Version 1
: Received: 23 July 2019 / Approved: 24 July 2019 / Online: 24 July 2019 (11:56:00 CEST)
How to cite:
Liu, D.; Huang, J.; Wu, C.; Liu, C.; Huan, R.; Wang, M.; He, H.; Chen, L. Purification, Characterization and Application for Preparation of Antioxidant Peptides of Extracellular Protease from Pseudoalteromonas sp. H2. Preprints2019, 2019070273
Liu, D.; Huang, J.; Wu, C.; Liu, C.; Huan, R.; Wang, M.; He, H.; Chen, L. Purification, Characterization and Application for Preparation of Antioxidant Peptides of Extracellular Protease from Pseudoalteromonas sp. H2. Preprints 2019, 2019070273
Liu, D.; Huang, J.; Wu, C.; Liu, C.; Huan, R.; Wang, M.; He, H.; Chen, L. Purification, Characterization and Application for Preparation of Antioxidant Peptides of Extracellular Protease from Pseudoalteromonas sp. H2. Preprints2019, 2019070273
APA Style
Liu, D., Huang, J., Wu, C., Liu, C., Huan, R., Wang, M., He, H., & Chen, L. (2019). Purification, Characterization and Application for Preparation of Antioxidant Peptides of Extracellular Protease from Pseudoalteromonas sp. H2. Preprints. https://doi.org/
Chicago/Turabian Style
Liu, D., Hailun He and Leilei Chen. 2019 "Purification, Characterization and Application for Preparation of Antioxidant Peptides of Extracellular Protease from Pseudoalteromonas sp. H2" Preprints. https://doi.org/
Abstract
In this study, an extracellular metalloprotease from Pseudoalteromonas sp. H2 was purified and identified. The EH2 maintained more than 80% activity over a wide pH range of 5-10 and the stability was also nearly independent of pH. More than 65% of activity was detected in a wide temperature of 20-70℃. The high stability of the protease in presence of different surfactants and oxidizing agent was also observed. Moreover, we also investigated the antioxidant activities of the hydrolysates generated from porcine and salmon skins collagen by EH2. The results show that salmon skins collagen hydrolysates demonstrated higher DPPH (42.88%±1.85) and hydroxyl radical (61.83%±3.05) scavenging activity compared to those produced with porcine skins collagen. For oxygen radical absorbance capacity, the hydrolysates from porcine skins collagen had higher efficiency (7.72±0.13 μmol·TE/μmol). Even 1 nM mixed peptides can effectively reduce the levels of intracellular ROS. And the two type of substrates exerted the best antioxidant activity when hydrolyzed for 3 hours. Hydrolysis time and type of substrate exerted important effect on the antioxidant property of hydrolysates. This study may have implications for the potential application of marine protease in biocatalysis industry. In addition, the hydrolyzed peptides from meat waste containing beneficial collagen by protease have good antioxidant activity indicating it may be a potential additive in the food processing industry and cosmetics industry.
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
