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Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from Acipenser schrencki

文献类型: 外文期刊

作者: Zu, Xiao-Yan 1 ; Liu, Wen-Bo 1 ; Xiong, Guang-Quan 1 ; Liao, Tao 1 ; Li, Hai-Lan 1 ;

作者机构: 1.Hubei Acad Agr Sci, Inst Agroprod Proc & Nucl Agr Technol, Minist Agr & Rural Affairs, Key Lab Cold Chain Logist Technol Agroprod, Wuhan 430064, Peoples R China

2.Wuhan Inst Technol, Sch Chem & Environm Engn, Wuhan 430205, Peoples R China

关键词: Acipenser schrencki; swim bladder polypeptides; antioxidant peptides; peptide sequence

期刊名称:FOODS ( 影响因子:5.2; 五年影响因子:5.5 )

ISSN:

年卷期: 2023 年 12 卷 10 期

页码:

收录情况: SCI

摘要: Swim bladder polypeptides (SBPs) of Acipenser schrencki were analyzed for their antioxidant activity and physicochemical properties. The results showed the optimal enzymatic conditions were alkaline protease with a solid-to-liquid ratio of 1:20, an incubation time of 4 h, a temperature of 55 degrees C, and an enzyme dosage of 5000 U/g. Three different molecular weight fractions (F1, F2, and F3) were obtained via ultrafiltration. F3 (912.44-2135.82 Da) showed 77.90%, 72.15%, and 66.25% removal of O-2 center dot(-), DPPH center dot, and center dot OH, respectively, at 10 mg/mL, which was significantly higher than the F1 and F2 fractions (p < 0.05). F3 contained proline (6.17%), hydroxyproline (5.28%), and hydrophobic amino acids (51.39%). The UV spectrum of F3 showed maximum absorption at 224 nm. Peptide sequence analysis showed that F3 contained antioxidant peptides (MFGF, GPPGPRGPPGL, and GPGPSGERGPPGPM) and exhibited inhibitory activities on angiotensin-converting enzyme and dipeptidyl peptidase III/IV (FRF, FPFL and LPGLF). F3 was considered a good raw material for obtaining bioactive peptides.

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