• Microbiology and Biotechnology Letters
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• v.47 no.3
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• pp.364-371
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• 2019

The use of GRAS microorganisms isolated from fermented foods during amylase production using an economical food-waste medium provides more opportunities to produce amylase with a wider range of applications. Hence, this study aimed to isolate a good amylase-producing fungi from the traditional Indonesian fermented cassava, gatot, and to identify the amylase-producing capability of the isolate in a potato peel waste (PPW) medium. Black-colored fungi isolated from gatot was morphologically identified and the amylase produced was characterized using SDS-PAGE and Native PAGE. The isolate was then grown on PPW medium, and the amylase produced was further characterized. Morphological identification and enzyme characterization revealed that the Aspergillus niger aggregate F isolated from gatot secreted an active extracellular ${\alpha}$-amylase with an optimum pH of 5-6. In conclusion, Aspergillus niger aggregate F isolated from gatot can be used to produce ${\alpha}$-amylase using PPW as a medium.

• Korean journal of applied entomology
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• v.28 no.2
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• pp.69-75
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• 1989

The extracellular amylase production by Bacillus thuringiensis subsp. kurstaki HD-l in amylase production media and its characteristics were investigated. The amylase production was highest in the medium composed of 0.2% soluble starch, 1.0% Bacto-peptone, 0.3% beef extract, 0.3% yeast extract, 0.5% NaCl, 0.3% $K_2HPO_4$, 0.1% $KH_2PO_4$, 0.012% $CaCl_2$.$2H_2O$, 0.005% $MnSO_4$.$H_2O$, and 0.03% $MgSO_4$.$7H_2O$. The amylase activity was inhibited by 50mM EDT A. The enzyme was optimally active from pH 6.5 to 7.0 at $55^{\circ}C$, The specific activity of the enzyme in the ethanol precipitate was 2.01 units/mg, and the Km value was approxi-mately 0.8 mg/ml.

• Mycobiology
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• v.29 no.4
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• pp.183-189
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• 2001

Extracellular amylase properties were examined with the mycelium of Tricholoma matsutake isolated from ectomycorrhizal roots of Pinus densiflora. The molecular weights of $\alpha$-amylase and glucoamylase were estimated as 34.2 kD and 11.5 kD, respectively, after eluted through Superdex 75 column. The optimum pH of the purified enzyme was found in a range of pH $5.0{\sim}6.0$, with a peak at pH 5.0. The activities of these enzymes were stable from $4^{\circ}C\;to\;30^{\circ}C$. The $\alpha$-amylase of T. matsutake readily hydrolyzed soluble starch and amylose-B, while it weakly hydrolyzed glycogen, dextrin, amylose and amylose-A. The main products of hydrolysis were confirmed to be glucose, maltose and maltotriose on the basis of the similarities in the thin layer chromatographic mobility.

• Microbiology and Biotechnology Letters
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• v.28 no.1
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• pp.59-61
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• 2000

The various extracellular enzymes produced by lactic acid bacteria isolated from kimchi were assayed to improve the shelf-life of kimchi. Peroxidase was not detected in all tested lactic acid bacteria and small amount of ascorbic acid oxidase was detected in Pediococcus pentosaceus and Lactobacillus brevis. In case of $\alpha$-amylase, 27.8 and 20.9 unit/mg were shown in Pediococcus acidilactici and Pediococcus pentosaceus, respectively but $\beta$-amylase and protease activities were very low. The enzyme related to textural property of kimchi, pectinesterase showed low activity but polygalacturonase activity was 0.28 unit/mg in Lactobacillus homohiochii and 0.27 unit/mg in Lactobacillus plantarum.

• Microbiology and Biotechnology Letters
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• v.16 no.5
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• pp.358-362
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• 1988

Aqueous two-phase fermentation system was tested for the overproduction of extracellular enzyme through $\alpha$-amylase fermentation by Bacillus amyloliquefaciens. By employing aqueous two-phase system $\alpha$-amylase activity showed 25% increase compared to the result using regular medium and no deactivation of the enzyme was observed. The presence of polyethylene glycol was observed to promote the enzyme production, while to inhibit the growth of the microorganism. It is recommended that polyethylene glycol be added during the log-growth phase and dextran be added after the enzyme activity reaches Its maximum for efficient $\alpha$-amylase fermentation and in situ recovery of the enzyme.

• Microbiology and Biotechnology Letters
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• v.40 no.4
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• pp.296-302
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• 2012

A bacterial strain was isolated from soybean paste fermented in a Korean Buddhist temple as a producer of the extracellular thermostable ${\alpha}$-amylase. The isolate YB-1234 has been identified as Bacillus licheniformis on the basis of its 16S rDNA sequence, morphology and biochemical properties. A gene encoding the thermostable ${\alpha}$-amylase of B. licheniformis YB-1234 was cloned into Escherichia coli and its nucleotide sequence was determined. The deduced amino acid sequence of ${\alpha}$-amylase was very highly homologous to those of the thermostable ${\alpha}$-amylases of B. licheniformis belonging to the glycosyl hydrolase family 13. The ${\alpha}$-amylase produced by recombinant E. coli carrying the ${\alpha}$-amylase gene exhibited maximal activity at pH 6.0, identical to ${\alpha}$-amylase in the culture filtrate of B. licheniformis, while the temperature profile was somewhat different between the two. Particularly, ${\alpha}$-amylase produced from B. lcheniformis is much more thermostable than that from recombinant E. coli. The predominant products resulting from the ${\alpha}$-amylase hydrolysis were glucose, maltose and maltotriose for maltotetraose and maltohexaose.

• The Korean Journal of Mycology
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• v.26 no.4 s.87
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• pp.496-501
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• 1998

The mycelia of Tricholoma matsutake DGUM 26001, 26101, 26210 and FRI 91024 were used to determine the extracellular enzyme activity in mycelia. When the filtrate of culture broth after 30-day cultivation at $24^{\circ}C$ was used as a crude solution of extracellular enzyme, the average specific activity of ${\alpha}-amylase$ was 6142.3 unit/mg protein. The specific activity of xylanase was comparatively high. However, little or no enzyme activities were found for ${\beta}-glucosidase$, ligninase, CMCase, chitinase, protease, and lipase.

• Proceedings of the Korean Society of Life Science Conference
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• 2002.03a
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• pp.40-40
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• 2002

• KSBB Journal
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• v.16 no.3
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• pp.246-252
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• 2001

We isolated a bacterium that produces an extracellular maltopentaose(G5)-forming amylase from amylose and soluble starch. The bacterium was identified and assigned as a Bacillus sp. AIR-5. The amylase did not hydrolyze maltose, maltotriose, maltotetraose or maltopentaose. Optimum medium composition for maltopentaose production in flask culture was 2%(w/v) soluble starch, 0.4%(w/v) tryptone, 0.5%(w/v) NaCl, 0.5%(w/v) K$_2$HPO$_4$, and 3 mM CaCl$_2$at pH 8.0, 28$^{\circ}C$. The highest yield for maltopentaose production in this condition was 6.45 g/L and was 32.55% of theoretical yield.

• Microbiology and Biotechnology Letters
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• v.16 no.5
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• pp.348-351
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• 1988

The production of extracellular $\alpha$-amylase by Bacillus thuringiensis 19 serotypes was examined by the hydrolysis test of starch. Thirteen serotypes produced the amylase. B. thuringiensis serovar thuringiensis alesti, kurstaki, sotto, kenya, israelensis, morrisoni, entomocidus, tolworthi, thompsoni, toumanoffi, pakistani, and indiana produced tee enzyme. The amylase produced by B. thuringiensis serovar israelensis showed highest activity around pH 6.7 to 7.2 and 55$^{\circ}C$ to $65^{\circ}C$. The high production medium of the amylase was composed of 1% bactopeptone, 0.3% beef-extract, 0.3% yeast ex-tract, 0.5% NaCl, 0.3% $K_2$HPO$_4$, 0.1% KH$_2$PO$_4$, 0.2% Soluble Starch, 0.012% CaCl$_2$.2$H_2O$$_2$, 0.005% MnCl$_2$, and 0.03% MgCl$_2$.7$H_2O$. The highest production of the enzyme was observed at 4 hours culture in the soluble starch (0.6 units/$m\ell$) or glucose (0.43 units/$m\ell$) substrate.