Heterologous secretory expression of β-glucosidase from Thermoascus aurantiacus in industrial Saccharomyces cerevisiae strains

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Biochemical characterization and mechanism of action of a thermostable beta-glucosidase purified from Thermoascus aurantiacus.

An extracellular beta-glucosidase from Thermoascus aurantiacus was purified to homogeneity by DEAE-Sepharose, Ultrogel AcA 44 and Mono-P column chromatography. The enzyme was a homotrimer, with a monomer molecular mass of 120 kDa; only the trimer was optimally active at 80 degrees C and at pH 4.5. At 90 degrees C, the enzyme showed 70% of its optimal activity. It was stable at pH 5.2 and at tem...

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A specific short dextrin-hydrolyzing extracellular glucosidase from the thermophilic fungus Thermoascus aurantiacus 179-5.

The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal activity of 30 U/ml after 336 h of fermentation. In solid-state fermentation, the activity of the enzyme was 22 U/ml at 144 h in medium containing wheat bran and 5.8 U/ml at 48 h...

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Article history: Received on: 24/11/2015 Revised on: 04/12/2015 Accepted on: 23/01/2016 Available online: 28/05/2016 Beta-Glucosidases (BGS) are the group of hydrolase enzymes, involved in the degradation processes and many biological processes. Due to demand, intensive screening of BGS is required to explore the natural microbial source of BGS. The current study deals with isolation and identi...

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ژورنال

عنوان ژورنال: Brazilian Journal of Microbiology

سال: 2019

ISSN: 1517-8382,1678-4405

DOI: 10.1007/s42770-019-00192-1