• Korean Journal of Microbiology
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• v.15 no.2
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• pp.63-76
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• 1977

Irradiation with high doses of gamma rays induced the reduction of mycelial weight and anaylase activity, and increased relative amylase activity in surface cultures. Biphase in growth curves was shown in aeration-agitation cultures but the behavior of the first phase of growth could be eliminated by replacing the amylasehydrolysed starch substrates, so that enzyme production was shortened ca. 40 hours and relative amylase activity was increased about 3 times higher before onset of autolysis. In the effect of gibberellin on amylase production, the positive stimulation was appeared to only surface culturs of the liquid medium and the negative effect to shake-cultures in a mutant. Trials of various continuous culture were resulted not only the approalch to the value of amylase activity in surface cultures of liquid medium, but also higher productivity than in batch cultures. The culture-degeneration was observed in two-stage continuous culture, but did not appear in continuous elevation culture.

• The Korean Journal of Food And Nutrition
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• v.9 no.1
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• pp.85-91
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• 1996

B-amylase(EC 3.2.1.2) was isolated from the root of arrowroot(Peuria thunbergiana Bentham) with distilled water and then fractionated with ammonium sulfate. Crude extract was partially purified by ion exchange chromatography and gel filtration. The enzymatic properties of partially purified $\beta$-amylase were as follows, the enzyme was fractionated with ammonium sulfate between 0.2 and 0.4 saturation, and showed the typical reaction properties of B-amylase producing only maltose from starch. Optinum pH and temperature were pH 6.5, $50^{\circ}C$ respectively. The activity of the enzyme had proportional relations with enzyme protein concentration below 4mg, and had Michaelis constant of 66.7mg% for soluble starch. The enzyme was inhibited by some metal louts such as silver, cadmium, mercury, aluminum, iron and copper.

• Microbiology and Biotechnology Letters
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• v.21 no.6
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• pp.534-541
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• 1993

The relationship between Schwanniomyces occidentalis CBS 2863 (formerly castellii) and CBS 1153 (formerly alluvius), and their variety persoonii was examined at alpha-amylase gene level. Using Sch. occidentalis alpha-amylase gene as probe, Sch. occidentalis alpha-amylase gene homologues were obtained from Sch. occidentalis CBS 1153 and Sch. occidentalis var. persoonii. The restriction analysis of these homologues showed that the restriction enzyme sites between Sch. occidentalis CBS 2863 and CBS 1153 was identical but different between these strains and Sch. occidentalis var. persoonii.

• Korean Journal of Microbiology
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• v.10 no.3
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• pp.106-108
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• 1972

The enzyme was produced by Asp.oryzae SHW 131. the enzymatic properties of .alpha.-amylase are following : 1) Crystallization of .alpha.-amylase is formed of longish square. 2) The range of stable pH is 5-10 and optimum ph is 5.5. 3) It is very unstable enzyme about EDTA and protection by $Ca^{++}$ ion and best activated at $50^{\circ}C$ about temperature. 4) Asp.oryzae SHW 131 produced .alpha.-amylase with acid-protease, neutral-protease and tepid-alkalin-protease.

• Korean Journal of Microbiology
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• v.10 no.3
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• pp.105-105
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• 1972

The enzyme was produced by Asp.oryzae SHW 131. the enzymatic properties of .alpha.-amylase are following : 1) Crystallization of .alpha.-amylase is formed of longish square. 2) The range of stable pH is 5-10 and optimum ph is 5.5. 3) It is very unstable enzyme about EDTA and protection by $Ca^{++}$ ion and best activated at $50^{\circ}C$ about temperature. 4) Asp.oryzae SHW 131 produced .alpha.-amylase with acid-protease, neutral-protease and tepid-alkalin-protease.

• Advances in Traditional Medicine
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• v.4 no.4
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• pp.227-234
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• 2004

An ${\alpha}-Amylase$ was purified to apparent homogeneity from germinating soybean seeds (Glycine max). Enzyme showed high specificity for starch. ${\alpha}-Amylase$ from soybean has optimum pH at 7.6 in the pH range 4.0-10.6. At this pH, the $K_m$ of starch was 2.63 mg/ml and the $V_{max}$ was equal to 52.6 mg/ml/min protein. Optimum temperature of the enzyme was found to be $55^{\circ}C,\;Q_{10}$ equal to 1.85 and energy of activation equal to 12 kcal/mol. Additives like, EDTA reduced the activity of ${\alpha}-amylase$ whereas PMSF enhanced the activity. ${\alpha}-Amylase$ was inhibited by several heavy metal ions.

• YAKHAK HOEJI
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• v.4 no.1
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• pp.35-38
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• 1959

The enzymatic activity of amylase which was isolated from a shell fish Veneridae Soxidmnus purpuratus Sowerby(Korean name :Gai-jo-gai") was studied and the obtained results were as follows: (1) The optimum pH of the enzyme was Ca. 6.2-6.4. (2) Prohibiting activity of metalic ions for the enzymatic activity was the order of 1/1000M-$Mg^{++}$>1/1000M-$Sr^{++}$>1/1000M-$Na^{+}$, and $Ca^{++}$ ion's prohibiting action was hardly showed. (3) Of 3 specimens of amyiase from Heptapancreas, Gastro-intestine and crystalline style, the highest activity was shown by amylase from crystlline style, and the other two showed almost same degree of activity. (4) Heptapancreas Amylase from the shell fish showed remarkably higher enzymatic activity than the pancreas amylase from a pig.

• Korean Journal of Microbiology
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• v.7 no.2
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• pp.86-90
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• 1969

1. Amylase producing bacteria have been isolated from natural sources and was identified out. The above strain is identical to Bacillus subtillis in every details of physiological and morphorogical characteristics by this investigations. 2. Sikworm chrysalis nad chlorella extracts are prove to be further effective for the stimulation of amylase production than any other sources. The former silkworm extract is more stronger in its activity. 3. It is found that effective results had been accepted by a less soybean meal addition per that of wheat bran in the mixture ratio of them, also less addition of corn is needed in the mixture ratio of between corn and whear bran. In the mixing ratio of wheat bran per silkworm or chlorella extracts, the addition of wheat bran is necessary for stimulation of amylase production. 4. Fro the stimulation of amylase production, the effective substances from natural sources and its order of activity in cultral media cultral media is proved as follows, silkworms ext.>chlorella ext.>alcohol>skim-milk and peptone>fermented milk>radish leaf ext.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.4
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• pp.556-562
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• 1995

The $\alpha$-amylase inhibitor from naked barley was purified by DEAE-cellulose, Concanavalin-A sepharose and superose 6 column chromatography, and confirmed by capillary electrophoresis. The purified $\alpha$-amylase inhibitor showed a single band of 29KD in molecular weight when estimated by the SDS-PAGE. Its purity was increased by 12-fold as compared to its crude extract, and its specific activity was found to be 336.7units/mg. The major amino acids of the $\alpha$-amylase inhibitor from naked barley was appeared to be glutamic acid, asparitic acid and arginine. The inhibitor from naked barley was glycoproteins and carbohydrate content of inhibitor was 1.0%.

• Korean Journal of Microbiology
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• v.15 no.1
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• pp.31-41
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• 1977

Dextrinogenic and glucoamylase activities of Aspergillus isolated from various habitat-substrates collected through South Korea are measured, and their amylase activities are surveyed in taxonomical and ecological viewpoints. 1. A. flavous group and A.wentii group exhibited higher activities for both amylases than others. 2. In the relations between amylase activity of Asperguillus and their habitat-sub-strates, the strains isolated from meju and cereals exhibited predominant dextrinogenic amylase activity. 3. Dextrinogenic amylase activity of Aspergillus is higher in the strains isolated from southern coast than the other regions. 4. Among the 601 strains of Aspergillus surveryed, strain No.74 and strain No.421 exhibited the most predominant activity for dextrinogenic amylase and glucoamylase, respectively.