Bibliographic Details
| Title: |
A Novel Gelatinase from Marine Flocculibacter collagenilyticus SM1988: Characterization and Potential Application in Collagen Oligopeptide-Rich Hydrolysate Preparation |
| Authors: |
Jian Li, Jun-Hui Cheng, Zhao-Jie Teng, Xia Zhang, Xiu-Lan Chen, Mei-Ling Sun, Jing-Ping Wang, Yu-Zhong Zhang, Jun-Mei Ding, Xin-Min Tian, Xi-Ying Zhang |
| Source: |
Marine Drugs, Vol 20, Iss 1, p 48 (2022) |
| Publisher Information: |
MDPI AG, 2022. |
| Publication Year: |
2022 |
| Collection: |
LCC:Biology (General) |
| Subject Terms: |
peptidase, the MEROPS S8 family, bovine bone collagen, oligopeptides, hydrolysate, Biology (General), QH301-705.5 |
| More Details: |
Although the S8 family in the MEROPS database contains many peptidases, only a few S8 peptidases have been applied in the preparation of bioactive oligopeptides. Bovine bone collagen is a good source for preparing collagen oligopeptides, but has been so far rarely applied in collagen peptide preparation. Here, we characterized a novel S8 gelatinase, Aa2_1884, from marine bacterium Flocculibacter collagenilyticus SM1988T, and evaluated its potential application in the preparation of collagen oligopeptides from bovine bone collagen. Aa2_1884 is a multimodular S8 peptidase with a distinct domain architecture from other reported peptidases. The recombinant Aa2_1884 over-expressed in Escherichia coli showed high activity toward gelatin and denatured collagens, but no activity toward natural collagens, indicating that Aa2_1884 is a gelatinase. To evaluate the potential of Aa2_1884 in the preparation of collagen oligopeptides from bovine bone collagen, three enzymatic hydrolysis parameters, hydrolysis temperature, hydrolysis time and enzyme-substrate ratio (E/S), were optimized by single factor experiments, and the optimal hydrolysis conditions were determined to be reaction at 60 ℃ for 3 h with an E/S of 400 U/g. Under these conditions, the hydrolysis efficiency of bovine bone collagen by Aa2_1884 reached 95.3%. The resultant hydrolysate contained 97.8% peptides, in which peptides with a molecular weight lower than 1000 Da and 500 Da accounted for 55.1% and 39.5%, respectively, indicating that the hydrolysate was rich in oligopeptides. These results indicate that Aa2_1884 likely has a promising potential application in the preparation of collagen oligopeptide-rich hydrolysate from bovine bone collagen, which may provide a feasible way for the high-value utilization of bovine bone collagen. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
1660-3397 |
| Relation: |
https://www.mdpi.com/1660-3397/20/1/48; https://doaj.org/toc/1660-3397 |
| DOI: |
10.3390/md20010048 |
| Access URL: |
https://doaj.org/article/9a69fde48199483bad8fd34637bb2089 |
| Accession Number: |
edsdoj.9a69fde48199483bad8fd34637bb2089 |
| Database: |
Directory of Open Access Journals |
