Cloning, expression, and nucleotide sequence of the alpha-amylase gene from the haloalkaliphilic archaeon Natronococcus sp. strain Ah-36

Kobayashi, Tetsuo; Kanai, Haruhiko; Aono, Rikizo; Horikoshi, Koki; Kudo, Toshiaki

doi:10.1128/jb.176.16.5131-5134.1994

Cited by 57 publications

(27 citation statements)

References 22 publications

(15 reference statements)

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“…The amylases from the mesophilic extremely halophilic Archaea, namely Halobacterium halobium (Good & Hartman, 1970) and Natronococcus amylolyticus (Kobayashi et al, 1992) and the moderately halophilic mesophilic aerobic bacterium Halomonas meridiana (Coronado et al, 2000a) have markedly different enzymic properties and range from being halotolerant enzymes, which are relatively stable and active at low salt concentrations, to extremely halophilic ones, which are inactivated at low salt concentrations. Studies have shown that the enzymes from Halomonas meridiana (Coronado et al, 2000b) and N. amylolyticus (Kobayashi et al, 1994), have significantly elevated levels of acidic amino acids but this characteristic is much more prevalent in the more halophilic N. amylolyticus amylase. In general, the amylase enzymes from mesophilic halophilic organisms may be of limited use in industrial starch-degrading applications as they are not active or stable at high temperatures (above 60 mC).…”

Section: Abbreviation : Dns Dinitrosalicylic Acidmentioning

confidence: 99%

Cloning, sequencing and expression of an α-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme a aThe GenBank accession number for the sequence reported in this paper is AF442961.

Mijts

Patel

2002

Microbiology

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A recombinant clone expressing an amylase was identified from an Escherichia coli generated genomic library of the thermophilic, moderately halophilic, anaerobic bacterium Halothermothrix orenii by activity screening, and the gene encoding the enzyme was designated AmyA. The amyA gene was 1545 bp long, and encoded a 515 residue protein composed of a 25 amino acid putative signal peptide and a 490 amino acid mature protein. It possessed the five consensus regions characteristic of the α-amylase family and showed the greatest homology to the Bacillus megaterium group of α-amylases. The amyA gene was expressed in E. coli as a hexahistidine-tagged enzyme and purified. The purified recombinant enzyme was optimally active at 65 SC in 5 % (w/v) NaCl at pH 75, with significant activity retained in the presence of up to 25 % (w/v) NaCl. It had a specific activity of 2232 U mg N1 and required NaCl and CaCl 2 for optimum activity and thermostability. The relatively high proportion of acidic amino acids typically observed for many enzymes from halophiles was absent in H. orenii AmyA.

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Section: Abbreviation : Dns Dinitrosalicylic Acidmentioning

confidence: 99%

Cloning, sequencing and expression of an α-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme a aThe GenBank accession number for the sequence reported in this paper is AF442961.

Mijts

Patel

2002

Microbiology

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“…strain Ah-36 awaits industrial exploitation. The enzyme exhibits maximal activity at 55°C, pH 8.7 and 2.5 M NaCl and hydrolyzes soluble starch, amylose, amylopectin and also glycogen, producing mainly maltotriose, with glucose and maltose as side products in negligible amounts (Kobayashi et al 1994). Most of the known archaeal pullulanases are Type II enzymes: they attack the α-1,6 glycosidic linkage in pullulan, producing maltotriose or, by α-1,4 glycosidic linkage, panose and isopanose, but they are inhibited by cyclodextrins.…”

Section: Archaeal Enzymes Of Biotechnological Interestmentioning

confidence: 99%

Perspectives on biotechnological applications of archaea

Schiraldi

Giuliano

Rosa

2002

Archaea

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Summary Many archaea colonize extreme environments. They include hyperthermophiles, sulfur-metabolizing thermophiles, extreme halophiles and methanogens. Because extremophilic microorganisms have unusual properties, they are a potentially valuable resource in the development of novel biotechnological processes. Despite extensive research, however, there are few existing industrial applications of either archaeal biomass or archaeal enzymes. This review summarizes current knowledge about the biotechnological uses of archaea and archaeal enzymes with special attention to potential applications that are the subject of current experimental evaluation. Topics covered include cultivation methods, recent achievements in genomics, which are of key importance for the development of new biotechnological tools, and the application of wild-type biomasses, engineered microorganisms, enzymes and specific metabolites in particular bioprocesses of industrial interest.

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“…Halophilic microorganisms are potential sources of enzymes uniquely adapted to activity at high salt concentrations with application in beverages, pharmaceutical and detergent industries (Kamekura et al 1992; Kobayashi et al 1994;Adams & Kelly 1995;Li et al 2002), leather industry (Birbir et al 1996) and food preservative industries (Ventosa et al 1995;Mellado et al 2003). However, no focused research has been undertaken.…”

Section: Introductionmentioning

confidence: 99%

Characterization of halophilic bacteria from environmental samples from the brackish water of Pulicat Lake, India

et al. 2011

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Culture dependent phenotypic characterization and 16S rDNA based phylogenetic analyses were applied to study the aerobic halophilic bacterial population present in the Pulicat brackish-water Lake of India. Five different media were employed for isolation of bacteria. A total of 198 morphotypes were recovered, purified and screened for salt tolerance in nutrient agar medium amended with 5-25% NaCl. Based on 16S rDNA restriction fragment length polymorphism analysis with three restriction endonucleases, 51 isolates tolerant to 5% or more NaCl were grouped into 29 clusters. Phylogenetic analysis using 16S rRNA gene sequences revealed that 29 strains could further be allocated into two clades: 19 to Firmicutes and 10 to γ-Proteobacteria. Firmicutes included low G+C Gram-positive bacteria related to family Bacillaceae, which included five genera Bacillus, Virgibacillus, Rummelibacillus, Alkalibacillus and Halobacillus. Another genera included in Firmicutes was Salimicrobium halophilum. In the γ-Proteobacteria group, all the isolates belonged to one genus Halomonas, represented by six different species Halomonas salina, H. shengliensis, H. salifodinae, H. pacifica, H. aquamarina and H. halophila. Most of the isolates exhibited cellulase, xylanase, amylase and protease activities.

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Cloning, expression, and nucleotide sequence of the alpha-amylase gene from the haloalkaliphilic archaeon Natronococcus sp. strain Ah-36

Cited by 57 publications

References 22 publications

Cloning, sequencing and expression of an α-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme a aThe GenBank accession number for the sequence reported in this paper is AF442961.

Cloning, sequencing and expression of an α-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme a aThe GenBank accession number for the sequence reported in this paper is AF442961.

Perspectives on biotechnological applications of archaea

Characterization of halophilic bacteria from environmental samples from the brackish water of Pulicat Lake, India

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