Results 111 to 120 of about 5,463 (163)

Antimicrobial activity and antifungal mechanistic study of 3‑substituted oxindoles against Aspergillus niger. [PDF]

Sci Rep
Ezelarab HAA, El-Bouseary MM, Yahia R, Abd El-Baky RM, Mawhoup MA, Ahmed EF, Sadiq GM, Ali TFS, Abbas SH, Hassan HA, Beshr EAM.   +10 more
europepmc   +1 more source

An artificial selection procedure enriches for known and suspected chitin degraders from the prokaryotic rare biosphere of multiple marine biotopes. [PDF]

BMC Microbiol
Meunier L, Keller-Costa T, Cannella D, Gonçalves JMS, Dechamps E, Marques M, Costa R, George IF.   +7 more
europepmc   +1 more source

Diverse nitrogen acquisition strategies of conifer-associated ectomycorrhizal fungi shape unique responses to changing nitrogen regimes. [PDF]

Front Plant Sci
Lofgren L, Maillard F, Michaud T, Gredeby A, Tunlid A, Kennedy PG.   +5 more
europepmc   +1 more source

Green bioconversion of insoluble chitin: chitinase development pathways via multi-strategy synergy. [PDF]

Bioresour Bioprocess
Sai ZP, Yin YR, Yang LQ, Wang JH, Yang XY, Liu FX, Jing X, Zhang Y, Li YD, Sang P, Yang ZF.   +10 more
europepmc   +1 more source

Comprehensive characterization of the impairing effects of Nosema bombycis on the host digestive integrity and function. [PDF]

mSphere
Cao L, Yin S, Liu D, Tang Y, Yang W, Ran M, Chen J, Pan G, Zhou Z, Bao J.   +9 more
europepmc   +1 more source

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Engineering chitin deacetylase AsCDA for improving the catalytic efficiency towards crystalline chitin

Carbohydrate Polymers, 2023
Chitin deacetylase (CDA) catalyzing the deacetylation of crystal chitin is a crucial step in the biosynthesis of chitosan, and also a scientific problem to be solved, which restricts the high-value utilization of chitin resources. This study aims to improve the catalytic efficiency of AsCDA from Acinetobacter schindleri MCDA01 by a semi-rational design
Guang, Yang, Zhihong, Hu, Yuhan, Wang, Hongjuan, Mo, Shu, Liu, Xiaoyue, Hou, Xudong, Wu, Hong, Jiang, Yaowei, Fang   +8 more
openaire   +2 more sources

Enzymatic modification of native chitin and chitin oligosaccharides by an alkaline chitin deacetylase from Microbacterium esteraromaticum MCDA02

International Journal of Biological Macromolecules, 2022
In this study, chitin deacetylase from Microbacterium esteraromaticum MCDA02 (MeCDA) was purified by ammonium sulfate precipitation, anion exchange chromatography, and superdex column chromatography. The molecular weight of purified MeCDA was approximately 26 kDa. The optimum pH and temperature of purified MeCDA were 8.0 and 30 °C, respectively.
Guang, Yang, Xiaoyue, Hou, Jing, Lu, Minbo, Wang, Yuhan, Wang, Yichen, Huang, Qitong, Liu, Shu, Liu, Yaowei, Fang   +8 more
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Shrimp chitin as substrate for fungal chitin deacetylase

Applied Microbiology and Biotechnology, 2001
The fungal chitin deacetylases (CDA) studied so far are able to perform heterogeneous enzymatic deacetylation on their solid substrate, but only to a limited extent. Kinetic data show that about 5-10% of the N-acetyl glucosamine residues are deacetylated rapidly. Thereafter enzymatic deacetylation is slow.
N N, Win, W F, Stevens
openaire   +2 more sources

Activity of chitin deacetylase from Colletotrichum gloeosporioides on chitinous substrates

Carbohydrate Polymers, 2013
Production of chitin deacetylases from the phytopathogenic fungus Colletotrichum gloeosporioides was successfully achieved by submerged fermentation. The highest specific activity of 0.018 U mg(-1) of protein was obtained after 96 h of cultivation at pH 6 and 28°C.
Pacheco, Neith, Trombotto, Stéphane, David, Laurent, Shirai, Keiko   +3 more
openaire   +3 more sources

Chitin deacetylases: new, versatile tools in biotechnology

Trends in Biotechnology, 2000
Chitin deacetylases have been identified in several fungi and insects. They catalyse the hydrolysis of N-acetamido bonds of chitin, converting it to chitosan. Chitosans, which are produced by a harsh thermochemical procedure, have several applications in areas such as biomedicine, food ingredients, cosmetics and pharmaceuticals.
I, Tsigos, A, Martinou, D, Kafetzopoulos, V, Bouriotis   +3 more
openaire   +2 more sources