Cloning and expression of the Rhizopus glucoamylase gene in yeast.

ASHKARI, Toshihiko; Nakamura, Norihisa; Tanaka, Yoshikazu; Kiuchi, Naoko; Shibano, Yuji; Tanaka, Takaharu; Amachi, Teruo; Yoshizumi, Hajime

doi:10.1271/bbb1961.49.2521

Cited by 9 publications

(4 citation statements)

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“…generally do not produce transglucosidase and thus have been widely used in the Amylo-process for conversion of starch to glucose with up to 100% efficiency (Yu and Hang 1991). The main advantage of glucoamylase derived from Rhizopus is that it exhibits a strong action on raw starch and its chemical properties, including optimum pH are well suited to the saccharification of cereal starch (Ashikari et al 1985). Three forms of glucoamylase were isolated from Rhizopus sp., Gluc 1, Gluc 2 and Gluc 3 (Takahashi et al 1985).…”

Section: Mold Glucoamylasesmentioning

confidence: 99%

“…Rhizopus oryzae has only one structural gene and its nucleotide sequence shows that the gene contains 4 introns and a signal sequence for 25 amino acids. The Rhizopus oryzae gene has been patented by Ashikari et al 1985.…”

Section: The Glucoamylase Multigene Familymentioning

confidence: 99%

“…Glucoamylases are abundant in many mold strains and a great deal of work has been done to clone fungal glucoamylase genes in Saccharomyces cerevisiae in order to develop an industrial strain which can produce ethanol from complex carbohydrates. Glucoamylase encoding genes have been cloned and sequenced from several filamentous fungi including Aspergillus niger (Boel et al 1984), Aspergillus awamori (Innis et al 1985), Aspergillus oryzae (Hata et al 1991), Aspergillus terreus (Ventura et al 1995), Neurospora crassa (Stone et al 1993), and Rhizopus oryzae (Ashikari et al 1985(Ashikari et al , 1986.…”

Section: Cloning Of Mold Glucoamylase Genesmentioning

confidence: 99%

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Glucoamylases: Microbial Sources, Industrial Applications and Molecular Biology ? A Review

James

Lee

1997

J Food Biochemistry

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Glucoamylase (EC 3.2.1.3) hydrolyzes polysaccharides from the nonreducing chain ends by cleaving α‐1,4 and α‐1,6 glycosidic bonds consecutively. Glucoamylases are used mainly in the production glucose syrup, high fructose corn syrup, and in whole grain and starch hydrolysis for alcohol production. This paper reviews the status of glucoamylases with respect to microbial sources, biochemical and physical properties. Methods used to assay glucoamylase activity are also compared, with reference being made to the specificity of spectrophotometric methods in detecting end products of the enzyme action. Commercial glucoamylases and development of immobilization techniques are discussed. Also, structural analysis of glucoamylase and the main amino acids involved in catalysis and starch binding are emphasized. The cloning of the glucoamylase gene in Saccharomyces cerevisiae for the brewing of low calorie beer is presented. This review highlights the use of glucoamylase in the food industry.

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Section: Mold Glucoamylasesmentioning

confidence: 99%

Section: The Glucoamylase Multigene Familymentioning

confidence: 99%

Section: Cloning Of Mold Glucoamylase Genesmentioning

confidence: 99%

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Glucoamylases: Microbial Sources, Industrial Applications and Molecular Biology ? A Review

James

Lee

1997

J Food Biochemistry

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“…kawachii (18), Aspergillus niger (9), Aspergillus oryzae (17), Aspergillus shirousamii (25), Hormoconis resinae (20), Humicola grisea var. thermoidea (cited in reference 4), Neurospora crassa (28), and Rhizopus oryzae (5). The nucleotide sequences of these genes clearly demonstrate an overall domain structure for the H. grisea, H. resinae, N. crassa, and Aspergillus glucoamylases, i.e., an N-terminal catalytic region and a C-terminal starch-binding domain.…”

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confidence: 87%