• 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.

• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.8
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• pp.1262-1269
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• 2003

In this study, enzymes were investigated as an antistaling agent for a Korean rice cake. Thermograms by a DSC demonstrated that the gelatinization-onset temperature of the Korean rice cake was at its lowest temperature of 71.1$^{\circ}C$ with the GP (glucoamylase+pullulanase) treatment, followed by $\beta$-amylase and $\alpha$-amylase. The gelatinization peak temperature of the Korean rice cake with enzyme treatment was relatively lower compared to the control. Furthermore, the Korean rice cake with GP treatment showed the lowest peak temperature. Melting enthalpy of the Korean rice cake increased with the enzyme treatment, with $\beta$-amylase, followed by $\alpha$-amylase and GP. Melting enthalpy of the Korean rice cake with GP treatment was significantly lower compared to the $\beta$- and $\alpha$-amylase treatment. Recrystallinity in the case of GP treatment was also significantly lower than control. The range of Avrami exponent (n) was 0.90 ∼ 1.20 and the time constant of retrogradation (1/k) of the Korean rice cake crystalline decreased in the following order: GP, $\beta$-, $\alpha$ -amylase and control. Textural characteristics of the Korean rice cake with enzyme treatment differed greatly from that of control. The L＊ values of all the Korean rice cakes made without $\beta$-amylase decreased and the a＊ values were significantly different at p<0.05. The GP treatment altered the b＊ value toward blue color, whereas $\beta$-and $\alpha$-amylase changed to the direction to yellow color. In sensory evaluation, the Korean rice cake with enzyme treatment showed higher evaluation compared to control.

• Journal of the Korean Society of Food Science and Nutrition
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• v.16 no.2
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• pp.128-135
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• 1987

Extracellular ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase produced by a thermophilic and cellulolytic bacterium, Herpetosiphon geysericola CUM 317, were partially purified by salting out with ammonium sulfate and by chromatography on a DEAE-cellulose column and on a CM-cellulose column. The Km values of ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase for potato starch were $2.31mg/m{\ell}$, $7.69mg/m{\ell}$, and $8.33mg/m{\ell}$. The molecular weights of ${\alpha}-amylase$, ${\beta}-amylase$ and glucoamylase were calculated to be about 84000 dalton, 76000 dalton and 80000 dalton, respectively.

• Bulletin of the Korean Chemical Society
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• v.15 no.10
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• pp.832-835
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• 1994

The ${alpha}$-amylase gene of Bacillus licheniformis has been cloned and two mutant ${alpha}$-amylase genes of which histidine 235 was changed to glutamine (H235Q) and aspartic acid 328 to glutamic acid (D328E) have been produced by site-directed mutagenesis. The kinetic parameters, optimum pH and thermostability of wild type(WT) and these two mutant amylases expressed in E. coli MC1061 have been compared after purification. The $K_m$ values of WT, H235Q and D328E ${alpha}$-amylases were 0.22%, 0.73%, and 0.80% respectively, when using starch as the substrate. The $V_max$ values of wild type ${alpha}$ -amylase and mutant ${alpha}$-amylases were 0.6-0.7%/minute, and did not show any significant differences among them. The optimum pH of D328E ${alpha}$-amylase was shifted to more acidic pH. Also, the thermostability of H235Q ${alpha}$-amylase was increased compared to the wild type ${alpha}$-amylase.

• Biotechnology and Bioprocess Engineering:BBE
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• v.5 no.1
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• pp.7-12
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• 2000

The expression of the mouse $\alpha-amylase$ gene in the methylotrophic yeast, P pastoris was investigated. The mouse $\alpha-amylase$ gene was inserted into the multi-cloning site of a Pichi a expression vector, pPIC9, yielding a new expression vector pME624. The plasmid pME624 was digested with SalI or BglII, and was introduced into P. pastoris strain GSl15 by the PEG1000 method. Fifty-three transformants were obtained by the transplacement of pME624 digested with SaiII or BglII into the HIS4locus $(38\;of\;Mut^+\;clone)$ or into the AOX1 locus $(15\;of\;Mut^s\;clone)$. Southern blot was carried out in 11 transformants, which showed that the mouse $\alpha-amylase$ gene was integrated into the Pichia chromosome. When the second screening was performed in shaker culture, transformant G2 showed the highest $\alpha-amylase$ activity, 290 units/ml after 3-day culture, among 53 transformants. When this expression level of the mouse $\alpha-amylase$ gene is compared with that in recombinant Saccharomyces cerevisiae harboring a plasmid encoding the same mouse $\alpha-amylase$ gene, the specific enzyme activity is eight fold higher than that of the recombinant S. cerevisiae.

• Korean Journal of Microbiology
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• v.6 no.2
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• pp.68-74
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• 1968

Effects of gibberellin on alpha and beta-amylase activities of Aspergillus orygae var. microsporus have been studied. Results obtained are as follows: 1. The growth of mycelium and dry weight of surface ped was accelerated by 0, 0001% gibberellin solution, spores of Aspergillus oryzae var. microsporus. were preveously soaked for three days. 2. Adding to culture media with 0, 0015% gibberellin, alpha-amylase was increased 50% much as beta-Amylase was as much as 50%.

• Korean Journal of Microbiology
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• v.35 no.1
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• pp.1-6
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• 1999

Benzylalcohol-$\alpha$-glucoside (BG) was synthesized from soluble starch by transglycosylation of $\alpha$-amylase. Transglycosylation in water-organic two phase system containing 1% soluble starch as a glycosyl donor, 90% benzylalcohol as a glycosyl acceplor, 10% citrate buffer solulion (0.1 M, pH 5.0), and 10 unit of $\alpha$-amylase (Aspergilllw oryzae) was showed highcst efficiency. About 4 mg BG was obtained from 10 mg starch in reaction for 80 hrs at $40^{\circ}C$. Initially benzylalcohol-$\alpha$-maltoside Q3M) was major product, but as the reaction proceeded, it was hydrolyzed to glucose and BG. Finally the product of transglycosylation by $\alpha$-amylase was only BG. The both products did not show reducing powcr and hydrolyzed by $\alpha$-glucosidase and $\alpha$-amylase, respectively. The molecular wcights of both were estimated to be 270 and 432 by ES1-Mass, respectively.

• Microbiology and Biotechnology Letters
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• v.13 no.1
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• pp.7-11
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• 1985

In order to investigate the biological activity of ginseng saponins, the effects of ginseng saponins on the reaction catalyzed by bacterial a-amylase were studied and the results obtained were summerized as follows. Bacterial ${\alpha}$-amylase activity was increased by the addition of protopanaxadiol (diol), protopanaxatriol (triol) and total saponin. Preincubation of ${\alpha}$-amylase with diol saponin at $40^{\circ}C$ for 3 min increased ${\alpha}$-amylase activity to the degree of 120%. In the protective effect on the heat denaturation of the enzyme, triol saponin protected the heat denaturation for 5 min at $60^{\circ}C$, but diol saponin accelerated the heat denaturation. The hydrolyzates of diol and triol saponin increased the enzyme activity more than the intact diol and triol saponin. In the catalysis system of bacterial ${\alpha}$-amylase, the addition of diol and triol saponin reduced the substrate inhibition in the presence of high concentration of the substrate.

• Preventive Nutrition and Food Science
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• v.22 no.3
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• pp.166-171
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• 2017

In this study, we investigated whether Sargassum yezoense extract (SYE) could inhibit ${\alpha}-glucosidase$ and ${\alpha}-amylase$ activities, and alleviate postprandial hyperglycemia in streptozotocin (STZ)-induced diabetic mice. Freeze-dried S. yezoense was extracted with 80% ethanol and concentrated for use in this study. The hypoglycemic effect was determined by evaluating the inhibitory activities of SYE against ${\alpha}-glucosidase$ and ${\alpha}-amylase$ as well as its ability to decrease postprandial blood glucose levels. The half-maximal inhibitory concentrations of SYE against ${\alpha}-glucosidase$ and ${\alpha}-amylase$ were $0.078{\pm}0.004$ and $0.212{\pm}0.064mg/mL$, respectively. SYE was a more effective inhibitor of ${\alpha}-glucosidase$ and ${\alpha}-amylase$ activities than the positive control, acarbose. The increase in postprandial blood glucose levels was significantly alleviated in the SYE group compared with that in the control group of STZ-induced diabetic mice. Furthermore, the area under the curves significantly decreased with SYE administration in STZ-induced diabetic mice. These results suggest that SYE is a potent inhibitor of ${\alpha}-glucosidase$ and ${\alpha}-amylase$ activities and alleviates postprandial hyperglycemia caused by dietary carbohydrates.