Results 141 to 150 of about 1,561 (158)

Over-expression of a bacterial chitosanase gene in Yarrowia lipolytica and chitosan hydrolysis by the recombinant chitosanase

Journal of Molecular Catalysis B: Enzymatic, 2012
Abstract The bacterial strain OUC1 was found to be closely related to Pseudomonas sp. A-01. A chitosanase gene ( chi ) cloned from the marine bacterium Pseudomonas sp. OUC1 was over-expressed in Yarrowia lipolytica which is generally regarded as safe.
Guang-Lei Liu, Yang Li, Hai-Xiang Zhou, Zhen-Ming Chi, Catherine Madzak   +4 more
openaire   +1 more source

Chitosanase-Catalyzed Hydrolysis of 4-Methylumbelliferyl  -Chitotr ioside

Journal of Biochemistry, 1999
4-Methylumbelliferyl beta-chitotrioside [(GlcN)(3)-UMB] was prepared from 4-methylumbelliferyl tri-N-acetyl-beta-chitotrioside [(GlcNAc)(3)-UMB] using chitin deacetylase from Colletotrichum lindemuthianum, and hydrolyzed by chitosanase from Streptomyces sp. N174.
Y, Honda, M, Kirihata, T, Fukamizo, S, Kaneko, K, Tokuyasu, R, Brzezinski   +5 more
openaire   +2 more sources

Characterization of a Chitosanase fromAspergillus fumigatusATCC13073

Bioscience, Biotechnology, and Biochemistry, 2012
Chitosanase II was purified from the culture filtrate of Aspergillus fumigatus ATCC13073. The purified enzyme had a molecular mass of 23.5 kDa. The N-terminal amino acid sequence of chitosanase II was identical to those of other Aspergillus chitosanases belonging to glycoside hydrolase family 75.
Katsuaki, Hirano, Sitthinan, Arayaveerasid, Kiyohiko, Seki, David J, Adams, Masaru, Mitsutomi   +4 more
openaire   +2 more sources

Some citrus chitinases also possess chitosanase activities

Experientia, 1993
Several acidic chitinase and chitosanase isoforms were found in 4-week-old nonembryogenic sweet orange (‘Valencia’ [Citrus sinensis (L.) Osbeck]) callus tissue. Two isoforms (designated A1-CF1 and A1-CF2) were purified to homogeneity using HPLC size exclusion, anion exchange, and chromatofocusing techniques.
W. F. Osswald, J. P. Shapiro, R. E. McDonald, R. P. Niedz, R. T. Mayer   +4 more
openaire   +1 more source

Chitosanases in the autolysis of Mucor rouxii

Mycopathologia, 1985
The mycelium of Mucor rouxii reached a 50% degree of lysis after 50 days incubation, and was then stable with the incubation time. The pH of the medium was 4.3 when autolysis began, rising to pH 7.6 after 6 days of autolysis and remaining there for the duration of the experiment. Maximum degradation of mycelium occurs during the first days of autolysis.
Fuensanta Reyes, R. Lahoz, M. J. Martinez, C. Alfonso   +3 more
openaire   +1 more source

Rapid detection of chitosanase activity in chitosanase gene-transformed strains of Enterobacter cloacae by lytic infection of specific bacteriophages

Journal of General Plant Pathology, 2003
In combination with lytic infection by virulent phages, a simple method for monitoring transgenic strains of Enterobacter cloacae was developed in this study. First, 15 strains of E. cloacae were used as indicator bacteria to isolate virulent phages with different host ranges.
Yoshihiro Takikawa, Yuuki Ishii, Keiichi Fujiwara, Yoshinori Matsuda, Teruo Nonomura, Koji Kakutani, Yukio Tosa, Shigeyuki Mayama, Hideyoshi Toyoda   +8 more
openaire   +1 more source

Cloning, purification, and characterization of chitosanase from Bacillus sp. DAU101

Applied Microbiology and Biotechnology, 2006
A chitosanase-producing Bacillus sp. DAU101 was isolated from Korean traditional food. This strain was identified on the basis of phylogenetic analysis of the 16S rDNA sequence, gyrA gene, and phenotypic analysis. The gene encoding chitosanase (csn) was cloned and sequenced. The csn gene consisted of an open reading frame of 837 nucleotides and encodes
Y S, Lee, J S, Yoo, S Y, Chung, Y C, Lee, Y S, Cho, Y L, Choi   +5 more
openaire   +2 more sources

Yeast Cell-Surface Expression of Chitosanase fromPaenibacillus fukuinensis

Bioscience, Biotechnology, and Biochemistry, 2007
To produce chitoorigosaccharides using chitosan, we attempted to construct Paenibacillus fukuinensis chitosanase-displaying yeast cells as a whole-cell biocatalyst through yeast cell-surface engineering. The localization of the chitosanase on the yeast cell surface was confirmed by immunofluorescence labeling of cells.
Takeshi, Fukuda, Danya, Isogawa, Madoka, Takagi, Michiko, Kato-Murai, Hisashi, Kimoto, Hideo, Kusaoke, Mitsuyoshi, Ueda, Shin-Ichiro, Suye   +7 more
openaire   +2 more sources

[Advances in the structure and function of chitosanase].

Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2023
Chitosanases represent a class of glycoside hydrolases with high catalytic activity on chitosan but nearly no activity on chitin. Chitosanases can convert high molecular weight chitosan into functional chitooligosaccharides with low molecular weight. In recent years, remarkable progress has been made in the research on chitosanases.
Jie, Xie, Yubin, Li, Jingwei, Liu, Yan, Gou, Ganggang, Wang   +4 more
openaire   +1 more source

Purification and hydrolytic action of a chitosanase from Nocardia orientalis

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
Chitosanase from the culture filtrate of Nocardia orientalis was purified to apparent homogeneity by precipitation with ammonium sulfate followed by CM-Sephadex chromatography, biospecific affinity chromatography on a Sepharose CL-4B with immobilized chitotriose and by gel filtration on Sephadex G-75.
K, Sakai, R, Katsumi, A, Isobe, F, Nanjo
openaire   +2 more sources