Optimization of Enzymatic Hydrolysis of Perilla Meal Protein for Hydrolysate with High Hydrolysis Degree and Antioxidant Activity
Open Access
- 6 February 2022
- Vol. 27 (3), 1079
- https://doi.org/10.3390/molecules27031079
Abstract
Botanical oils are staple consumer goods globally, but as a by-product of oil crops, meal is of low utilization value and prone to causing environmental problems. The development of proteins in meal into bioactive peptides, such as Perilla peptide, through biotechnology can not only solve environmental problems, but also create more valuable nutritional additives. In the present work, the hydrolysis process of Perilla meal protein suitable for industrial application was optimized with the response surface methodology (RSM) on the basis of single-factor experiments. Alcalase was firstly selected as the best-performing among four proteases. Then, based on Alcalase, the optimal hydrolysis conditions were as follows: enzyme concentration of 7%, hydrolysis temperature of 61.4 °C, liquid-solid ratio of 22.33:1 (mL/g) and hydrolysis time of 4 h. Under these conditions, the degree of hydrolysis (DH) of Perilla meal protein was 26.23 ± 0.83% and the DPPH scavenging capacity of hydrolysate was 94.15 ± 1.12%. The soluble peptide or protein concentration of Perilla meal protein hydrolysate rose up to 5.24 ± 0.05 mg/mL, the ideal yield of which was estimated to be 17.9%. SDS-PAGE indicated that a large proportion of new bands in hydrolysate with small molecular weights appeared, which was different from the original Perilla meal protein. The present data contributed to further, more specific research on the separation, purification and identification of antioxidant peptide from the hydrolysate of Perilla meal protein. The results showed that the hydrolysis of Perilla meal protein could yield peptides with high antioxidant activity and potential applications as natural antioxidants in the food industry.Funding Information
- Applied Basic Research Program in Shanxi Province - China (201801D221279, 2020L0625, 2017)
This publication has 43 references indexed in Scilit:
- Characterization of antioxidant activity and volatile compounds of Maillard reaction products derived from different peptide fractions of peanut hydrolysateFood Research International, 2011
- Antioxidant and Antiproliferative Activities of Loach (Misgurnus anguillicaudatus) Peptides Prepared by Papain DigestionJournal of Agricultural and Food Chemistry, 2011
- In vitro antioxidant activity and in vivo anti-fatigue effect of loach (Misgurnus anguillicaudatus) peptides prepared by papain digestionFood Chemistry, 2011
- Pretreatment technologies for an efficient bioethanol production process based on enzymatic hydrolysis: A reviewBioresource Technology, 2010
- Influence of degree of hydrolysis on functional properties and angiotensin I-converting enzyme-inhibitory activity of protein hydrolysates from cuttlefish (Sepia officinalis) by-productsJournal of the Science of Food and Agriculture, 2010
- DPPH antioxidant assay revisitedFood Chemistry, 2009
- Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometryFood Chemistry, 2008
- Improved Method for Determining Food Protein Degree of HydrolysisJournal of Food Science, 2001
- Oxidative stressCurrent Opinion in Microbiology, 1999
- pH-stat method to predict protein digestibility in white shrimp (Penaeus vannamei)Aquaculture, 1997