Characterization of an alkalophilic extracellular chitosanase from Bacillus cereus GU-02

Goo, Bon Geun; Park, Jae Kweon

doi:10.1016/j.jbiosc.2013.11.005

Cited by 18 publications

(8 citation statements)

References 32 publications

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“…The optimum pH range for both isoforms is 3 to 4, and they retain 70% to 100% relative activity between pH 3 and 6 (Hsu, Chung, Chang, & Sung, 2012). Alkaline chitosanases have also been found, such as the chitosanase from Bacillus cereus GU-02 (optimum pH 9) (Goo & Park, 2014). The optimum temperatures for chitosanases activity are related to their sources and normally in the range 40 • C to 60 • C. Two thermally stable chitosanase isoforms were purified from the sheaths of chitosan-treated bamboo shoots, and their optimal temperatures were 70 • C and 60 • C, respectively (Hsu et al, 2012).…”

Section: Biochemical Properties and Catalytic Mechanismsmentioning

confidence: 99%

Section: Marine‐polysaccharide Degrading Enzymesmentioning

confidence: 99%

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Marine‐polysaccharide degrading enzymes: Status and prospects

Sun

Gao

Xue

et al. 2020

Comp Rev Food Sci Food Safe

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Marine-polysaccharide degrading enzymes have recently been studied extensively. They are particularly interesting as they catalyze the cleavage of glycosidic bonds in polysaccharide macromolecules and produce oligosaccharides with low degrees of polymerization. Numerous findings have demonstrated that marine polysaccharides and their biotransformed products possess beneficial properties including antitumor, antiviral, anticoagulant, and anti-inflammatory activities, and they have great value in healthcare, cosmetics, the food industry, and agriculture. Exploitation of enzymes that can degrade marine polysaccharides is in the ascendant, and is important for high-value use of marine biomass resources. In this review, we describe research and prospects regarding the classification, biochemical properties, and catalytic mechanisms of the main types of marine-polysaccharide degrading enzymes, focusing on chitinase, chitosanase, alginate lyase, agarase, and carrageenase, and their product oligosaccharides. The state-of-the-art discussion of marine-polysaccharide degrading enzymes and their properties offers information that might enable more efficient production of marine oligosaccharides. We also highlight current problems in the field of marine-polysaccharide degrading enzymes and trends in their development. Understanding the properties, catalytic mechanisms, and modification of known enzymes will aid the identification of novel enzymes to degrade marine polysaccharides and facilitation of their use in various biotechnological processes. K E Y W O R D S agarase, alginate lyase, carrageenase, chitinase, chitosanase 1 INTRODUCTION Ocean occupies >70% of the global surface, and the vast oceanic water environment has spawned large and complex marine ecosystems with rich biodiversity. There is a wide variety of marine resources, however, they are largely unexploited. This situation makes the marine environment very attractive for bioprospecting to discover new functions and molecules (Arnaud-Haond, Arrieta, & Duarte, 2011). Research into marine compounds, especially polysaccharides from renewable biomass, is attracting increasing attention. Polysaccharides make up one of the largest

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Section: Biochemical Properties and Catalytic Mechanismsmentioning

confidence: 99%

Section: Marine‐polysaccharide Degrading Enzymesmentioning

confidence: 99%

Marine‐polysaccharide degrading enzymes: Status and prospects

Sun

Gao

Xue

et al. 2020

Comp Rev Food Sci Food Safe

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“…Some bioactive chitooligosaccharides have anti‐inflammatory , antihypertensive, antitumor , antimicrobial , and antioxidant effects. Functional properties of chitooligosaccharides are strongly related to their molecular weights . Most bacterial chitinases have been prepared from Serratia , Chromobacterium , Klebsiella , Bacillus , and Streptomyce s genus .…”

Section: Introductionmentioning

confidence: 99%

Characterization of a chitinase from Salinivibrio sp. BAO‐1801 as an antifungal activity and a biocatalyst for producing chitobiose

2018

J Basic Microbiol

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Salinivibrio genus is commonly found in salted seafood products. In this study, chitinase produced by Salinivibrio sp. BAO-1801 isolated from salted fermented shrimp was purified and subsequently characterized. The molecular weight of BAO-1801 chitinase was approximately 94.2 kDa by SDS-PAGE analysis. It was classified as a chitinase C based on homology analysis of its N-terminal amino acid residues. This strain BAO-1801 chitinase was then used for synthesis of (GlcNAc)2. Degradation of colloidal chitin and N-acetyl chitooligosaccharides by BAO-1801 chitinase was then analyzed and (GlcNAc)2 was identified as the main product by thin layer chromatography and high-performance liquid chromatography. Effects of temperature and pH on activity and stability of BAO-1801 chitinase were also investigated. Furthermore, this enzyme inhibited fungal growth in a dose-dependent manner. Taken together, these results suggest that this Salinivibrio or its chitinase can be used for the enzymatic degradation of chitin to produce chitobiose in industrial process.

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“…The application of chitosanase can be divided into several kinds. An alkalophilic extracellular chitosanase (pH 10 medium) was obtained from B. cereus and the corresponding COS were prepared (28) . The Exo-and endo-chitosanase were obtained from Gongronella butleri (9) and B.…”

Section: Application and Puri Cation Of Chitosanasementioning

confidence: 99%

Increasing chitosanase production in Bacilluse cereus by a novel mutagenesis and screeen method

Zhang

Zhao

2020

Preprint

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Background Chitosan hydrolysis by chitosanase is one of the most effective methods to produce chitosan oligosaccharides, however, the low yield of chitosanase cannot meet the current requirement. In this paper, a strain producing chitosanase was screened, and a novel mutagenesis system (1)) was selected to increase the yield of chitosanase. The hydrolyzed products from chitosan by chitosanase produced by mutan train were also analyzed by LC-MS. Results A strain of Bacillus cereus capable of producing chitosanase was screened and identified from soil samples. A mutant strain of Bacillus cereus was obtained by ARTP mutagenesis and bioscreening method, and chitosanase activity was 2.49 folds that of the original bacteria. After optimized fermentation conditions, the enzyme activity of the mutant strain was 3.3 folds that of the original bacteria. The relative molecular weight of the purified chitosanase was 43 kDa. Ten chitosan oligosaccharides(2–4 oligosaccharides) were obtained by hydrolyzing chitosan with it. Conclutions: The results showed that the ARTP mutagenesis and bioscreening method could significantly increase the yield of chitosanase in B. cereus, and had little effect on the properties of the enzyme. These findings have potential applications in mutagenesis of other enzyme-producing microorganisms.

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Characterization of an alkalophilic extracellular chitosanase from Bacillus cereus GU-02

Cited by 18 publications

References 32 publications

Marine‐polysaccharide degrading enzymes: Status and prospects

Marine‐polysaccharide degrading enzymes: Status and prospects

Characterization of a chitinase from Salinivibrio sp. BAO‐1801 as an antifungal activity and a biocatalyst for producing chitobiose

Increasing chitosanase production in Bacilluse cereus by a novel mutagenesis and screeen method

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