Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Zhemin Liu"'
Autor:
Xinyang Liu, Jiao Liu, Zhemin Liu, Qianqian Qiao, Xiaomeng Ni, Jinxing Yang, Guannan Sun, Fanghe Li, Wenjuan Zhou, Xuan Guo, Jiuzhou Chen, Shiru Jia, Yu Zheng, Ping Zheng, Jibin Sun
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 11 (2024)
Allosteric regulation by pathway products plays a vital role in amino acid metabolism. Homoserine dehydrogenase (HSD), the key enzyme for the biosynthesis of various aspartate family amino acids, is subject to feedback inhibition by l-threonine and l
Externí odkaz:
https://doaj.org/article/494f5fb264df49a28c51892a9c96dad8
Autor:
Qingping Liang, Youtao Huang, Zhemin Liu, Mengshi Xiao, Xinmiao Ren, Tianhong Liu, Hongyan Li, Dongxing Yu, Ying Wang, Changliang Zhu
Publikováno v:
Foods, Vol 12, Iss 21, p 4039 (2023)
Alginate lyase has been demonstrated as an efficient tool in the preparation of functional oligosaccharides (AOS) from alginate. The high viscosity resulting from the high concentration of alginate poses a limiting factor affecting enzymatic hydrolys
Externí odkaz:
https://doaj.org/article/ec649f0af7e84293a32b17f7c39a4d87
Autor:
Jiao Liu, Moshi Liu, Tuo Shi, Guannan Sun, Ning Gao, Xiaojia Zhao, Xuan Guo, Xiaomeng Ni, Qianqian Yuan, Jinhui Feng, Zhemin Liu, Yanmei Guo, Jiuzhou Chen, Yu Wang, Ping Zheng, Jibin Sun
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Corynebacterium glutamicum is a major workhorse in industrial biomanufacturing of amino acids. Here, the authors employ CRISPR-assisted rational flux-tuning and CRISPRi screening of a L-proline exporter to covert a wild-type C. glutamicum to a hyperp
Externí odkaz:
https://doaj.org/article/8909610a7e924f37b99a9cdaf4ef0ff8
Publikováno v:
Microbial Biotechnology, Vol 14, Iss 4, Pp 1525-1538 (2021)
Summary To further extend the practical application of a thermostable and acidic resistance β‐mannanase (ManAK) in animal feed additives, an effective strategy that combined directed evolution and metabolic engineering was developed. Four positive
Externí odkaz:
https://doaj.org/article/97ab27fae3e14fe3b89d6893cc6110b4
Autor:
Ming Tian, Chen Ning, Siyuan Peng, Deyu Li, Renyi Jin, Yang Zhang, Zhemin Liu, Haijin Mou, Changliang Zhu
Publikováno v:
Foods, Vol 12, Iss 6, p 1252 (2023)
In recent years, cardiovascular and cerebrovascular diseases have been the focus of several studies. In this study, oyster protein hydrolysate was produced via enzyme hydrolysis and used as a fermentation substrate to ferment recombinant strain PSP2
Externí odkaz:
https://doaj.org/article/73dd4a01fc8d4d06b3f931abd19c98a4
Publikováno v:
Microbiology Spectrum, Vol 10, Iss 1 (2022)
ABSTRACT Aspergillus flavus aflR, a gene encoding a Zn(II)2Cys6 DNA-binding domain, is an important transcriptional regulator of the aflatoxin biosynthesis gene cluster. Our previous results of Gene ontology (GO) analysis for the binding sites of Afl
Externí odkaz:
https://doaj.org/article/ac00031079594a1a910f3003c31124c8
Autor:
Qingping Liang, Yuming Zhan, Mingxue Yuan, Linyuan Cao, Changliang Zhu, Haijin Mou, Zhemin Liu
Publikováno v:
Frontiers in Microbiology, Vol 12 (2021)
In order to improve the catalytic efficiency of a thermostable and acidophilic β-mannanase (ManAK; derived from marine Aspergillus kawachii IFO 4308), three mutants were designed by amino acid sequence consensus analysis with a second β-mannanase (
Externí odkaz:
https://doaj.org/article/bf4bb3e2c41e44f082cc472aab828039
Publikováno v:
Frontiers in Microbiology, Vol 11 (2020)
Glucose oxidase (GOx) with high enzyme activity at low temperature (4°C) is potentially useful for food preservation, especially for aquatic products preservation. A cold-active GOx with approximately 83% similarity to known protein sequences, was i
Externí odkaz:
https://doaj.org/article/e662d1d718c64b80942c936ae3348ded
Publikováno v:
Marine Drugs, Vol 18, Iss 6, p 305 (2020)
Alginate is one of the most abundant polysaccharides in algae. Alginate lyase degrades alginate through a β-elimination mechanism to produce alginate oligosaccharides with special bioactivities. Improving enzyme activity and thermal stability can pr
Externí odkaz:
https://doaj.org/article/3e0de1dd6af6450490aa8cdcc6380ecb
Publikováno v:
Frontiers in Microbiology, Vol 8 (2017)
κ-Carrageenase belongs to glycoside hydrolase family 16 and cleaves the β-(1→4) linkages of κ-carrageenan. In this study, genes encoding the full-length (cgkZ), Por secretion tail-truncated (cgkZΔPst) and carbohydrate binding domain-truncated (
Externí odkaz:
https://doaj.org/article/ab0d0190b88442568b5bb95dc7e22086