干旱区生态环境知识资源中心(Arid): Molecular Identification of Keratinase DgokerA from Deinococcus gobiensis for Feather Degradation

Arid

DOI	10.3390/app12010464
	Molecular Identification of Keratinase DgokerA from Deinococcus gobiensis for Feather Degradation
	Meng, Yong; Tang, Yin; Zhang, Xiuhong; Wang, Jin; Zhou, Zhengfu
通讯作者	Zhou, ZF (corresponding author)，Chinese Acad Agr Sci, Biotechnol Res Inst, Beijing 100081, Peoples R China.
来源期刊	APPLIED SCIENCES-BASEL
EISSN	2076-3417
出版年	2022
卷号	12 期号:1
英文摘要	Keratin is a tough fibrous structural protein that is difficult to digest with pepsin and trypsin because of the presence of a large number of disulfide bonds. Keratin is widely found in agricultural waste. In recent years, especially, the development of the poultry industry has resulted in a large accumulation of feather keratin resources, which seriously pollute the environment. Keratinase can specifically attack disulfide bridges in keratin, converting them from complex to simplified forms. The keratinase thermal stability has drawn attention to various biotechnological industries. It is significant to identify keratinases and improve their thermostability from microorganism in extreme environments. In this study, the keratinases DgoKerA was identified in Deinococcus gobiensis I-0 from the Gobi desert. The amino acid sequence analysis revealed that DgoKerA was 58.68% identical to the keratinase MtaKerA from M. thermophila WR-220 and 40.94% identical to the classical BliKerA sequence from B. licheniformis PWD-1. In vitro enzyme activity analysis showed that DgoKerA exhibited an optimum temperature of 60 degrees C, an optimum pH of 7 and a specific enzyme activity of 51147 U/mg. DgoKerA can degrade intact feathers at 60 degrees C and has good potential for industrial applications. The molecular modification of DgoKerA was also carried out using site-directed mutagenesis, in which the mutant A350S enzyme activity was increased by nearly 30%, and the results provide a theoretical basis for the development and optimization of keratinase applications.
英文关键词	Deinococcus gobiensis keratinase thermostability feather degradation site-directed mutation
类型	Article
语种	英语
开放获取类型	gold
收录类别	SCI-E
WOS记录号	WOS:000750890200001
WOS关键词	STENOTROPHOMONAS-MALTOPHILIA ; THERMOCOCCUS-KODAKARAENSIS ; PROTEASE ; EXTREMOPHILES ; EXPRESSION ; SEQUENCE ; INSIGHTS ; WASTE ; SITE
WOS类目	Chemistry, Multidisciplinary ; Engineering, Multidisciplinary ; Materials Science, Multidisciplinary ; Physics, Applied
WOS研究方向	Chemistry ; Engineering ; Materials Science ; Physics
资源类型	期刊论文
条目标识符	http://119.78.100.177/qdio/handle/2XILL650/376726
作者单位	[Meng, Yong; Zhang, Xiuhong] Mianyang Habio Bioengn Co Ltd, Mianyang 621011, Sichuan, Peoples R China; [Tang, Yin; Wang, Jin; Zhou, Zhengfu] Chinese Acad Agr Sci, Biotechnol Res Inst, Beijing 100081, Peoples R China
推荐引用方式 GB/T 7714	Meng, Yong,Tang, Yin,Zhang, Xiuhong,et al. Molecular Identification of Keratinase DgokerA from Deinococcus gobiensis for Feather Degradation[J],2022,12(1).
APA	Meng, Yong,Tang, Yin,Zhang, Xiuhong,Wang, Jin,&Zhou, Zhengfu.(2022).Molecular Identification of Keratinase DgokerA from Deinococcus gobiensis for Feather Degradation.APPLIED SCIENCES-BASEL,12(1).
MLA	Meng, Yong,et al."Molecular Identification of Keratinase DgokerA from Deinococcus gobiensis for Feather Degradation".APPLIED SCIENCES-BASEL 12.1(2022).