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

Lee, Yong Seok; Park, Inhye; Yoo, Ju-Soon; Chung, Sang-Min; Lee, Young Choon; Cho, Young-Su; Ahn, Soon‐Cheol; Kim, Cheol-Min; Choi, Yong-Lark

doi:10.1016/j.biortech.2006.09.048

Cited by 96 publications

(67 citation statements)

References 34 publications

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“…Additionally, H6SCChi-1 hydrolyzed acidic chitosan. Chitinase activity has been associated only with chitin and has not been demonstrated for chitosan (1,4). Our study showed that SCChi-1 isolated from B. atrophaeus SC081 functions as a chitinase hydrolyzing chitin and chitosan ( Fig.…”

Section: Determination Of Scchi-1 Chitinase Activitymentioning

confidence: 76%

“…1B-D). Similar to these chitinases, SCChi-1 is composed of three domains in the following order: a glycosyl hydrolase domain from Ser-34 to Pro-448 (1, 5, 9), a fibronectin 3 (Fn3) domain from Ser-458 to Thr-539 (1,3,10), and a chitin binding domain (ChiBD) from Lys-549 to Leu-582 (3,9). These domains contain consensus residues, as indicated in Fig.…”

Section: Cloning and Sequencing Of Chitinase Scchi-1mentioning

confidence: 99%

“…1C), the conserved Pro, Ser, and Thr residues are important for the degradation of insoluble and crystalline polysaccharides such as chitin. Several well-conserved Pro residues implies a proline-specific protease, and hydroxyamino acid residues such as Ser and Thr connect the catalytic domain and the chitin binding domain as a domain linker (1,3). Therefore, the Fn3 domain is found in several enzymes such as chitinases, cellulases, amylases, poly (3-hydroxybutyrate) depolymerases, and bacterial glycosyl hydrolases (10).…”

Section: Cloning and Sequencing Of Chitinase Scchi-1mentioning

confidence: 99%

“…In particular, bacteria produce various chitinases to digest chitin and utilize it as an energy source (3), and most of these chitinases have been isolated and characterized from Bacillus species (1,4,5). Bacillus species secrete a large number of chitinases into the medium, which complicate downstream processing and affect product stability (1,4).…”

Section: Introductionmentioning

confidence: 99%

“…Chitin, a highly insoluble biopolymer, is one of the most abundant organic compounds in nature (1). The enormous amounts of chitin that are continuously generated require disposal and recycling on a formidable scale.…”

Section: Introductionmentioning

confidence: 99%

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Overexpression and characterization of thermostable chitinase from Bacillus atrophaeus SC081 in Escherichia coli

Cho

Choi²,

Choi

2011

BMB Reports

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The chitinase-producing strain SC081 was isolated from Korean traditional soy sauce and identified as Bacillus atrophaeus based on a phylogenetic analysis of the 16S rDNA sequence and a phenotypic analysis. A gene encoding chitinase from B. atrophaeus SC081 was cloned in Escherichia coli and was named SCChi-1 (GQ360078). The SCChi-1 nucleotide sequences were composed of 1788 base pairs and 596 amino acids, which were 92.6, 89.6, 89.3, and 78.9% identical to those of Bacillus subtilis (ABG57262), Bacillus pumilus (ABI15082), Bacillus amyloliquefaciens (ABO15008), and Bacillus licheniformis (ACF40833), respectively. A recombinant SCChi-1 containing a hexahistidine tag at the amino-terminus was constructed, overexpressed, and purified in E. coli to characterize SCChi-1. H6SCChi-1 revealed a hydrolytic band on zymograms containing 0.1% glycol chitin and showed the highest lytic activity on colloidal chitin and acidic chitosan. The optimal temperature and pH for chitinolytic activity were 50 o C and pH 8.0, respectively. [BMB reports 2011; 44(3) : 193-198]

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Section: Determination Of Scchi-1 Chitinase Activitymentioning

confidence: 76%

Section: Cloning and Sequencing Of Chitinase Scchi-1mentioning

confidence: 99%

Section: Cloning and Sequencing Of Chitinase Scchi-1mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Overexpression and characterization of thermostable chitinase from Bacillus atrophaeus SC081 in Escherichia coli

Cho

Choi²,

Choi

2011

BMB Reports

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Marine Microbes as a Resource for Novel Enzymes

Suganya

Sudha

Mishra

et al. 2022

Role of Microbes in Industrial Products and Processes

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A thermophilic chitinase 1602 from the marine bacterium Microbulbifer sp. BN3 and its high‐level expression in Pichia pastoris

et al. 2020

Biotech and App Biochem

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Chitinases play an important role in many industrial processes, including the preparation of oligosaccharides with potential applications. In the present study, a 1,713 bp gene of Chi1602, derived from a marine bacterium Microbulbifer sp. BN3, encoding a GH18 family chitinase, was expressed at high levels in Pichia pastoris. Distinct from most of the marine chitinases, the recombinant chitinase 1602 exhibited maximal activity at 60 °C and over a broad pH range between 5.0 and 9.0, and was stable at 50 °C and over the pH range 4.0–9.0. The hydrolytic products derived from colloidal chitins comprised mainly (GlcNAc)2 and GlcNAc, indicating that rChi1602 is a GH18 processive chitinase in conformity with its hypothetical structure. However, rChi1602 showed traces of β‐N‐acetylglucosaminidase activity on substrates such as powder chitin, chitosan, and ethylene glycol chitin. The thermophilic rChi1602, which manifests adaptation to a wide pH range and can be expressed at a high level in P. pastoris, is advantageous for applications in industrial processes.

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

Cited by 96 publications

References 34 publications

Overexpression and characterization of thermostable chitinase from Bacillus atrophaeus SC081 in Escherichia coli

Overexpression and characterization of thermostable chitinase from Bacillus atrophaeus SC081 in Escherichia coli

Marine Microbes as a Resource for Novel Enzymes

A thermophilic chitinase 1602 from the marine bacterium Microbulbifer sp. BN3 and its high‐level expression in Pichia pastoris

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