Purification and properties of .ALPHA.-glucosidase from Penicillium purpurogenum.

Yamasaki, Yudai; Suzuki, Yukio; Ozawa, Junjiro

doi:10.1271/bbb1961.40.669

Cited by 12 publications

(13 citation statements)

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“…racemosus, 11) Paecilomyces varioti, 12) and Penicillium spp. 13,14) degraded soluble starch to some extent. Their substrate speciˆcities are in contrast to those of fungal glucoamylases (EC 3.2.1.3), the other exo-type enDownloaded by [University of North Texas] at 08: 19 27 November 2014 zymes that act more eŠectively on a-glucans such as starch and glycogen.…”

Section: Purification and Characterization Of A Novelmentioning

confidence: 99%

Purification and Characterization of a Novel Fungal α-Glucosidase fromMortierella alliaceawith High Starch-hydrolytic Activity

Tanaka

Aki

Hidaka

et al. 2002

Bioscience, Biotechnology, and Biochemistry

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The fungal strain Mortierella alliacea YN-15 is an arachidonic acid producer that assimilates soluble starch despite having undetectable alpha-amylase activity. Here, a alpha-glucosidase responsible for the starch hydrolysis was purified from the culture broth through four-step column chromatography. Maltose and other oligosaccharides were less preferentially hydrolyzed and were used as a glucosyl donor for transglucosylation by the enzyme, demonstrating distinct substrate specificity as a fungal alpha-glucosidase. The purified enzyme consisted of two heterosubunits of 61 and 31 kDa that were not linked by a covalent bond but stably aggregated to each other even at a high salt concentration (0.5 M), and behaved like a single 92-kDa component in gel-filtration chromatography. The hydrolytic activity on maltose reached a maximum at 55 degrees C and in a pH range of 5.0-6.0, and in the presence of ethanol, the transglucosylation reaction to form ethyl-alpha-D-glucoside was optimal at pH 5.0 and a temperature range of 45-50 degrees C.

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Section: Purification and Characterization Of A Novelmentioning

confidence: 99%

Purification and Characterization of a Novel Fungal α-Glucosidase fromMortierella alliaceawith High Starch-hydrolytic Activity

Tanaka

Aki

Hidaka

et al. 2002

Bioscience, Biotechnology, and Biochemistry

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“…1) A Penicillium purpurogenum enzyme synthesizes mostly a-1,4-linked maltotriose from maltose. 2) There are few studies of the a-glucosidases that synthesize oligosaccharides containing a-1,2-, or a-1,3-glucosidic linkages (Fig. 1).…”

mentioning

confidence: 99%

Purification and Characterization of a New Type of α-Glucosidase fromPaecilomyces lilacinusThat Has Transglucosylation Activity to Produce α-1,3- and α-1,2-Linked…

Kobayashi¹,

Tokuda²,

Hashimoto

et al. 2003

Bioscience, Biotechnology, and Biochemistry

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“…Because only a-1,6-oligosaccharides were detected as transferase products, the conclusion was that the enzyme was capable only of glucosyl transfer via a-1,6-glucosidic bonds. The action pattern of B-4389 maltase seems distinct from those of microbial a-glucosidases that were able to synthesize a-1,4-oligosaccharides by glucosyltransferase activity (2,7,(32)(33)(34). Also, unlike many enzymes previously examined (4,7,(22)(23)(24), the enzyme from B. brevis was not able to synthesize the trisaccharide panose.…”

Section: Discussionmentioning

confidence: 84%

Extracellular Maltase of Bacillus brevis

McWethy

Hartman

1979

Appl Environ Microbiol

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Bacillus brevis NRRL B-4389 produced extracellular maltase (a-glucosidase; EC 3.2.1.20) only in the presence of short a-1,4-glucosidic polymers, such as maltose and maltotriose. An optimum medium was developed; it contained 2.5% maltose, 0.5% nonfat dry milk, 0.4% yeast extract, and 0.01% CaCl2. The enzyme was produced extracellularly during the logarithmic phase of growth; no cellbound activity was detected at any time. Partial purification of the maltase was accomplished by using diethylaminoethyl cellulose batch adsorption, ammonium sulfate precipitation, and Sephadex G-200 gel filtration. Maltase, isomaltase (oligo-1,6-glucosidase), and glucosyltransferase activities were purified 20.0-, 19.1-, and 11.5-fold, respectively. Some properties of the partially purified maltase were determined: optimum pH, 6.5; optimum temperature, 48 to 50°C; pH stability range, 5.0 to 7.0; temperature stability range, 0 to 50°C; isoelectric point, pH 5.2; and molecular weight, 52,000. The relative rates of hydrolysis of maltose (G2), maltotriose (G3), G4, methyl-aD -maltoside, G40, dextrin, and isomaltose were 100, 22, 12, 10, 10, 8, and 5%, respectively; the Km on maltose was 5.8 mM; Dglucose, p-nitrophenyl-aD -glucoside, and tris(hydroxymethyl) aminomethane were competitive inhibitors; transglucosylase activity of the enzyme on maltose resulted in the synthesis of isomaltose, isomaltotroise, and larger oligosaccharides. Maltases (a-glucosidases; EC 3.2.1.20) presently play an important role in the industrial production of glucose syrups used by the food industry. To the present, only two extracellular maltases from bacteria have been characterized in detail (9, 29). It was the purpose of this study to isolate a bacterium that produced extracellular maltase, to maximize enzyme production, and to purify and characterize the maltase. MATERIALS AND METHODS Isolation and mutagenesis. Over 100 isolates capable of producing extracellular maltase were obtained from soil samples by using the screening procedure of Wang et al. (30). An isolate that produced the most maltase in shake culture was identified as Bacillus brevis (S. J. McWethy, Ph.D. thesis, Iowa State University, Ames, 1977). The isolate was subjected repeatedly to N-methyl-N'-nitro-N-nitrosoguanidine mutagenesis (1). Conditions for mutagenesis were: 100 ,ug of N-methyl-N'-nitro-N-nitrosoguanidine per ml, pH 6.0 (0.05 M tris(hydroxymethyl)aminomethane [Tris]-maleate buffer), and 20 min of exposure at 35°C. Mutants were screened for extracellular maltase production (30), and a three-step mutant that produced elevated levels of maltase was selected for further study.

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Purification and properties of .ALPHA.-glucosidase from Penicillium purpurogenum.

Cited by 12 publications

References 1 publication

Purification and Characterization of a Novel Fungal α-Glucosidase fromMortierella alliaceawith High Starch-hydrolytic Activity

Purification and Characterization of a Novel Fungal α-Glucosidase fromMortierella alliaceawith High Starch-hydrolytic Activity

Purification and Characterization of a New Type of α-Glucosidase fromPaecilomyces lilacinusThat Has Transglucosylation Activity to Produce α-1,3- and α-1,2-Linked…

Extracellular Maltase of Bacillus brevis

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