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Purification and characterization of cold-active endo-1,4-β-glucanase produced by Pseudoalteromonas sp. AN545 from Antarctica

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Chinese Journal of Oceanology and Limnology 2011年第5期29卷 1086-1092页

作者：沈继红阚光锋史翠娟雷振环解秋菊钱文佳 Key Laboratory of Marine Bio-active Substances State Oceanic Administration School of the Ocean Harbin Institute of Technology at Weihai

A bacterium hydrolyzing carboxymethylcellulose, isolated from Antarctic sea ice, was identified as Pseudoalteromonas sp. based on 16S rDNA gene sequences and named as Pseudoalteromonas sp. AN545. The extracellular endo-1,4-β-glucanase AN-1 was purified successively by ammonium sulfate precipitation, DEAE-Sepharose ion exchange chromatography and Sephadex G-75 gel filtration chromatography. The molecular mass of AN-1 was estimated to be 47.5 kDa utilizing SDS-PAGE and gel chromatography analysis. AN-1 could hydrolyze caboxymethylcellulose, avicel and β-glucan, but not cellobiose, xylan and p-Nitrophenyl-β-D-glucopyranoside. The optimal temperature and pH for the β-glucanase activity of AN-1 were determined to be at 30℃ and pH 6.0, respectively. AN-1 was stable at acidic solutions of pH 5.0-6.5 and temperatures below 30℃ for 1 h. Moreover, the specific activity was enhanced by Ca2＋ and Mg2., and inhibited by Cu2＋. The kinetic parameters Michaelis constant （Km） and maximum velocity （Vmax） of AN-1 were 3.96 mg/mL and 6.06×10-2 mg/（***）, respectively.

关键词： Pseudoalteromonas endo-l,4-β-glucanase cold-active enzyme Antarctic sea ice stability

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Molecular Cloning and Characterization of a New cold-active Extradiol Dioxygenase from a Metagenomic Library Derived from Polychlorinated Biphenyl-contaminated Soil

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Chemical Research in Chinese Universities 2012年第4期28卷 666-671页

作者： REN He-jun LU Yang ZHOU Rui DAI Chun-yan WANG Yah ZHANG Lan-ying Key Laboratory of Groudwater Resources and Environment Ministry of EducationCollege of Environment and ResourcesJilin UniversityChangehun 130021P.R.China Jilin Academy of Agricultural Sciences Changehun 130033P.R.China Institute of Virology and AIDS Research the First Hospital of Jilin UniversityChangchun 130061P.R.China

To find new extradiol dioxygenases（EDOs,EC 1.***.11.2）,a metagenomics library was constructed from polychlorinated biphenyl-contaminated soil and was screened for some dioxygenase with aromatic ring cleavage activity.A novel EDO,designated as BphC_A,was identified and heterologously expressed in Escherichia *** deduced amino acid sequence of BphC_A exhibited a homology of less than 60% with other known *** analysis of BphC_A suggests that the protein is a novel member of the EDO *** enzyme exhibits higher substrate affinity and catalytic efficiency toward 3-methylcatechol than toward 2,3-dihydroxybiphenyl or catechol,the preferred substrate of other known *** optimum activity of purified BphC_A occurred at pH=8.5 and 35 °C,and BphC_A showed more than 40% of its initial activity at 5 °*** activity of purified BphC_A was significantly induced by Mn^2＋ and slightly reduced by Al^3＋,Cu^2＋ and Zn^2＋.

关键词： Extradiol dioxygenase Metagenome cold-active enzyme Gene cloning Functional characterization

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Molecular cloning & Expression of the prolyl endopeptidase of Haliotis discus hannai

Molecular cloning & Expression of the prolyl endopeptidase o...

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华东地区生物化学与分子生物学学会联合会2017年学术交流会暨安徽省生物化学与分子生物学学会理事会议

作者： LI Yue HU Jianjian CAO Minjie College of food & biological engineering Jimei University

Prolyl endopeptidase,a new class of serine peptidases as a large cytosolic enzyme,plays important roles both in the degradation of proteins of aquatic products and,reported by recent researches,the regulation of nervous system since its property of the degradation on proline residues in short peptides.A type of prolyl endopeptidase from gonad of Haliotis discus hannai(Hdh-PEP) was identified and cloned by polymerase chain reaction(PCR) and rapid amplification of cDNA endings(RACE) *** full-length cDNA of Hdh-PEP was 3224 bp with an open reading frame of 2121 bp encoding a putative PEP of 706 amino acid residues(GenBank:KY214290).The coding sequence of Hdh-PEP was ligated into the pET-28 a vector and we successfully got the purified Hdh-PEP with a relatively high enzyme *** researches showed that the optimal temperature for Hdh-PEP is about15 ℃,on which retained a relative enzyme activity of nearly 60%in 5 ℃.Compared to Cyprinus carpio(optimal temperature of 35 ℃),Ctenopharyngodon idellus,(optimal temperature of 30 ℃) and Decapterus maruadsi(optimal temperature of 35 ℃),Hdh-PEP is of a lower optimal temperature and a wider range of activity in low temperature,which showed a potentiality of cold-active enzyme.

关键词： Prolyl endopeptidase Haliotis discus hannai recombined expression cold-active enzyme

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