Purification and characterization of a Bacillus cereus exochitinase

Wang, Shu Yi; Moyne, Anne Laure; Thottappilly, G.; Wu, Shaw Jye; Locy, Robert D.; Singh, Narendra K.

doi:10.1016/s0141-0229(00)00362-8

Cited by 83 publications

(54 citation statements)

References 21 publications

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“…6). The chosen genes corresponded to previously described factors implicated in bacterial virulence: thermolabile haemolysin (TLH) (Wong et al, 2012), metalloprotease (Mersni-Achour et al, 2014) and exochitinase (Wang et al, 2001). …”

Section: Expression Of Genes Encoding Potential Virulence Factors Durmentioning

confidence: 99%

Factors other than metalloprotease are required for full virulence of French Vibrio tubiashii isolates in oyster larvae

et al. 2015

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Vibrio tubiashii is a marine pathogen isolated from larval and juvenile bivalve molluscs that causes bacillary necrosis. Recent studies demonstrated the isolation of this species in a French experimental hatchery/nursery affecting Crassostrea gigas spat in 2007. Here, using larvae of C. gigas as an interaction model, we showed that the French V. tubiashii is virulent to larvae and can cause bacillary necrosis symptoms with an LD 50 of about 2.3¾10 3 c.f.u. ml "1 after 24 h.Moreover, complete or gel permeation HPLC fractionated extracellular products (ECPs) of this strain appeared toxic to larvae. MS-MS analysis of the different ECP fractions revealed the existence of an extracellular metalloprotease and other suspected virulence factors. This observation is also supported by the expression level of some potential virulence factors. The overall results suggest that the pathology caused by the French V. tubiashii in C. gigas oysters is caused by a group of toxic factors and not only the metalloprotease.

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Section: Expression Of Genes Encoding Potential Virulence Factors Durmentioning

confidence: 99%

Factors other than metalloprotease are required for full virulence of French Vibrio tubiashii isolates in oyster larvae

et al. 2015

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“…Chitinase는 N-acetyl-1,4-glucosamine을 가수분해하여 chitooligosaccharide를 생산해내는 endochitinase (EC 3.2.1.14) 와 chitin의 비환원성 말단으로부터 GlcNAc와 chitobiose를 생 산해내는 exochitinase 등 두가지 형태가 존재하는 것으로 알려 져 있다 (Chernin et al, 1998;Wang et al, 2001).…”

Section: Of the 169 Strains Of Microorganisms Stored In Polar And Alpunclassified

“…: Chitin은 N-acetylglucosamine (GlcNAc)의 β-1,4 결합의 polymer로 자연계에 풍부하게 존재하는 다당류(polysaccharide) 중 하나이다 (Dutta et al, 2004;El-Hamshary et al, 2008). 이러 한 chitin은 각종 갑각류의 외피, 곰팡이 등의 세포벽을 구성하는 성분이며, chitinase는 chitin을 가수분해하는 효소로서 박테리아 나 곰팡이와 같은 생물에서 많이 발견되고 있는데, chitinase 생 산 미생물들은 생물방제제로서의 활용가치가 높아 산업적으로 많이 이용되고 있다 (Howard et al, 2003).Chitinase는 N-acetyl-1,4-glucosamine을 가수분해하여 chitooligosaccharide를 생산해내는 endochitinase (EC 3.2.1.14) 와 chitin의 비환원성 말단으로부터 GlcNAc와 chitobiose를 생 산해내는 exochitinase 등 두가지 형태가 존재하는 것으로 알려 져 있다 (Chernin et al, 1998;Wang et al, 2001).극한의 환경에서 적응, 진화해온 극지 생물들은 산업적·의학 적 활용을 위해 신기능성 유전자원의 탐색을 위한 유용한 생물 소재로 각광받고 있다 (Nichols et al, 1999;Antranikian and Egorova, 2007;Huston, 2008) …”

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Characterization of a Chitinase Gene and Screening of Cold Active Chitinase from Polar Microorganisms

Park¹,

Kim²,

Lee³

et al. 2012

The Korean Journal of Microbiology

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Of the 169 strains of microorganisms stored in Polar and Alpine Microbial Collection of Korea Polar ResearchInstitute, 27 strains were selected for their chitinase activity on ZoBell plates supplemented with 0.4% colloidal chitin. Among them, PAMC 21693 strain have shown the highest chitinolytic enzyme activity toward pNP-(GlcNAc)1 at low temperature and the highest growth rate at 4℃. We cloned a full-length chitinase gene of 2,857 bp which contains an open reading frame of 2,169 bp encoding 872-amino acid polypeptide. Recombinant chitinase protein was expressed in E. coli and its molecular weight was confirmed 96 kDa. In this paper, we suggest the potential use of cold-active chitinase from polar microorganisms in the field of biotechnology.Keywords: chitinase, cold-active chitinase, iPCR, polar microorganisms, screening *For correspondence. E-mail: ickim@kopri.re.kr; Tel.: Chitin은 N-acetylglucosamine (GlcNAc)의 β-1,4 결합의 polymer로 자연계에 풍부하게 존재하는 다당류(polysaccharide) 중 하나이다 (Dutta et al., 2004;El-Hamshary et al., 2008). 이러 한 chitin은 각종 갑각류의 외피, 곰팡이 등의 세포벽을 구성하는 성분이며, chitinase는 chitin을 가수분해하는 효소로서 박테리아 나 곰팡이와 같은 생물에서 많이 발견되고 있는데, chitinase 생 산 미생물들은 생물방제제로서의 활용가치가 높아 산업적으로 많이 이용되고 있다 (Howard et al., 2003).Chitinase는 N-acetyl-1,4-glucosamine을 가수분해하여 chitooligosaccharide를 생산해내는 endochitinase (EC 3.2.1.14) 와 chitin의 비환원성 말단으로부터 GlcNAc와 chitobiose를 생 산해내는 exochitinase 등 두가지 형태가 존재하는 것으로 알려 져 있다 (Chernin et al., 1998;Wang et al., 2001).극한의 환경에서 적응, 진화해온 극지 생물들은 산업적·의학 적 활용을 위해 신기능성 유전자원의 탐색을 위한 유용한 생물 소재로 각광받고 있다 (Nichols et al., 1999;Antranikian and Egorova, 2007;Huston, 2008)

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“…G-1. Yi -Wang et al (2001) stated that the optimum temperature of exochitinase from Bacillus cereus was 35°C who it was lower than chitinase from isolate 99, but relatively similar to chitinase from Enterobacter sp. G-1.…”

Section: Discussionmentioning

confidence: 99%

“…G-1. Yi-Wang et al (2001) reported Bacillus cereus had a wide range of temperature stability, the range was from 4 to 70°C. The temperature stability of chitinase from isolate 99 and Enterobacter sp.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Extracellular Chitinase from Bacterial Isolate 99 and Enterobacter sp. G-1 from Matsue City, Japan

Mahata¹,

Dharma²,

Ryanto³

et al. 2008

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Purification and characterization of a Bacillus cereus exochitinase

Cited by 83 publications

References 21 publications

Factors other than metalloprotease are required for full virulence of French Vibrio tubiashii isolates in oyster larvae

Factors other than metalloprotease are required for full virulence of French Vibrio tubiashii isolates in oyster larvae

Characterization of a Chitinase Gene and Screening of Cold Active Chitinase from Polar Microorganisms

Characterization of Extracellular Chitinase from Bacterial Isolate 99 and Enterobacter sp. G-1 from Matsue City, Japan

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