Nucleotide sequence of the maltotetraohydrolase gene from <i>Pseudomonas saccharophila</i>

Zhou, Jianhua; Baba, Tadashi; Takano, Toshiya; Kobayashi, Shôichi

doi:10.1016/0014-5793(89)81056-7

Cited by 33 publications

(13 citation statements)

References 32 publications

(37 reference statements)

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“…The a-amylases of Pseudomonas stutzeri, Pseudomonas saccharophila and Pseudomonas sp. 7197 were all maltotetraose-forming enzymes (Fujita et al 1989;Zhou et al 1989). The Pseudomonas sp.…”

Section: Discussionmentioning

confidence: 99%

Psychrotrophic amylolytic bacteria from deep sea sediment of Prydz Bay, Antarctic: diversity and characterization of amylases

Zhang

Zeng

2007

World J Microbiol Biotechnol

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Seventeen psychrotrophic bacteria with coldadaptive amylolytic, lipolytic or proteolytic activity were isolated from deep sea sediment of Prydz Bay, Antarctic. They were affiliated with c-Proteobacteria (12 strains) and gram-positive bacteria (5 strains) as determined by 16S rDNA sequencing. The amylase-producing strains belonged to genus Pseudomonas, Rhodococcus, and Nocardiopsis. Two Pseudomonas strains, 7193 and 7197, which showed highest amylolytic activity were chosen for further study. The optimal temperatures for their growth and amylase-producing were between 15 and 20°C. Both of the purified amylases showed highest activity at 40°C and pH 9.0, and retained 50% activity at 5°C. The SDS-PAGE and zymogram activity staining showed that the molecular mass of strain 7193 and 7197 amylases were about 60 and 50 kDa respectively. The Pseudomonas sp. 7193 amylase hydrolyzed soluble starch into glucose, maltose, maltotriose, and maltotetraose, indicating that it had both activities of a-amylase and glucoamylase. The product hydrolyzed by Pseudomonas sp. 7197 amylase was meltotetraose.

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“…The a-amylases of Pseudomonas stutzeri, Pseudomonas saccharophila and Pseudomonas sp. 7197 were all maltotetraose-forming enzymes (Fujita et al 1989;Zhou et al 1989). The Pseudomonas sp.…”

Section: Discussionmentioning

confidence: 99%

Psychrotrophic amylolytic bacteria from deep sea sediment of Prydz Bay, Antarctic: diversity and characterization of amylases

Zhang

Zeng

2007

World J Microbiol Biotechnol

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“…Homology searches by protein blast indicated that AmyP (CAM98700) amino acid sequence showed 73% identities to glucan 1,4-alpha-maltotetraohydrolase precursor from Pseudomonas stutzeri A1501 (ABP81117) (Yan et al 2008), 72% to maltotetraose-forming amylase (AAA25707) from Pseudomonas stutzeri MO-19 (Fujita et al 1989), 72% to glucan 1,4-alpha-maltotetraohydrolase (CAA34708) from Pseudomonas saccharophila (Zhou et al 1989) and 67% to Glucan 1,4-alpha-maltotetraohydrolase (YP_00118 8621) from Pseudomonas mendocina ymp (unpublished). Four regions (I-IV) similar to G4-amylase which are conserved in a-amylases were also found in AmyP (Fig.…”

Section: Identification Of Strain 7193mentioning

confidence: 98%

Molecular cloning and expression of an extracellular α-amylase gene from an Antarctic deep sea psychrotolerant Pseudomonas stutzeri strain 7193

Zhang

Zeng

2010

World J Microbiol Biotechnol

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Psychrotolerant Pseudomonas stutzeri strain 7193 capable of producing an extracellular a-amylase was isolated from deep sea sediments of Prydz Bay, Antarctic. The 59678-Da protein (AmyP) was encoded by 1665-bp gene (amyP). The deduced amino acid sequence was identified with four regions, which are conserved in amylolytic enzymes and form a catalytic domain, and was predicted to be maltotetraose forming extracellular amylase by using the I-TASSER online server. Purification of AmyP amylases from both the recombinant of Escherichia coli Top 10 F 0 and strain 7193 was conducted. Biochemical characterization revealed that the optimal amylase activity was observed at pH 9.0 and temperature 40°C. The enzymes were unstable at temperatures above 30°C, and only retain half of their highest activity after incubation at 60°C for 5 min. Thin-layer chromatography analysis of the products of the amylolytic reaction showed the presence of maltotetraose, maltotriose, maltose and glucose in the starch hydrolysate.

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“…So far various maltooligosaccharide-forming enzymes have been reported from Pseudomonas spp. That is, genes coding for G4-, and GS-forming amylases have been cloned (Fujita et al, 1989: Zhou et al,1989: Shida et al:. 1992.…”

Section: Starch Hydrolysis With Cloned Amylasementioning

confidence: 99%

Cloning, sequencing and expression of the amylase isozyme gene from Pseudomonas sp. KFCC 10818

Kim

Jhon

et al. 1996

Biotechnol Lett

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Nucleotide sequence of the maltotetraohydrolase gene from Pseudomonas saccharophila

Cited by 33 publications

References 32 publications

Psychrotrophic amylolytic bacteria from deep sea sediment of Prydz Bay, Antarctic: diversity and characterization of amylases

Psychrotrophic amylolytic bacteria from deep sea sediment of Prydz Bay, Antarctic: diversity and characterization of amylases

Molecular cloning and expression of an extracellular α-amylase gene from an Antarctic deep sea psychrotolerant Pseudomonas stutzeri strain 7193

Cloning, sequencing and expression of the amylase isozyme gene from Pseudomonas sp. KFCC 10818

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