was hydrolyzed using trypsin and fractionated by ultrafiltration. Molecular weight fraction (<3 kDa) with the highest antioxidant activity was purified using prep-HPLC and analytical HPLC. The purification fold of the peptide (fraction V) obtained from PSM protein hydrolysate on DPPH radical scavenging activity, ABTS radical scavenging activity, and reducing power was 1.79-, 1.59-, and 1.81-fold, respectively, after the three-step purification procedure. The sequence of the purified peptide from fraction V that exhibited free radical scavenging activity and reducing power was identified as Ile-Ser-Pro-Arg-Ile-Leu-Ser-Tyr-Asn-Leu-Arg (1,330.77 Da). These results demonstrate that PSM protein, a by-product from the oil seed extraction, can be used as a source of natural antioxidant peptides for food and/or nutraceutical applications.
