Purification and Some Properties of a Novel <i>α</i>-Amylase Produced by a Strain of <i>Thermoactinomyces vulgaris</i>

Shimizu, Mizuho; Kanno, Mutsuo; Tamura, Masaki; Suekane, Mikio

doi:10.1080/00021369.1978.10863231

Cited by 12 publications

(13 citation statements)

References 4 publications

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“…Previous studies and the results obtained in this study indicate that neopullulanase, maltogenic amylases, CDases and Thermoactinomyces vulgaris amylase II share similar, if not identical, substrate specificities, catalytic properties, protein sequences [26–28] and probably tertiary structures [29]. Therefore, these enzymes are likely to constitute a subfamily of glycoside hydrolase family 13.…”

Section: Discussionmentioning

confidence: 62%

Catalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose

Cheong

Kim

Yoon

et al. 2002

Biotech and App Biochem

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Multi-substrate specificity of neopullulanase towards cyclodextrin, acarbose and maltose was investigated using a clone originating from Bacillus stearothermophilus IMA6503. The enzyme purified from Escherichia coli harbouring the corresponding nplA gene hydrolysed beta-cyclodextrin (beta-CD) to maltose and glucose. It exhibited substrate preference for beta-CD, starch and pullulan in the proportions of 10.4:1.2:1. The enzyme not only hydrolysed acarbose, an alpha-amylase inhibitor, to a pseudotrisaccharide (PTS) and glucose, but also transferred PTS to glucose, forming isoacarbose. Moreover, it hydrolysed maltose to glucose and transferred the glucose to another maltose molecule to form panose when maltose was present at a low concentration (0.5%) in the reaction solution. The enzyme catalysed condensation between two maltose molecules and subsequent hydrolysis of the resulting 6(2)-O-alpha-maltosyl-maltose to glucose and panose, when maltose concentration was increased to 20%. Neopullulanase was likely to be present in monomer-dimer equilibrium with a molar ratio of 1:9 in 50 mM sodium acetate buffer (pH 6.0). The association-dissociation equilibrium of neopullulanase was shifted to monomerization by KCl. When the content of monomer increased in the reaction mixture, the specific activity towards soluble starch increased to 150%, while that towards beta-CD decreased to 80%. Therefore, multi-substrate specificity of neopullulanase was likely to be modulated by the shift of monomer-dimer association equilibrium.

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Section: Discussionmentioning

confidence: 62%

Catalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose

Cheong

Kim

Yoon

et al. 2002

Biotech and App Biochem

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“…This enzyme is markedly similar to the maltogenic a-amylases of B. stearothermophilus KP 1064 (Suzuki & Imai, 1985) and Thermoactinomyces vulgaris in terms of substrate specificity (Shimizu et al, 1978;Sakano et al, 1982a). This enzyme is markedly similar to the maltogenic a-amylases of B. stearothermophilus KP 1064 (Suzuki & Imai, 1985) and Thermoactinomyces vulgaris in terms of substrate specificity (Shimizu et al, 1978;Sakano et al, 1982a).…”

Section: New Enzymes Possessing Both «-Amylase and Puuulanase Activitiesmentioning

confidence: 73%

“…3. ) Takasaki (1989) Takasaki (1976) Shinke et al (1979a, Namori et al (1983) Napier (1977, Shimizu et al (1978), Sakano et al (1982a) Hidaka & Adachi (1980) Fairbairn et al (1985) Hyslop & Sleeper (1964), Brosnan et al (1989) Doyle et al (1989 Wako et al. B. stearothermophilus.…”

Section: Maltose-producing Enzymesmentioning

confidence: 99%

“…No. a-Amylase of Thermoactinomyces vulgaris (Shimizu et al, 1978;Sakano et al, 1982a) possessed both a-l,4-and a-l,6hydrolysing activities and gave maltose (74%) and glucose (12%) from starch and produced panose (97%) exclusively from pullulan. It was stable in the pH range 5-10 and retained 74% activity after 30 min at 100°C (Obi & Odibo, 1984).…”

Section: New Maltose-producing Amylases Of Actinomycetesmentioning

confidence: 99%

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Microbial Enzymes and Biotechnology

Fogarty¹,

Kelly²

1990

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“…vulgaris was cultivated using the same method as Shimizu et al 5 ) Genomic DNA was prepared from T. vulgaris cells as described by…”

Section: Cloning Of the Tv A II Gene By Screening Of Amylase-producinmentioning

confidence: 99%

A Neopullulanase-typeα-Amylase Gene fromThermoactinomyces vulgarisR-47

Tonozuka

Ohtsuka

Mogi

et al. 1993

Bioscience, Biotechnology, and Biochemistry

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Purification and Some Properties of a Novel α-Amylase Produced by a Strain of Thermoactinomyces vulgaris

Cited by 12 publications

References 4 publications

Catalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose

Catalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose

Microbial Enzymes and Biotechnology

A Neopullulanase-typeα-Amylase Gene fromThermoactinomyces vulgarisR-47

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