Zobrazeno 1 - 10
of 55
pro vyhledávání: '"YI-RUI YIN"'
Autor:
Yi-Rui Yin, En-Min Zhou, Hong Ming, Wael Nabil Hozzein, Iftikhar Ahmed, Hongchen Jiang, Wen-Jun Li
Publikováno v:
Frontiers in Microbiology, Vol 15 (2024)
Externí odkaz:
https://doaj.org/article/f081bc1985dd4e9f86c194959adb0816
Autor:
Yi-Rui Yin, Xin-Wei Li, Chao-Hua Long, Lei Li, Yu-Ying Hang, Meng-Di Rao, Xin Yan, Quan-Lin Liu, Peng Sang, Wen-Jun Li, Li-Quan Yang
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-12 (2023)
Abstract A xylanase gene (named xyngmqa) was identified from the metagenomic data of the Gumingquan hot spring (92.5 °C, pH 9.2) in Tengchong City, Yunnan Province, southwest China. It showed the highest amino acid sequence identity (82.70%) to endo
Externí odkaz:
https://doaj.org/article/2fee364b2fa344279a94f50993421d0e
Autor:
Yu-Ying Huang, Zhi-Hua Lv, Hong-Zhao Zheng, Qian Zhu, Meng-Ting Liu, Peng Sang, Fei Wang, Dan Zhu, Wen-Dong Xian, Yi-Rui Yin
Publikováno v:
Frontiers in Microbiology, Vol 14 (2023)
Introductionβ-Glucosidase serves as the pivotal rate-limiting enzyme in the cellulose degradation process, facilitating the hydrolysis of cellobiose and cellooligosaccharides into glucose. However, the widespread application of numerous β-glucosida
Externí odkaz:
https://doaj.org/article/ff2a334df66143848ccffb1822c69924
Autor:
Zheng-Shuang Hua, Yan-Ni Qu, Qiyun Zhu, En-Min Zhou, Yan-Ling Qi, Yi-Rui Yin, Yang-Zhi Rao, Ye Tian, Yu-Xian Li, Lan Liu, Cindy J. Castelle, Brian P. Hedlund, Wen-Sheng Shu, Rob Knight, Wen-Jun Li
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
The phylum of archaea Aigarchaeota is poorly characterized due to limited genomic sampling. Here, Hua and colleagues use genome-resolved metagenome sequencing to reconstruct six hot spring strains of Aigarchaeota and then infer their metabolism and e
Externí odkaz:
https://doaj.org/article/0ae3a0c02a264a15b8733a21f244952d
Autor:
Yi-Rui Yin, Peng Sang, Wen-Dong Xian, Xin Li, Jian-Yu Jiao, Lan Liu, Wael N. Hozzein, Min Xiao, Wen-Jun Li
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
The bioconversion of lignocellulose in various industrial processes, such as biofuel production, requires the degradation of cellulose. Actinomadura amylolytica YIM 77502T is an aerobic, Gram-positive actinomycete that can efficiently degrade crystal
Externí odkaz:
https://doaj.org/article/78b13f34380b4130ab9a59b1664e2fc5
Autor:
Yi-Rui Yin, Zhao-Hui Meng, Qing-Wen Hu, Zhao Jiang, Wen-Dong Xian, Lin-Hua Li, Wei Hu, Feng Zhang, En-Min Zhou, Xiao-Yang Zhi, Wen-Jun Li
Publikováno v:
Frontiers in Microbiology, Vol 8 (2017)
Thermoactinospora rubra YIM 77501T is an aerobic, Gram-positive, spore-forming and cellulose degrading thermophilic actinomycete isolated from a sandy soil sample of a volcano. Its growth temperature range is 28–60°C. The genomic sequence of this
Externí odkaz:
https://doaj.org/article/943e8e3378994462bcaad45537520e27
Autor:
Yu-Ying Huang, Zhi-Hua Lv, Hong-Zhao Zheng, Qian Zhu, Meng-Ting Liu, Peng Sang, Fei Wang, Dan Zhu, Wen-Dong Xian, Yi-Rui Yin
Publikováno v:
Frontiers in Microbiology; 2024, p01-13, 13p
Autor:
Xin-Wei Li, Dan Zhu, Lei Li, Run-Feng Yang, Shi-Yuan Fan, Zhi-Hua Lv, Meng-Di Rao, Rong-Huang Song, Peng Sang, Yi-Rui Yin, Li-Quan Yang
Xylanases are used in a wide range of applications such as food, feed, and bioenergy production. Many industrial applications need to be carried out at high temperatures, so it is important to discover new thermophilic xylanases. In this study, a xyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bd45a3ea2fdc6fface68c99d38dbeb2b
https://doi.org/10.21203/rs.3.rs-2486846/v1
https://doi.org/10.21203/rs.3.rs-2486846/v1
Publikováno v:
Biomass Conversion and Biorefinery.
Autor:
Min Xiao, Yi-Rui Yin, Li-Quan Yang, Shuai Li, Peng Sang, Run-Fen Yang, Tao Li, Hong-Yan Liu, Wen-Jun Li
Publikováno v:
Biomass Conversion and Biorefinery. 12:3399-3408
A novel endoglucanase gene (1425 bp), designated thrcel5A, was cloned from Thermoactinospora rubra YIM 77501Tand determined to be a member of glycoside hydrolase family 5. The putative amino acid sequence displayed 76% conservation with reported endo