Purification, Characterization, and Application for Preparation of Antioxidant Peptides of Extracellular Protease from Pseudoalteromonas sp. H2
文献类型: 外文期刊
作者: Liu, Dan 1 ; Huang, Jiafeng 1 ; Wu, Cuiling 3 ; Liu, Congling 1 ; Huang, Ran 1 ; Wang, Weng 1 ; Yin, Tingting 1 ; Yan, Xiaotao 1 ; He, Hailun 1 ; Chen, Leilei 4 ;
作者机构: 1.Cent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R China
2.Guangxi Med Univ, Dept Biochem & Mol Biol, Nanning 530021, Peoples R China
3.Changzhi Med Coll, Dept Biochem, Changzhi 046000, Peoples R China
4.BTBU, Beijing Adv Innovat Ctr Food Nutr & Human Hlth, Beijing 100048, Peoples R China
5.Shandong Acad Agr Sci, Inst Agrofood Sci & Technol, Jinan 250100, Shandong, Peoples R China
关键词: Pseudoalteromonas; protease; hydrolysis; collagen; antioxidant peptides
期刊名称:MOLECULES ( 影响因子:4.411; 五年影响因子:4.587 )
ISSN:
年卷期: 2019 年 24 卷 18 期
页码:
收录情况: SCI
摘要:
The study reported on the isolation of a metalloprotease named EH2 from Pseudoalteromonas sp. H2. EH2 maintained more than 80% activity over a wide pH range of 5-10, and the stability was also nearly independent of pH. Over 65% activity was detected at a wide temperature range of 20-70 degrees C. The high stability of the protease in the presence of different surfactants and oxidizing agents was also observed. Moreover, we also investigated the antioxidant activities of the hydrolysates generated from porcine and salmon skin collagen by EH2. The results showed that salmon skin collagen hydrolysates demonstrated higher DPPH (1,1-diphenyl-2-picrylhydrazyl) (42.88% +/- 1.85) and hydroxyl radical (61.83% +/- 3.05) scavenging activity than porcine skin collagen. For oxygen radical absorbance capacity, the hydrolysates from porcine skin collagen had higher efficiency (7.72 +/- 0.13 mu mol
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