Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from <i>Acipenser schrencki</i>
Xiao-Yan Zu,
Wen-Bo Liu,
Guang-Quan Xiong,
Tao Liao,
Hai-Lan Li
Affiliations
Xiao-Yan Zu
Key Laboratory of Cold Chain Logistics Technology for Agro-Product (Ministry of Agriculture and Rural Affairs), Institute of Agro-Products Processing and Nuclear Agricultural Technology, Hubei Academy of Agricultural Sciences, Wuhan 430064, China
Wen-Bo Liu
Key Laboratory of Cold Chain Logistics Technology for Agro-Product (Ministry of Agriculture and Rural Affairs), Institute of Agro-Products Processing and Nuclear Agricultural Technology, Hubei Academy of Agricultural Sciences, Wuhan 430064, China
Guang-Quan Xiong
Key Laboratory of Cold Chain Logistics Technology for Agro-Product (Ministry of Agriculture and Rural Affairs), Institute of Agro-Products Processing and Nuclear Agricultural Technology, Hubei Academy of Agricultural Sciences, Wuhan 430064, China
Tao Liao
Key Laboratory of Cold Chain Logistics Technology for Agro-Product (Ministry of Agriculture and Rural Affairs), Institute of Agro-Products Processing and Nuclear Agricultural Technology, Hubei Academy of Agricultural Sciences, Wuhan 430064, China
Hai-Lan Li
Key Laboratory of Cold Chain Logistics Technology for Agro-Product (Ministry of Agriculture and Rural Affairs), Institute of Agro-Products Processing and Nuclear Agricultural Technology, Hubei Academy of Agricultural Sciences, Wuhan 430064, China
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 °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 O2•-, DPPH•, and •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.
