Identification, overexpression, purification, and biochemical characterization of a novel hyperthermostable keratinase from Geoglobus acetivorans-Reference-Cited by-同舟云学术

Identification, overexpression, purification, and biochemical characterization of a novel hyperthermostable keratinase from Geoglobus acetivorans

Published:2020-11-27 Issue:1 Volume:11 Page:
ISSN:2190-572X
Container-title:3 Biotech
language:en
Short-container-title:3 Biotech

Author:

Sittipol Duangjai,Rodpan Sudarat,Ajingi Ya’u S.^ORCID,Lohnoo Tassanee,Lerksuthirat Tassanee,Kumsang Yothin,Yingyong Wanta,Khunrae Pongsak^ORCID,Rattanarojpong Triwit^ORCID,Pattanapanyasat Kovit^ORCID,Jongruja Nujarin^ORCID

Funder

•Thailand Science Research and Innovation and Office of the Higher Education Commission

•Research funding from the Faculty of Science, King Mongkut’s University of Technology Thonburi, KMUTT

Research Fund, and Petchra Pra Jom Klao Ph.D. scholarship

Publisher

Springer Science and Business Media LLC

Subject

Agricultural and Biological Sciences (miscellaneous),Environmental Science (miscellaneous),Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s13205-020-02538-1.pdf

Reference42 articles.

1. Agrahari S, Wadhwa N (2010) Degradation of chicken feather a poultry waste product by keratinolytic bacteria isolated from dumping site at ghazipur poultry process. Plant Int J S 9:482–489. https://doi.org/10.3923/ijps.2010.482.489

2. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215:403–410. https://doi.org/10.1016/S0022-2836-80360-2

3. Bohacz J (2017) Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporiumand statistical optimization of feather mass loss. World J Microbio Biotechnol. 33:13–29. https://doi.org/10.1007/s11274-016-2177-2

4. Bradford MM (1976) A Rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding (PDF). Anal Bioc 72:248–254. https://doi.org/10.1016/0003-2697(76)90527-3

5. Christopher TS, James AC, Diep MN, Chang-Hao W, Benjamin MZ, James RC, Jonathan MC, Jonathan KO, Gina LL, Gerrit JS, Michael WA, Robert MK (2018) Biotechnology of extremely thermophilic archaea. FEMS Microbiol Rev 42:543–578. https://doi.org/10.1093/femsre/fuy012

Cited by 9 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Design, development and characterization of a chimeric protein with disulfide reductase and protease domain showing keratinase activity;International Journal of Biological Macromolecules;2024-10

2. Perspective on Agricultural Industrialization: Modification Strategies for Enhancing the Catalytic Capacity of Keratinase;Journal of Agricultural and Food Chemistry;2024-06-04

3. Synthesis and characterization of keratinase laden green synthesized silver nanoparticles for valorization of feather keratin;Scientific Reports;2023-07-18

4. Cloning, recombinant expression, purification, and functional characterization of AGAAN antibacterial peptide;3 Biotech;2023-02-18

5. Research progress on the degradation mechanism and modification of keratinase;Applied Microbiology and Biotechnology;2023-01-12