Zobrazeno 1 - 10
of 1 034
pro vyhledávání: '"Enzymology and Protein Engineering"'
Publikováno v:
Appl Environ Microbiol
Rhizopus oryzae lipase (ROL) is one of the most important enzymes used in the food, biofuel, and pharmaceutical industries. However, the highly demanding conditions of industrial processes can reduce its stability and activity. To seek a feasible met
Publikováno v:
Appl Environ Microbiol
CYP105D18 supports H(2)O(2) as an oxygen surrogate for catalysis well and shows high H(2)O(2) resistance capacity. We report the hydroxylation of different steroids using H(2)O(2) as a cosubstrate. Testosterone was regiospecifically hydroxylated to 2
Autor:
Shohei Kajimoto, Miwa Ohashi, Yusuke Hagiwara, Daisuke Takahashi, Yasuhiro Mihara, Tomoharu Motoyama, Sohei Ito, Shogo Nakano
Publikováno v:
Appl Environ Microbiol
Oligonucleotide therapeutics have great potential as a next-generation approach to treating intractable diseases. Large quantities of modified DNA/RNA containing xenobiotic nucleic acids (XNAs) must be synthesized before clinical application. In this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7be01e23faa51166bc5cdfd3437e05d
https://europepmc.org/articles/PMC9746290/
https://europepmc.org/articles/PMC9746290/
Publikováno v:
Appl Environ Microbiol
Alginate lyases play a vital role in the degradation of alginate, an important marine carbon source. Alginate is a complex macromolecular substrate, and the synergy of alginate lyases is important for the alginate utilization by microbes and the appl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47dbba2057396ec36a7520548485f4c0
https://europepmc.org/articles/PMC9746311/
https://europepmc.org/articles/PMC9746311/
Autor:
Jean-Lou Reyre, Sacha Grisel, Mireille Haon, David Navarro, David Ropartz, Sophie Le Gall, Eric Record, Giuliano Sciara, Olivier Tranquet, Jean-Guy Berrin, Bastien Bissaro
Publikováno v:
Appl Environ Microbiol
Applied and Environmental Microbiology
Applied and Environmental Microbiology, 2022, 88 (23), pp.1-16. ⟨10.1128/aem.01581-22⟩
Applied and Environmental Microbiology
Applied and Environmental Microbiology, 2022, 88 (23), pp.1-16. ⟨10.1128/aem.01581-22⟩
Filamentous fungi are keystone microorganisms in the regulation of many processes occurring on Earth, such as plant biomass decay, pathogenesis as well as symbiotic associations. In many of these processes, fungi secrete carbohydrate-active enzymes (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d34796c7e1fcc68471dacd8d3483947a
https://europepmc.org/articles/PMC9746322/
https://europepmc.org/articles/PMC9746322/
Publikováno v:
Appl Environ Microbiol
Microbial Vpr-like proteases are extracellular multidomain subtilases with diverse functions and can form oligomers, but their maturation and oligomerization mechanisms remain to be elucidated. Here, we report a novel Vpr-like protease (BTV) from the
Autor:
Jie Zheng, Han-qing Liu, Xing Qin, Kun Yang, Jian Tian, Xiao-lu Wang, Ya-ru Wang, Yuan Wang, Bin Yao, Hui-ying Luo, Huo-qing Huang
Publikováno v:
Appl Environ Microbiol
Exploring the potential functions of nonconserved residues on the outer side of α-helices and systematically optimizing them are pivotal for their application in protein engineering. Based on the evolutionary structural conservation analysis of GH5_
Autor:
Xiangfeng Meng, Xiaodan Li, Tjaard Pijning, Xiaofei Wang, Sander S. van Leeuwen, Lubbert Dijkhuizen, Guanjun Chen, Weifeng Liu
Publikováno v:
Appl Environ Microbiol
Applied and environmental microbiology, 88(16):e0103122. AMER SOC MICROBIOLOGY
Applied and environmental microbiology, 88(16):e0103122. AMER SOC MICROBIOLOGY
Branching sucrases, a subfamily of Glycoside Hydrolase family (GH70), display transglycosidase activity using sucrose as donor substrate to catalyze glucosylation reaction in the presence of suitable acceptor substrates. In this study, the (α1→3)
Publikováno v:
Appl Environ Microbiol
Hesperidin, a flavonoid enriched in citrus peel, can be enzymatically glycosylated using CGTase with significantly improved water solubility. However, the reaction catalyzed by wild-type CGTase is rather inefficient, reflected in the poor production
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d6814168024346f9aedbd4270391732
https://europepmc.org/articles/PMC9469708/
https://europepmc.org/articles/PMC9469708/