An arginine aminopeptidase from marine Bacillus axarquiensis SWJSX8 and its application in improving pumpkin seed protein hydrolysis. (10th June 2021)

• Record Type: Journal Article
• Authors: Lei, Fenfen; Chen, Yaqi; Chen, Lin; Zhang, Liwei; Zheng, Jincheng
• Is Part Of: International journal of food science & technology. Volume 56:Number 9(2021)
• Page Start: 4680
• Page End: 4689
• Publication Date: 2021-06-10
• Subjects: Antioxidant capacity -- arginine aminopeptidase -- debittering -- enzyme characteristics -- pumpkin seed protein; Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.15163
• Languages: English
• ISSNs: 0950-5423

Abstract

Summary: An arginine aminopeptidase from Bacillus axarquiensis SWJSX8 (BAAP) was developed for the first time. The enzyme was purified 16.6‐fold with specificity activity of 267.2 U/mg protein and a total yield of 10.5% and was estimated to be 67.0 KDa by SDS‐PAGE. It exhibited the maximum activity at 55 °C and pH 8.5 and was activated by 15–20% NaCl with 50% improvement. BAAP was a metalloaminopeptidase and showed better preference for Arg‐ p NA, Leu‐ p NA and Lys‐ p NA amongst the substrates tested. The introduction of BAAP improved the hydrolysis degree of pumpkin seed protein hydrolysates (PSPHs) by 5.7–8.2% and significantly increased the contents of small peptides and free amino acids, while decreased the bitter intensity score of the PSPHs hydrolysed by Alcalase 2.4 L. The antioxidant capacity of the PSPHs had also been improved. The newly developed BAAP has great potential to be used in hydrolysing proteins that are rich in arginine. Abstract : The study purified and characterized a new arginine aminopeptidase from Bacillus axarquiensis SWJSX8. The introduction of the aminopeptidase significantly improved the hydrolysis efficiency and antioxidant capacity of the pumpkin seed protein hydrolysates. The newly developed aminopeptidase has great potential to be used in hydrolyzing proteins that rich in arginine.