Cloning and characterization of the constitutively expressed chitinase C gene from a marine bacterium, Salinivibrio costicola strain 5SM-1

Aunpad, Ratchaneewan; Panbangred, A. N. D. Watanalai

doi:10.1016/s1389-1723(04)70145-0

Cited by 32 publications

(17 citation statements)

References 32 publications

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“…By comparison with few studies on halo-tolerance of chitinases, same results of salt tolerant chitinase has been proved with others chitinases produced from halophilic bacteria such as Salinivibrio costicola 5SM-1 [23], Planococcus rifitoensis M2-26 [7]. As well as by the marine bacteria Vibrio harveyi and Alteromonas sp.…”

Section: Intracellular Physicochemical Chitinase Characterizationsupporting

confidence: 65%

Antimicrobial Behavior of Intracellular Proteins from Two Moderately Halophilic Bacteria: Strain J31 of Terribacillus halophilus and Strain M3- 23 of Virgibacillus marismortui

Essghaier¹,

Dhieb²,

Boudabous³

et al. 2014

J Plant Pathol Microbiol

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In the present study, we firstly aimed to determine the ability of halophilic bacteria to improve tomato growth. as well as to detect the antimicrobial activities from two moderately halophilic bacteria strain M3-23 of Virgibacillus marismortui and strain J31 of Terribacillus halophilus exhibited by their intracellular proteins. The results showed that both bacteria were able to improve stem tomato growth by comparison of untreated tomato. The halophilic bacteria were also able to produce intracellular antifungal enzyme: glucanase produced by V. marismortui (1.74U/mg) and chitinase (39.39U/mg) produced by T. halophilus. Both chitinases were halotolerants (active in the presence of (0% to 30% NaCl (w/v)). Chitinase produced by strain J31 was alcaline (pH optimum pH 12), but chitinase from strain M3-23 was acidic (pH 4 optimum) more than 90% and 80% of activities were retained in the presence of pH value from 4 to 12, respectively for strain J31 and M3-23. Both enzymes were thermotolerants; optimum temperature was 80°C and 90°C respectively for strain J31 and strain M3-23. Both strains have lysozyme activity and value ranging from 6.6 U/ml to 6.8 U/ml respectively for strain J31 and strain M3-23. On the whole, the most potent in vitro antifungal effect was demonstrated by intracellular compound produced by strain J31 compared to strain M3-23. This study, was the first showing the antimicrobial efficiency of moderately halophilic bacteria by means of their intracellular compounds, by means of the spore germination reduction and the destroy of mycelial growth of Botrytis cinerea, in vitro. The distinguishable characteristics of their intracellular halotolerant and thermotolerant chitinases make them as good candidates for biotechnological applications.

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Section: Intracellular Physicochemical Chitinase Characterizationsupporting

confidence: 65%

Antimicrobial Behavior of Intracellular Proteins from Two Moderately Halophilic Bacteria: Strain J31 of Terribacillus halophilus and Strain M3- 23 of Virgibacillus marismortui

Essghaier¹,

Dhieb²,

Boudabous³

et al. 2014

J Plant Pathol Microbiol

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“…Escherichia coli DH5a (pCHISI) harbours a chitinase C (ChiC) gene (Genbank accession number AF261749) from the marine bacterium, Salinivibrio costicola strains 5SM-1 (Aunpad and Panbangred, 2003). Recombinant (transfromant) E. coli were cultured in Luria-Bertani-medium (1% tryptone, 0.5% yeast extract and 0.5% NaCl) containing 50 µg/ml ampicillin at 37 o C under shaking at 200 rpm (New Brunswick Scientific, NJ, USA).…”

Section: Methodsmentioning

confidence: 99%

“…Salinivibrio costicola strain 5SM-1 is a moderately halophilic bacterium that was isolated from saline mud in Thailand (Aunpad and Panbangred, 2003). Salinivibrio costicola was originally isolated and described in 1938 from salted food (Mellado et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterisation of two forms of halo- and thermo-tolerant chitinase C ofSalinivibrio costicola expressed inEscherichia coli

et al. 2007

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Two forms of chitinase C (Chi-I and Chi-II) were purified until homogeneity from the culture supernatant of a transformant Escherichia coli harbouring chitinase C gene from the halophilic bacterium Salinivibrio costicola strain 5SM-1. Chi-II was derived from Chi-I by C-terminal processing. Chi-I and Chi-II showed similar salinity optimum at 1-2% NaCl and retained more than 80% of their activity at 3-5% NaCl and more than 50% residual activity at 14% NaCl. The two enzymes could also well function (activity > 95%) in the absence of NaCl. Both had highest activity at pH 7.0 and 50 o C and both were stable over a wide range of pH (3.0-10.0). More than 50% activity remained at 80 o C after 60 min treatment. Among 4 major cations contained in sea water, only Mg 2+ at 10 mM increased activity about 10%. Using p-nitrophenyl-N,N'-diacetylchitobiose as substrate, Chi-I and Chi-II had K m of 30 and 31.8 µM and V max of 10 and 9.2 µmol/h/mg protein, respectively. Chi-I and Chi-II were classified as exochitinases by product analysis of the E. coli culture supernatant with high performance liquid chromatography (HPLC) and thin-layer chromatography (TLC).

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“…O7, V. parahaemolyticus [125], Salinivibrio costicola [126] and Microbulbifer degradans [127]. Chitinase is responsible for hydrolyzing the β-1,4-glycosidic bond of different types of chitin.…”

Section: Chitinasementioning

confidence: 99%

Marine Microbiological Enzymes: Studies with Multiple Strategies and Prospects

2016

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Marine microorganisms produce a series of promising enzymes that have been widely used or are potentially valuable for our daily life. Both classic and newly developed biochemistry technologies have been broadly used to study marine and terrestrial microbiological enzymes. In this brief review, we provide a research update and prospects regarding regulatory mechanisms and related strategies of acyl-homoserine lactones (AHL) lactonase, which is an important but largely unexplored enzyme. We also detail the status and catalytic mechanism of the main types of polysaccharide-degrading enzymes that broadly exist among marine microorganisms but have been poorly explored. In order to facilitate understanding, the regulatory and synthetic biology strategies of terrestrial microorganisms are also mentioned in comparison. We anticipate that this review will provide an outline of multiple strategies for promising marine microbial enzymes and open new avenues for the exploration, engineering and application of various enzymes.

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Cloning and characterization of the constitutively expressed chitinase C gene from a marine bacterium, Salinivibrio costicola strain 5SM-1

Cited by 32 publications

References 32 publications

Antimicrobial Behavior of Intracellular Proteins from Two Moderately Halophilic Bacteria: Strain J31 of Terribacillus halophilus and Strain M3- 23 of Virgibacillus marismortui

Antimicrobial Behavior of Intracellular Proteins from Two Moderately Halophilic Bacteria: Strain J31 of Terribacillus halophilus and Strain M3- 23 of Virgibacillus marismortui

Biochemical characterisation of two forms of halo- and thermo-tolerant chitinase C ofSalinivibrio costicola expressed inEscherichia coli

Marine Microbiological Enzymes: Studies with Multiple Strategies and Prospects

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