Results 171 to 180 of about 2,147 (208)
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Chitosanases in the autolysis of Mucor rouxii
Mycopathologia, 1985The 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 +3 more
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Multiple forms of chitosanase activities
Phytochemistry, 1992Abstract Leaf, seed and fruit crude extracts from several species were tested for chitosanase activity using a polyacrylamide gel assay. Chitosanase activity was found in higher and in lower plant species. Depending on extracts, one to six acidic isoforms and one to three basic isoforms could be detected.
Souad El Ouakfaoui, Alain Asselin
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Diversity of chitosanase activity in cucumber
Plant Science, 1992Abstract Chitosanase activity was studied in different organs of cucumber ( Cucumis sativus L.) during development by polyacrylamide gel electrophoretic assays. Some chitosanase forms were present in leaves, roots, flowers, fruits and seeds. Up to five acidic and four basic forms were detected in the various extracts.
Souad El Ouakfaoui, Alain Asselin
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Properties of Chitosanase from Bacillus cereus S1
Current Microbiology, 2000Chitosanase from Bacillus cereus S1 was purified, and the enzymatic properties were investigated. The molecular weight was estimated to 45,000 on SDS-PAGE. Optimum pH was about 6, and stable pH in the incubation at 40 degrees C for 60 min was 6-11. This chitosanase was stable in alkaline side.
M, Kurakake +4 more
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Chitosanase from Streptomyces griseus
1988Publisher Summary This chapter describes the assay method and procedure for the purification of chitosanase from Streptomyces griseus. The assay is based on the estimation of amino sugars produced in the hydrolysis of glycol chitosan, a water-soluble derivative of chitosan, by the method of Rondle and Morgan, s using glucosamine as a reference ...
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Uncoupling chitosanase production from chitosan
Bioengineered Bugs, 2011There is a growing interest in chitosanases as enzymatic tools to hydrolyze chitosan into bioactive forms: low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS). However chitosanases are still expensive and methods of large-scale production of these enzymes are not yet established.
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Chitosanase from Bacillus species
1988Publisher Summary Several chitosanases have been isolated from some microorganisms, including fungi, bacteria, and actinomycetes. This chapter discusses the assay method and isolation procedure for chitosanase from Bacillus species. The assay is based on the estimation of reducing sugars produced in the hydrolysis of soluble chitosan by a ...
Yasushi Uchida, Akira Ohtakara
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[Advances in the structure and function of chitosanase].
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2023Chitosanases 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 +4 more
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Quantitative fluorometric analysis of plant and microbial chitosanases
Analytical Biochemistry, 1992A quantitative fluorometric assay for chitosanase activity in bacterial and plant tissues was developed. The assay can be conducted with either finely milled preparations of chitosan in suspension or dissolved chitosan; activity is based on measurements of glucosamine (GlcN) or oligomers of GlcN.
W F, Osswald +4 more
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Characteristics of chitosanases fromAspergillus fumigatus KB-1
Archives of Pharmacal Research, 2003Two chitosanases produced by Aspergillus fumigatus KB-1 were purified by ion exchange and size exclusion chromatographies. Molecular weights of chitosanases were 111.23 kDa (chitosanase I) and 23.38 kDa (chitosanase II). The N-terminal amino acid sequence of chitosanase II was determined as follows: YNLPNNLKQIYDKHKGKXSXVLAKGFTN.
Tae Kyoung, Eom, Kang Man, Lee
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