Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacterium
In this study, a gene encoding serine protease (PmSpr288) from cold-adapted bacterium, namely Planococcus maritimus XJ11, was cloned and overexpressed in Escherichia coli BL21 (DE3). Bioinformatics analysis revealed that PmSpr288 belongs to serine protease S8 superfamily with a classical catalytic t...
Saved in:
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Tsinghua University Press
2023-09-01
|
| Series: | Food Science and Human Wellness |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453023000253 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832546468252090368 |
|---|---|
| author | Weijun Leng Xiaoyun Wu Xianghui Qi Hongying Liu Li Yuan Ruichang Gao |
| author_facet | Weijun Leng Xiaoyun Wu Xianghui Qi Hongying Liu Li Yuan Ruichang Gao |
| author_sort | Weijun Leng |
| collection | DOAJ |
| description | In this study, a gene encoding serine protease (PmSpr288) from cold-adapted bacterium, namely Planococcus maritimus XJ11, was cloned and overexpressed in Escherichia coli BL21 (DE3). Bioinformatics analysis revealed that PmSpr288 belongs to serine protease S8 superfamily with a classical catalytic triad comprised by the Asp49, His86 and Ser251. Moreover, PmSpr288 was found to be active over broad alkaline pH and low-moderate temperature, and exhibited wide range of protein substrate specificity. In addition, PmSpr288 was able to hydrolyze the meat proteins actin and myosin, and molecular docking results suggested that the crucial interaction between PmSpr288 and actin/myosin complexes was mainly occupied by hydrogen bonds. The muscle protein hydrolysates of silver carp prepared by PmSpr288 was shown to have antioxidant activity via DPPH radical scavenging assay, which presented an IC50 valve of 1.309 mg/mL. In conclusion, these characteristics imply that PmSpr288 has potential biotechnological application prospect for the production of bioactive peptides. |
| format | Article |
| id | doaj-art-7a07a769e64a4747a62d31b7386b4988 |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2023-09-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-7a07a769e64a4747a62d31b7386b49882025-02-03T06:52:50ZengTsinghua University PressFood Science and Human Wellness2213-45302023-09-0112517511761Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacteriumWeijun Leng0Xiaoyun Wu1Xianghui Qi2Hongying Liu3Li Yuan4Ruichang Gao5School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaOcean College of Hebei Agriculture University, Qinhuangdao 066000, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China; Corresponding authors.School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China; Corresponding authors.In this study, a gene encoding serine protease (PmSpr288) from cold-adapted bacterium, namely Planococcus maritimus XJ11, was cloned and overexpressed in Escherichia coli BL21 (DE3). Bioinformatics analysis revealed that PmSpr288 belongs to serine protease S8 superfamily with a classical catalytic triad comprised by the Asp49, His86 and Ser251. Moreover, PmSpr288 was found to be active over broad alkaline pH and low-moderate temperature, and exhibited wide range of protein substrate specificity. In addition, PmSpr288 was able to hydrolyze the meat proteins actin and myosin, and molecular docking results suggested that the crucial interaction between PmSpr288 and actin/myosin complexes was mainly occupied by hydrogen bonds. The muscle protein hydrolysates of silver carp prepared by PmSpr288 was shown to have antioxidant activity via DPPH radical scavenging assay, which presented an IC50 valve of 1.309 mg/mL. In conclusion, these characteristics imply that PmSpr288 has potential biotechnological application prospect for the production of bioactive peptides.http://www.sciencedirect.com/science/article/pii/S2213453023000253ProteaseSilver carpProtein hydrolysatesMolecular dockingBioactive peptides |
| spellingShingle | Weijun Leng Xiaoyun Wu Xianghui Qi Hongying Liu Li Yuan Ruichang Gao Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacterium Food Science and Human Wellness Protease Silver carp Protein hydrolysates Molecular docking Bioactive peptides |
| title | Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacterium |
| title_full | Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacterium |
| title_fullStr | Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacterium |
| title_full_unstemmed | Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacterium |
| title_short | Systematic functional analysis and potential application of a serine protease from cold-adapted Planococcus bacterium |
| title_sort | systematic functional analysis and potential application of a serine protease from cold adapted planococcus bacterium |
| topic | Protease Silver carp Protein hydrolysates Molecular docking Bioactive peptides |
| url | http://www.sciencedirect.com/science/article/pii/S2213453023000253 |
| work_keys_str_mv | AT weijunleng systematicfunctionalanalysisandpotentialapplicationofaserineproteasefromcoldadaptedplanococcusbacterium AT xiaoyunwu systematicfunctionalanalysisandpotentialapplicationofaserineproteasefromcoldadaptedplanococcusbacterium AT xianghuiqi systematicfunctionalanalysisandpotentialapplicationofaserineproteasefromcoldadaptedplanococcusbacterium AT hongyingliu systematicfunctionalanalysisandpotentialapplicationofaserineproteasefromcoldadaptedplanococcusbacterium AT liyuan systematicfunctionalanalysisandpotentialapplicationofaserineproteasefromcoldadaptedplanococcusbacterium AT ruichanggao systematicfunctionalanalysisandpotentialapplicationofaserineproteasefromcoldadaptedplanococcusbacterium |