The utilization of starch by yeasts

McCann, A. Kate; Barnett, James A.

doi:10.1002/yea.320020206

Cited by 45 publications

(20 citation statements)

References 68 publications

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“…This analog has been used with various regimens of mutagenesis to select carbon catabolite-derepressed mutants that produce amylolytic activity during growth on glucose (32). A few mutants of this type have been isolated from different Schwanniomyces species (6,20,30,39). To determine whether 2-deoxyglucose affects glucoamylase expression in the same way as glucose, cells adapted to minimal medium with 1% glucose were shifted to minimal medium containing 1% (wt/vol) 2-deoxyglucose, harvested at 30, 60, and 90 min, and analyzed for glucoamylase expression as described earlier (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The supernatant was carefully decanted, and the cell pellet was immediately frozen in a dry ice-methanol bath. To each 0.5-to 1.0-g (wet weight) pellet of frozen cells, the following were added: an equal volume of glass beads (0.5-mm diameter), 20 ,ul of 100% Sarkosyl (CIBA-GEIGY Corp.; nl 30), 20 ,ul of antifoam A (Sigma), 4.0 ml of 4 …”

Section: Methodsmentioning

confidence: 99%

“…Many yeast and fungi possess amylolytic enzymes (17,20). Glucoamylase appears to be the most versatile of these enzymes, cleaving terminal a-1,4 glucosidic bonds from the nonreducing ends of starch, dextrins, and maltose to release glucose.…”

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confidence: 99%

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Expression and regulation of glucoamylase from the yeast Schwanniomyces castellii

Dowhanick¹,

Russell²,

Scherer³

et al. 1990

J Bacteriol

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Expression of the 146-kilodalton (kDa) extracellular glucoamylase by the budding yeast Schwanniomyces castellii is induced by maltose and starch. By use of antiglucoamylase antisera, we found that this expression was regulated at the level of the mRNA, taking place within 30 min after exposure of yeast cells to the respective sugars. Polyacrylamide gel electrophoresis analysis of the in vitro-translated products of total RNA from maltose-treated cells established that the glucoamylase precursor was approximately 120 kDa in size. Stable glucoamylase transcript was not produced in cells exposed to glucose, 2-deoxyglucose, and heat shock. Cells exposed to these two sugars also degraded intracellular and extracellular glucoamylase. In the presence of sugars such as cellobiose, galactose, lactose, and xylose or in the absence of any carbohydrate, a low-level, constitutive-like expression of this preglucoamylase occurred. The nascent glucoamylase underwent at least two posttranslational modifications, resulting in a 138-kDa cell-associated form and the 146-kDa active form that was found free in the medium. These results suggest that glucoamylase expression is tightly regulated similarly to expression of the enzymes responsible for maltose metabolism in Saccharomyces yeasts.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Expression and regulation of glucoamylase from the yeast Schwanniomyces castellii

Dowhanick¹,

Russell²,

Scherer³

et al. 1990

J Bacteriol

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“…Numerous yeasts, beside Schwanniomyces spp., produce glucoamylases and/or cu-amylases [4]. Of these, the genes encoding the glucoamylase [5] and the cu-amylase [6] from Saccharomycopsis fibuiigera have been isolated and expressed in Saccharomyces cerevisiae.…”

Section: Introductionmentioning

confidence: 99%

Isolation and expression in Saccharomyces cerevisiae of a gene encoding an α‐amylase from Schwanniomyces castellii

et al. 1989

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A gene (SWA1) encoding an α‐amylase activity from Schwanniomyces castellii has been cloned and expressed, via yeast cloning vector YEp13, in Saccharomyces cerevisiae. By using a riboprobe which is internal to the SWA1 gene, a 1.55 kb transcript was detected in the poly(A)+ RNA from both Sw. castellii and a S. cerevisiae clone harboring the SWA1 gene. This transcript should, therefore, correspond to the SWA1 gene. In addition, the DNA strand determining the α‐amylase activity has been defined. Transcription of the SWA1 gene appears to be highly regulated in Sw. castellii, whereas it is constitutive in the S. cerevisiae harboring this gene.

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“…Starch-assimilation was found in a large number of ascomycetous and non-ascomycetous yeast species (De Mot et al 1984a,b). Yeasts from several genera, such as Ambrosiozyma, Arxula, Aureobasidium, Candida, Debaryomyces, Lipomyces, Saccharomyces, Saccharomycopsis (Endomycopsis) and Schwanniomyces, rank among the best producers of glucoamylases (Spencer-Martins & van Uden 1979;McCann & Barnett 1986;Chi et al 2009a,b). The detailed molecular studies have been done mainly on glucoamylases from Saccharomyces cerevisiae, S. cerevisiae var.…”

Section: Introductionmentioning

confidence: 99%

Yeast glucoamylases: molecular-genetic and structural characterization

Hostinová

Gašperík

2010

Biologia

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Glucoamylase is an extracellular enzyme produced mainly by microorganisms. It belongs to the commercially frequently exploited biocatalysts. The major application of glucoamylase is in the starch bioprocessing to produce glucose and in alcoholic fermentations of starchy materials. Filamentous fungi have been the source of glucoamylases for industrial purposes as well as an object of numerous research studies. Some yeasts also secrete a large amount of glucoamylase with biochemical characteristics slightly different from those of filamentous fungi. Modern biotechnological applications require glucoamylases of certain properties optimal for a given process. Novel biocatalysts can be prepared from already existing enzymes using techniques of protein engineering or directed evolution. Tailoring of a commercial glucoamylase requires knowledge, on a molecular level, of structure/function relationships of enzymes originating from various sources and having different catalytic properties. Sequences of the cloned genes, their recombinant expression and the tertiary structure determination of glucoamylase are prerequisite to obtain such information. The presented review focuses on molecular-genetic and structural aspects of yeast glucoamylases, supplemented with the basic biochemical characterization of the given enzymes.

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The utilization of starch by yeasts

Cited by 45 publications

References 68 publications

Expression and regulation of glucoamylase from the yeast Schwanniomyces castellii

Expression and regulation of glucoamylase from the yeast Schwanniomyces castellii

Isolation and expression in Saccharomyces cerevisiae of a gene encoding an α‐amylase from Schwanniomyces castellii

Yeast glucoamylases: molecular-genetic and structural characterization

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