Literature DB >> 9729602

Molecular and biotechnological aspects of microbial proteases.

M B Rao1, A M Tanksale, M S Ghatge, V V Deshpande.   

Abstract

Proteases represent the class of enzymes which occupy a pivotal position with respect to their physiological roles as well as their commercial applications. They perform both degradative and synthetic functions. Since they are physiologically necessary for living organisms, proteases occur ubiquitously in a wide diversity of sources such as plants, animals, and microorganisms. Microbes are an attractive source of proteases owing to the limited space required for their cultivation and their ready susceptibility to genetic manipulation. Proteases are divided into exo- and endopeptidases based on their action at or away from the termini, respectively. They are also classified as serine proteases, aspartic proteases, cysteine proteases, and metalloproteases depending on the nature of the functional group at the active site. Proteases play a critical role in many physiological and pathophysiological processes. Based on their classification, four different types of catalytic mechanisms are operative. Proteases find extensive applications in the food and dairy industries. Alkaline proteases hold a great potential for application in the detergent and leather industries due to the increasing trend to develop environmentally friendly technologies. There is a renaissance of interest in using proteolytic enzymes as targets for developing therapeutic agents. Protease genes from several bacteria, fungi, and viruses have been cloned and sequenced with the prime aims of (i) overproduction of the enzyme by gene amplification, (ii) delineation of the role of the enzyme in pathogenecity, and (iii) alteration in enzyme properties to suit its commercial application. Protein engineering techniques have been exploited to obtain proteases which show unique specificity and/or enhanced stability at high temperature or pH or in the presence of detergents and to understand the structure-function relationships of the enzyme. Protein sequences of acidic, alkaline, and neutral proteases from diverse origins have been analyzed with the aim of studying their evolutionary relationships. Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes. Deciphering these secrets would enable us to exploit proteases for their applications in biotechnology.

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Year:  1998        PMID: 9729602      PMCID: PMC98927          DOI: 10.1128/MMBR.62.3.597-635.1998

Source DB:  PubMed          Journal:  Microbiol Mol Biol Rev        ISSN: 1092-2172            Impact factor:   11.056


  271 in total

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Authors:  S Gottesman; M R Maurizi
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4.  Candida albicans aspartic proteinase: cDNA cloning and comparison among strains.

Authors:  S Y Murayama; O Takeda; H Mukai; K Takesako; E Sono; I Kato; H Yamaguchi
Journal:  Adv Exp Med Biol       Date:  1995       Impact factor: 2.622

5.  Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein.

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Journal:  J Bacteriol       Date:  1984-09       Impact factor: 3.490

6.  Sequence of the gene encoding a highly thermostable neutral proteinase from Bacillus sp. strain EA1: expression in Escherichia coli and characterisation.

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8.  Molecular cloning of the cDNA and gene for an elastinolytic aspartic proteinase from Aspergillus fumigatus and evidence of its secretion by the fungus during invasion of the host lung.

Authors:  J D Lee; P E Kolattukudy
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9.  Primary structure of Mucor miehei aspartyl protease: evidence for a zymogen intermediate.

Authors:  G L Gray; K Hayenga; D Cullen; L J Wilson; S Norton
Journal:  Gene       Date:  1986       Impact factor: 3.688

10.  Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalis.

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Journal:  FEBS Lett       Date:  1991-07-29       Impact factor: 4.124

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  243 in total

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3.  Purification and characterization of secretory serine protease from necrotrophic oomycete, Pythium myriotylum Dreschler.

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4.  Compatibility of alkaline xylanases from an alkaliphilic Bacillus NCL (87-6-10) with commercial detergents and proteases.

Authors:  B Kamal Kumar; H Balakrishnan; M V Rele
Journal:  J Ind Microbiol Biotechnol       Date:  2004-02-19       Impact factor: 3.346

Review 5.  Development of soil microbiology methods: from respirometry to molecular approaches.

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Journal:  J Ind Microbiol Biotechnol       Date:  2010-11-18       Impact factor: 3.346

6.  Purification and stability characteristics of an alkaline serine protease from a newly isolated Haloalkaliphilic bacterium sp. AH-6.

Authors:  M S Dodia; C M Rawal; H G Bhimani; R H Joshi; S K Khare; S P Singh
Journal:  J Ind Microbiol Biotechnol       Date:  2007-11-10       Impact factor: 3.346

7.  Physiology of biofilms of thermophilic bacilli-potential consequences for cleaning.

Authors:  S G Parkar; S H Flint; J D Brooks
Journal:  J Ind Microbiol Biotechnol       Date:  2003-08-28       Impact factor: 3.346

8.  Quorum sensing inhibitory effect of bergamot oil and aspidosperma extract against Chromobacterium violaceum and Pseudomonas aeruginosa.

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9.  Modulation of the Bacillus anthracis secretome by the immune inhibitor A1 protease.

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10.  Improving Production of Protease from Pseudoalteromonas sp. CSN423 by Random Mutagenesis.

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