Results 141 to 150 of about 59,813 (190)

Taguchi L9 optimization of BsPdaC-CD production in Escherichia coli. [PDF]

Sci Rep
Carnicer M, Haasnoot P, Texidó M, Planas A.   +3 more
europepmc   +1 more source

The oligomeric state of chitooligosaccharide deacetylase from the marine bacterium Vibrio campbellii. [PDF]

Biophys Rep (N Y)
Pongnan S, Robinson RC, Kamonsutthipaijit N, Fukamizo T, Suginta W.   +4 more
europepmc   +1 more source

Cell wall-forming chitin synthases in a chytrid fungus. [PDF]

Npj Fungal Sci
Gaikwad T, Cunliffe M.
europepmc   +1 more source

Genomic and transcriptomic analysis reveals chitin metabolic pathways in the marine bacterium Microbulbifer harenosus CGMCC 1.13584^T. [PDF]

BMC Microbiol
Ren X, Song X, Zhang H, Wang G, Xie F, Muhetaerhan H, Ai L, Tian Y.   +7 more
europepmc   +1 more source

Study on Enzymatic Characteristics of Chitin Deacetylase

Advanced Materials Research, 2011
Chitin deacetylase (CDA) catalyzes the conversion of chitin to chitosan by the deacetylation of N-acetyl-D-glucosamine residues. The results of the fundamental enzymatic properties of chitin deacetylase producing from the high productivity chitin deacetylase strain Z7 show that, the optimum temperature of strain Z7 was 40°C, the optimum pH was 6.5 ...
Jun Ang Liu, Yuan Hao He
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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.
Yaowei Fang, Xiaoyue Hou
exaly   +3 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   +4 more sources

DMSO strengthens chitin deacetylase-chitin interaction: Physicochemical, kinetic, structural and catalytic insights

Carbohydrate Polymers, 2019
Chitin deacetylase, an enzyme isolated from Cryptococcus laurentii RY1, catalyzes the hydrolysis of acetamido group of N-acetyl-D-glucosamine unit of chitin. The primary objective of this study was to characterize and comprehend the activation of chitin deacetylase by DMSO. The secondary structure of the protein was determined by circular dichroism(CD).
Sanjib Senapati, Soumyadev Sarkar, Ratan Gachhui   +2 more
exaly   +3 more sources

Deacetylation of chitin oligosaccharides of dp 2–4 by chitin deacetylase from Colletotrichum lindemuthianum

Carbohydrate Research, 1997
Chitin oligosaccharides of degree of polymerization 2-4 were deacetylated by purified chitin deacetylase isolated from Colletotrichum lindemuthianum to give their corresponding breakdown products after purification by liquid chromatography. Data from FABMS analyses suggested that N,N',N",N"'-tetraacetylchitotetraose and N,N',N"-triacetylchitotriose ...
Ken Tokuyasu, Kiyoshi Hayashi, Mayumi Ohnishi-Kameyama   +2 more
exaly   +3 more sources

Yeast ascospore wall assembly requires two chitin deacetylase isozymes [PDF]

FEBS Letters, 1999
Chitin deacetylases are required for spore wall rigidity in Saccharomyces cerevisiae. Two chitin deacetylase genes (CDA1 and CDA2) have been identified in yeast.
Peter Briza, Vassilis Bouriotis
exaly   +2 more sources