Molecular Cloning and Sequence Analysis of Two Distinct Halotolerant Extracellular Proteases from<i>Bacillus subtilis</i>FP-133

Takenaka, Shinji; Yoshida, Norimasa; Yoshida, Kenichi; Murakami, Shinichiro; Aoki, Kenji

doi:10.1271/bbb.100588

Cited by 11 publications

(11 citation statements)

References 25 publications

(36 reference statements)

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“…3B). AprE JK and SB4 showed sequences similar to AprE FP133, 3) which also showed a similar result for salt resistance. Some other amino acid residues, including N109, N243, E251, D197, N252, and 259D has been reported to be related to salt resistance.…”

Section: )mentioning

confidence: 57%

“…Some other amino acid residues, including N109, N243, E251, D197, N252, and 259D has been reported to be related to salt resistance. 3,14) We found that there was no difference between CN2 and 168 at these sites except for 259D, which was replaced by 259S in AprE CN2. It is not clear whether D 259S can cause low salt resistance to AprE, although our data indicate that CN2 had low resistance to NaCl.…”

Section: )mentioning

confidence: 64%

“…A number of AprE proteases have been purified and characterized, and their genes have been analyzed in view of their uses or potential applications in biotechnological fields. Strains of Bacillus species isolated from traditional fermented foods, such as Choggokkinase (CK) from Korean honggok-Jang and subtilisin DFE from Chinese Dou-chi, 2) and recently B. subtilis FP-133 3) and B. amyloliquefaciens CH51 always produce high activity of AprE proteases. 4) These proteases can be used in the detergent industry, food and feed processing, for medical purposes, and in other applications.…”

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confidence: 99%

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Molecular Cloning and Sequence Analysis of an Extracellular Protease from Four Bacillus subtilis Strains

Han

Shiwa

Itoh

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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confidence: 57%

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confidence: 64%

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confidence: 99%

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Molecular Cloning and Sequence Analysis of an Extracellular Protease from Four Bacillus subtilis Strains

Han

Shiwa

Itoh

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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“…The species of Bacillus described as halophilic to date are as follows: B. hemicentroti ( Chen et al , 2011 ); B. humanensis ( Chen et al , 2011 ); B. xianensis ( Sanchez-Porro et al , 2003 ; Schlegel et al , 1970 ); B. alkaliphilic ( Zhang et al. , 2012 ); B. halochares ( Pappa et al , 2010 ); B. chungangensis ( Cho et al , 2010 ) and B. subtilis ( Takenaka et al , 2011 ). Thus, the possibility that a new species of halophilic Bacillus was isolated from a compost process is noteworthy.…”

Section: Resultsmentioning

confidence: 99%

Halotolerant bacteria in the São Paulo Zoo composting process and their hydrolases and bioproducts

Oliveira¹,

Ramos²,

Marem³

et al. 2015

Braz. J. Microbiol.

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Halophilic microorganisms are able to grow in the presence of salt and are also excellent source of enzymes and biotechnological products, such as exopolysaccharides (EPSs) and polyhydroxyalkanoates (PHAs). Salt-tolerant bacteria were screened in the Organic Composting Production Unit (OCPU) of São Paulo Zoological Park Foundation, which processes 4 ton/day of organic residues including plant matter from the Atlantic Rain Forest, animal manure and carcasses and mud from water treatment. Among the screened microorganisms, eight halotolerant bacteria grew at NaCl concentrations up to 4 M. These cultures were classified based on phylogenetic characteristics and comparative partial 16S rRNA gene sequence analysis as belonging to the genera Staphylococcus, Bacillus and Brevibacterium. The results of this study describe the ability of these halotolerant bacteria to produce some classes of hydrolases, namely, lipases, proteases, amylases and cellulases, and biopolymers. The strain characterized as of Brevibacterium avium presented cellulase and amylase activities up to 4 M NaCl and also produced EPSs and PHAs. These results indicate the biotechnological potential of certain microorganisms recovered from the composting process, including halotolerant species, which have the ability to produce enzymes and biopolymers, offering new perspectives for environmental and industrial applications.

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“…Bacillus subtilis strain FP‐133 is a moderately halotolerant bacterium that was isolated from fermented fish paste and produces several halotolerant hydrolytic enzymes . Extracellular serine protease and metalloprotease from strain FP‐133 have been purified and characterized , and their genes have been cloned . Strain FP‐133 produces other extracellular hydrolytic enzymes, some of which are stable and retain activity under moderately high salt conditions, and are therefore expected to be useful industrial enzymes.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the native form and the carboxy‐terminally truncated halotolerant form of α‐amylases from Bacillus subtilis strain FP‐133

Takenaka

Miyatake

Tanaka

et al. 2015

J. Basic Microbiol.

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Two amylases, amylase I and amylase II from Bacillus subtilis strain FP-133, were purified to homogeneity and characterized. Their stabilities toward temperature, pH, and organic solvents, and their substrate specificities toward polysaccharides and oligosaccharides were similar. Under moderately high salt conditions, both amylases were more stable than commercial B. licheniformis amylase, and amylase I retained higher amylase activity than amylase II. The N-terminal amino acid sequence, genomic southern blot analysis, and MALDI-TOFF-MS analysis indicated that the halotolerant amylase I was produced by limited carboxy-terminal truncation of the amylase II peptide. The deduced amino acid sequence of amylase II was >95% identical to that of previously reported B. subtilis α-amylases, but their carboxy-terminal truncation points differed. Three recombinant amylases--full-length amylase corresponding to amylase II, an artificially truncated amylase corresponding to amylase I, and an amylase with a larger artificial C-terminal truncation--were expressed in B. subtilis. The artificially truncated recombinant amylases had the same high amylase activity as amylase I under moderately high salt conditions. Sequence comparisons indicated that an increased ratio of Asp/Glu residues in the enzyme may be one factor responsible for increasing halotolerance.

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Molecular Cloning and Sequence Analysis of Two Distinct Halotolerant Extracellular Proteases fromBacillus subtilisFP-133

Cited by 11 publications

References 25 publications

Molecular Cloning and Sequence Analysis of an Extracellular Protease from Four Bacillus subtilis Strains

Molecular Cloning and Sequence Analysis of an Extracellular Protease from Four Bacillus subtilis Strains

Halotolerant bacteria in the São Paulo Zoo composting process and their hydrolases and bioproducts

Characterization of the native form and the carboxy‐terminally truncated halotolerant form of α‐amylases from Bacillus subtilis strain FP‐133

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