Characterization of extracellular chitinase from Chitinibacter sp. GC72 and its application in GlcNAc production from crayfish shell enzymatic degradation

Gao, Cong; Zhang, Alei; Chen, Kequan; Hao, Zhikui; Jun-mao, Tong; Ouyang, Pingkai

doi:10.1016/j.bej.2015.02.010

Cited by 55 publications

(39 citation statements)

References 43 publications

(43 reference statements)

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“…So far, many microbial chitinases have been identified and characterized [1,12,13], whereas there is still few information on the chitinases from marine bacteria [10,11,14,15]. Two chitinases from marine bacterium Paenibacillus barengoltzii have been reported in our recent studies: PbChi70 is an endo type chitinase with a molecular mass of 70.6 kDa.…”

Section: Discussionmentioning

confidence: 97%

“…Generally, chitinases are optimally active in a temperature range of 20-50 o C and stable at the temperatures below 55 o C [1,13,24]). The optimal temperature of PbChi67 was found to be 60 °C (Fig.…”

Section: Discussionmentioning

confidence: 98%

“…[7], Bacillus cereus [9], Bacillus licheniformis [12], Chitinibacter sp. [13] and Pseudoaltermonas tunicata [14]. However, most of them are mesothermal or neutral chitinases, which could not meet the diverse requirements of harsh industrial environments.…”

Section: Introductionmentioning

confidence: 99%

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Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

Yan

Wang

et al. 2016

International Journal of Biological Macromolecules

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 98%

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Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

Yan

Wang

et al. 2016

International Journal of Biological Macromolecules

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“…Chitin is traditionally chemically degraded to GlcNAc and N-acetyl COS S using acid, which leads to toxicity and risks associated with serious pollution during the production process [13]. With increased environmental awareness, increasing attention has been paid to developing enzymatic hydrolysis of chitin using chitinolytic enzymes as catalysts because they are environmentally friendly and result in products with high bioactivity compared to classical chemical routes [14].…”

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confidence: 99%

A novel bacterial β-N-acetyl glucosaminidase from Chitinolyticbacter meiyuanensis possessing transglycosylation and reverse hydrolysis activities

Zhang

Zhou

et al. 2020

Preprint

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Abstract Background: N-acetyl glucosamine (GlcNAc) and N-acetyl chitooligosaccharides (N-acetyl COSs) exhibit many biological activities, and have been widely used in the pharmaceutical, agriculture, food, and chemical industries. Particularly, higher N-acetyl COSs with degree of polymerization from 4 to 7 ((GlcNAc)4−(GlcNAc)7) show good antitumor and antimicrobial activity, as well as possessing strong stimulating activity towards natural killer cells. Thus, it is of great significance to discover a β-N-acetyl glucosaminidase (NAGase) that can not only produce GlcNAc, but also synthesize N-acetyl COSs. Results: The gene encoding the novel β-N-acetyl glucosaminidase, designated CmNAGase, was cloned from Chitinolyticbacter meiyuanensis SYBC-H1. The deduced amino acid sequence of CmNAGase contains a glycoside hydrolase family 20 catalytic module that shows low identity (12−35%) with the corresponding domain of most well-characterized NAGases. The CmNAGase gene was highly expressed with an active form in Escherichia coli BL21 (DE3) cells. The specific activity of purified CmNAGase toward p-nitrophenyl-N-acetyl glucosaminide (pNP-GlcNAc) was 4,878.6 U/mg of protein. CmNAGase had a molecular mass of 92 kDa, and its optimum activity was at pH 5.4 and 40ºC. The Vmax, Km, Kcat, and Kcat/Km of CmNAGase for pNP-GlcNAc were 16,666.67 μmol min-1 mg-1, 0.50 μmol mL-1, 25,555.56 s-1, and 51,111.12 mL μmol-1 s-1, respectively. Analysis of the hydrolysis products of N-acetyl COSs and colloidal chitin revealed that CmNAGase is a typical exo-acting NAGase. Particularly, CmNAGase can synthesize higher N-acetyl COSs ((GlcNAc)3−(GlcNAc)7) from (GlcNAc)2−(GlcNAc)6, respectively, showed that it possesses transglycosylation activity. In addition, CmNAGase also has reverse hydrolysis activity toward GlcNAc, synthesizing various linked GlcNAc dimers. Conclusions: The observations recorded in this study that CmNAGase is a novel NAGase with exo-acting, transglycosylation, and reverse hydrolysis activities, suggests a possible application in the production of GlcNAc or higher N-acetyl COSs.

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“…Chitin is traditionally chemically degraded to GlcNAc and N-acetyl COS S using acid, which leads to toxicity and risks associated with serious pollution during the production process [9]. With increased environmental awareness, increasing attention has been paid to developing enzymatic hydrolysis of chitin using chitinolytic enzymes as catalysts because they are environmentally friendly and result in products with high bioactivity compared to classical chemical routes [10].…”

mentioning

confidence: 99%

A novel β-N-acetyl glucosaminidase from Chitinolyticbacter meiyuanensis possessing transglycosylation activity and its use in generating long-chain N-acetyl chitooligosaccharides

Zhang

Zhou

et al. 2020

Preprint

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Abstract Background: N-acetyl glucosamine (GlcNAc) and N-acetyl chitooligosaccharides (N-acetyl COSs) exhibit antitumor and antimicrobial activities, and have been widely used in the pharmaceutical, agriculture, food, and chemical industries. Thus, it is crucial to discover a NAGase that can both synthesize GlcNAc and N-acetyl COSs. Results: The gene encoding the novel β-N-acetyl glucosaminidase, designated CmNAGase, was cloned from Chitinolyticbacter meiyuanensis SYBC-H1. The deduced amino acid sequence of CmNAGase contains a glycoside hydrolase family 20 catalytic module that shows low identity with the corresponding domain of the well-characterized NAGases. CmNAGase gene was highly expressed with soluble form in Escherichia coli BL21 (DE3) cells, whereupon it had a specific activity of 4,878.6 U/mg of protein toward p-nitrophenyl-N-acetyl glucosaminide. CmNAGase had a molecular mass of 92 kDa, and its optimum activity was at pH 5.4 and 40ºC. The Vmax, Km, and Kcat of CmNAGase were 833.33 μmol·L-1 ·min-1, 10.9 mmol, and 6.37 ´ 108 mM·mg-1, respectively. Analysis of the hydrolysis products of N-acetyl chitooligosaccharides and colloidal chitin revealed that CmNAGase exhibits exo-acting activities. Particularly, it possesses transglycosylation activity, which can synthesize (GlcNAc)n+1 from (GlcNAc)n (n=1−6), respectively. In addition, CmNAGase also can catalyze GlcNAc to its dimers with various linked forms. Conclusions: The observations recorded in this study that CmNAGase is an exo NAGase with unique transglycosylation activity, suggests a possible application in the production of long-chain N-acetyl CHOs. This is first report of a bacterial NAGase, which can produce long-chain N-acetyl COSs via transglycosylation activity.

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Characterization of extracellular chitinase from Chitinibacter sp. GC72 and its application in GlcNAc production from crayfish shell enzymatic degradation

Cited by 55 publications

References 43 publications

Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

Purification and biochemical characterization of novel acidic chitinase from Paenicibacillus barengoltzii

A novel bacterial β-N-acetyl glucosaminidase from Chitinolyticbacter meiyuanensis possessing transglycosylation and reverse hydrolysis activities

A novel β-N-acetyl glucosaminidase from Chitinolyticbacter meiyuanensis possessing transglycosylation activity and its use in generating long-chain N-acetyl chitooligosaccharides

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