• KSBB Journal
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• v.11 no.3
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• pp.311-316
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• 1996

The effects of polyethylene glycol (PEG) on glucoamylase production in recombinant Saccharomyces cerevisiae were studied. By PEG addition, the cell growth was not affected. However, the glucoamylase production was increased in all range of PEG molecular weights and concentrations. The optimal molecular weight of PEG was 6000 and the optimal concentration was 1g/L. Using these optimals, the extracellular glucoamylase activity was 23% higher in PEG-containing medium than that in medium without PEG.

• Korean Journal of Microbiology
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• v.14 no.2
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• pp.49-49
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• 1976

Enzyme activities, such as glucoamylase dextrinogenic amylase, cellulase, acid protase and neutral protease, of Rhizopus isolated from various substrates collected throughout South Korea are measured, and their enzyme activities are surveyed from taxonomical, ecological and physiological viewpoint. Effect of carbon sources and phytohormones on the amylalse production of Rhizopus are also measured. Among the 735 strains of Phizopus isolated, strain number 587 exhibiting most prominent dextrinogenic amylase and netral protease activity is selected as the best strain, and the strain number 673, 108, 329, 165 and 728 are seleted for their predominant cellulase, acid protease, glucoamylase, dextrinogenic amylase and neutral protease activities, respectively. R.acidus and R.nigricans which exhibited relatively higher callulalse activity, showed lower activities for both amylase. R.tritici exhibited higher protease activity. The relations between activities and various substrates of wild strains are not outstnading difference, although the strains isolated from inland region exhibited more or less higher amylase and cellulase activities, than those of coast region, generally. Lactose and dextrin are most effective carbon sources for glucoamylase and dextrinogenic amylase production of the Rhizopus niveus, respectively. Although all phytohormones tested are effective for production of amylase by the Rhizopus strains, except nicotinamide for glucoamylase production, biotin and ascorbate are most effective for dextrinogenic amylase and glucoamylase production, respectively.

• Korean Journal of Microbiology
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• v.14 no.2
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• pp.47-56
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• 1976

Enzyme activities, such as glucoamylase dextrinogenic amylase, cellulase, acid protase and neutral protease, of Rhizopus isolated from various substrates collected throughout South Korea are measured, and their enzyme activities are surveyed from taxonomical, ecological and physiological viewpoint. Effect of carbon sources and phytohormones on the amylalse production of Rhizopus are also measured. Among the 735 strains of Phizopus isolated, strain number 587 exhibiting most prominent dextrinogenic amylase and netral protease activity is selected as the best strain, and the strain number 673, 108, 329, 165 and 728 are seleted for their predominant cellulase, acid protease, glucoamylase, dextrinogenic amylase and neutral protease activities, respectively. R.acidus and R.nigricans which exhibited relatively higher callulalse activity, showed lower activities for both amylase. R.tritici exhibited higher protease activity. The relations between activities and various substrates of wild strains are not outstnading difference, although the strains isolated from inland region exhibited more or less higher amylase and cellulase activities, than those of coast region, generally. Lactose and dextrin are most effective carbon sources for glucoamylase and dextrinogenic amylase production of the Rhizopus niveus, respectively. Although all phytohormones tested are effective for production of amylase by the Rhizopus strains, except nicotinamide for glucoamylase production, biotin and ascorbate are most effective for dextrinogenic amylase and glucoamylase production, respectively.

• Microbiology and Biotechnology Letters
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• v.28 no.4
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• pp.195-201
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• 2000

Glucoamylase of Saccharomyces diastaticus is produced as a large precursor composed of signal peptide (21 amino acid residues), Thr and Ser-rich region and functional glucoamylase. To evaluate the utility of the glucoamylase signal peptide (GSP) for the secretion of foreign proteins, four types of GSP mutants (ml : Pro-18 longrightarrowLeu-18, m2 : Tyr-13 longrightarrowLeu, m3 : Ser-9longrightarrowLeu-9, m4 : Asn-5 longrightarrowPro-5) were constructed and secretion efficiency of each mutant was compared with that of native GSP by the expression and secretion of Bacillus subtilis CMCase under the control of GAP in N-terminal domain and hydrophobic domain. n mutant 4, a polar amino acid was replaced by a helix - breaking Pro residue. CMCase activity assay and Western blot analysis revealed that CMCase secretion by GSP mutants replaced by Leu were increased compared with native GSP. In the case of m2 and m3, the substitution of Leu for Tyr-13 and Ser-9 in the hydrophobic region resulted in a twofold increase in the extracellular CMCase activity.

• Korean Journal of Microbiology
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• v.30 no.5
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• pp.403-409
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• 1992

For the development of a glucanolytic yeast strain. the seceretion of endo-1.4-$\beta$-D-glucanase (CMCase) of Bacillus subtilis was performed in yeast using glucoamylase gene (STA1) of Saccharomyces diastaticus. A 1.7 kb-DNA fragment of STA1 gene containing authentic promoter, signal sequence, threonine serine-rich (TS) region and N-terminal region (98 amino acids) of mature glucoamylase was ligated to YEp 24. E. coli-yeast shuttle vector. And then. CMCase structural gene of B. subtilis was fused in frame with the 1.7 kb-DNA fragment of STA1 gene, resulting in recombinant plasmid pYES('24. Yeast transformant harboring pYESC24 had no CMCase activity. So. we deleted TS region and N-terminal region of mature glucoamylase existing between signal sequence and CMCase structural gene in pYESC24. consequently constructed recombinant plasmid pYESC11. The yeast transformed with the newly constructed recombinant plasmid pYESC11 efficiently secreted CMCase to extracellular medium. After 4 days culture. total CMCase activity of this transformant was 44.7 units/ml and over 93% of total CMCase activity was detected in culture supernatant.

• Culinary science and hospitality research
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• v.23 no.1
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• pp.95-102
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• 2017

This study was activity of ${\alpha}-amylase$, glucoamylase of liquid Nuruk prepared using liquid Nuruk (NK) and Aspergillus kawachii (AK), Aspergillus niger (AN), Aspergillus oryzae (AO), Monascus kaoliang (MK). To investigate the relationship between the enzymatic activity and the total sugar content of liquid Nuruk depending on the types of Nuruk molds and the degree of rice-polishing. The activity of ${\alpha}-amylase$ depending on the types of Nuruk molds was shown to be 8.82, 8.72 units/mL in AN and AK treatments in brown rice liquid Nuruk at 24 hours after incubation, as the degree of rice-polishing increased, the activity of ${\alpha}-amylase$ was significantly lower (p<0.05). When brown rice was incubated in AN, it showed 8.83 units/mL at 48 hours after incubation, which was the highest activity, but there was no significantly difference (p<0.05), as the degree of rice- polishing was higher, the activity of ${\alpha}-amylase$ was lower. The activity of glucoamylase depending on the degree of rice-polishing showed 3,013 units/mL in AO treatment in brown rice liquid Nuruk at 24 hours after incubation, and the enzymatic activity was significantly higher (p<0.05). As the degree of rice-polishing increased, the activity of glucoamylase decreased, so liquid brown rice Nuruk showed the highest enzymatic activity, liquid white rice Nuruk was the lowest enzymatic activity. The highest enzymatic activity appeared in liquid Nuruk with brown rice at 48 hours after incubation. The activity of ${\alpha}-amylase$, glucoamylase showed higher enzymatic productivity as the degree of rice-polishing was lower, and there was an inverse correlation with the total sugar content.

• Microbiology and Biotechnology Letters
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• v.18 no.6
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• pp.653-659
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• 1990

The gene encoding glucoamylase from Schwanniomyces cagtellii CBS 2863 was cloned and expressed in Saccharomyces cerevisiae. Southern blot analysis confirmed that this glucoamylase gene was derived from the genomic DNA of Schwanniomyces ccastellii and that no DNA fragments corresponding to 5.1 or 1.3 kb of Sch. casteltii DNA were detected in S. cereuisiae. The glucoamylase activity from S. cerevisiae transformant was approximately 2,000 times less than that of donor yeast. No expression was found in E. coti. The secreted glucoamylase from S. cerevisiae transformant was indistinguishable from that of Sch. eastellii on the basis of molecular weight and enzyme properties.

• Journal of Microbiology and Biotechnology
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• v.11 no.1
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• pp.13-16
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• 2001

Maltose and soluble starch were used as secondary sources of carbon for glucoamylase production by Aspergillus awamori in solid state fermentation. During batch cultivation, maltose above 2.5%(w/w) repressed glucoamylase production, but, by adding either 2.5% (w/w) maltose or 1.25% (w/w) soluble starch to fed-batch cultivations, glucoamylase activity was increased by 15% and 170% over standard medium, respectively. The data showed that maltose is a weak inducer of glucoamylase production in solid stat fermentation.

• Journal of the Korean Society of Food Science and Nutrition
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• v.40 no.8
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• pp.1179-1183
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• 2011

This study was conducted to investigate the quality characteristics, antioxidant activity, and ${\alpha}$-glucoamylase inhibitory activity of Dahyang, a Chungnam Agricultural Research & Extension Service's newly bred cultivar of brown button mushroom. Total phenolic compound contents of Dahyang and the no. 705 mushroom were 189${\pm}$12 mg% and 168${\pm}$8 mg%, respectively. The major free sugars in Dahyang were mannitol (3.11%), xylose (0.12%), and trehalose (0.08%). ${\beta}$-Glucan content was 28.34% in Dahyang and 26.55% in the no. 705 mushroom, respectively. Electron donating ability by DPPH in Dahyang and the no. 705 mushroom was 52.14% and 45.27% for the water extract, and 57.81% and 46.93% for the 80% ethanol extract, respectively. ${\alpha}$-Glucoamylase inhibitory activity in a 10 mg/mL concentration of water extract were was 33.25% in Dahyang and 29.22% in the no. 705 mushroom, respectively.

• Microbiology and Biotechnology Letters
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• v.44 no.3
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• pp.376-382
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• 2016

The amylolytic enzyme activities of nuruks collected or produced in this study were examined. A maximum α-amylase activity of 24,747.1 ± 777.7 units/mg protein was obtained for a nuruk incubated at a relative humidity of 40% at 30℃. A nuruk matured at a relative humidity of 50% at 25℃ showed the highest glucoamylase acitivity. Among the 98 fungal strains isolated from the nuruk exhibiting the highest amylolytic enzyme activities, 26 strains of Aspergillus oryzae and 18 strains of Rhizopus oryzae were identified. Rhizopus oryzae MBF345 showed an α-amylase activity of 36,724.9 ± 10.2 units/mg protein and a glucoamylase activity of 4,911.8 ± 48.1 SP. These values were 1.7-fold and 1.4-fold greater, respectively, than those of the control strain. Strain MBF345 was deposited as KCTC46312 in the Korean Culture Type Collection.