• Korean Journal of Weed Science
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• v.2 no.1
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• pp.13-19
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• 1982

The effect of metolachlor [2-chloro-N-(2-ethyl 1-6-methylphenyl)-N-(2-methoxy-l-methylethyl)-acetamide] on starch, sugar and protein content in relation with ${\alpha}$-amylase activity, and its interaction with GA in the germinating stage of rice were determined. The distinctive phytotoxic symptom was the failure of the primary leaf of rice to break the coleoptile. An inhibitory effect of metolachlor was nullified by the external application of GA $10^{-3}$M. A significantly slower starch degradation accompanying the lower content of sugars was observed in the gain of the metolachlor treated seedlings. Further, the total ${\alpha}$-amylase activity was significantly lower in the grain of rice seedlings treated with metolachlor than that of the untreated one, and the lower total ${\alpha}$-amylase activity could be due to an inhibition of ${\alpha}$-amylase formation.

• Microbiology and Biotechnology Letters
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• v.4 no.3
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• pp.91-97
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• 1976

During the course of studies on the production and utilization of thermostable ${\alpha}$-amylase from a thormophilic actinomycete species isolated from soil, partial characterization of the ${\alpha}$-amylase has been (arried out. The optimum pH for the dextrinogenic activity of the enzyme was found to be 6.5 and the maximum reaction rate was achieved at a temperature range of 55$^{\circ}$ to 65$^{\circ}C$. Calcium ion was recognized to have a slight effect in activating the enzyme, while heavy metal salts especially ferrous and cupric ions showed a remarkable inhibition effect. The enzyme was best protected iron thermal denaturation at pH 8.0 with tris-HCI buffer；inactivation was rapid at higher or lower pH values. Furthermore, its thermal stability was greatly increased by calcium ion, particulary at the final concentration of 1${\times}$10$\^$－2/ mole in the reaction mixture. The Km value for the ${\alpha}$-amylase was calculated to be 2.17${\times}$10$\^$－4/g per $m\ell$ and the energy of activation for the dextrinogenic reaction to be 12,000${\pm}$580 ㎈ per mole.

• Food Science and Preservation
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• v.13 no.5
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• pp.563-568
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• 2006

The properties of mung bean were investigated depending on hydrolysis condition. The results showed that enzyme treatments (${\alpha}$-amylase and protease each at 0.1% (w/w)) by varying hydrolysis temperature showed better properties than non-pretense treatment (control group). The treatment with 0.08% ${\alpha}$-amylase was best for optimum hydrolysis of mung bean starch The treatment using a mixture of 0.08% (w/w) ${\alpha}$-amylase and 0.12% (w/w) protease was best for optimum hydrolysis of meg bean protein. The effects of Hydrolysis time of mung bean showed that the optimum time was 60 and 90 min and there fore the optimum time was set at 60 min. These result showed that the best hydrolysis conditions of mung bean were the treatment at $60^{\circ}C$ for 60 min using a mixture of 0.08%(w/w) ${\alpha}$-amylase and 0.12% (w/w) pretense, with the sugar level shown at $5.8^{\circ}Brix$, reducing sugar at 2,022.13 mg% and crude protein at 7,666.17 mg%.

• Journal of Applied Biological Chemistry
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• v.59 no.1
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• pp.75-81
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• 2016

Glutaraldehyde was used as a cross-linking agent for immobilization of purified ${\alpha}$-amylase from Exiguobacterium sp. DAU5. Befitting concentration of glutaradehyde and cross-linking time is the key to preparation of cross-linking chitosan beads. Based on optimized immobilization condition for ${\alpha}$-amylase, an overall yield of 56% with specific activity of 2,240 U/g on chitosan beads and 58% with specific activity of 2,320 U/g on chitosan-carbon beads was obtained. The optimal temperature and pH of each immobilized enzyme activity were $50^{\circ}C$ and 50 mM glycine-NaOH buffer pH 8.5, respectively. Those retained more than 75 and 90% of its maximal enzyme activity at pH 7.0-9.5 and after incubation at $50^{\circ}C$ for 1 h, respectively. In addition, the immobilization product showed higher organic-solvent tolerance than free enzymes. The mode of hydrolyzing soluble starch revealed that the ${\alpha}$-amylase possessed high hydrolyzing activity. These results indicate that chitosan is good support and has broad application prospects of enzyme immobilization.

• The Korean Journal of Mycology
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• v.17 no.3
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• pp.145-148
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• 1989

An acid-stable ${\alpha}-amylase$ produced by Aspergillus niger K-25 strain was purified by fractional precipitation with ammonium sulfate, ethacridine and acetone. The final preparation was homogeneous in cellulose acetate electrophoresis. The enzyme retained 91 % of its oringinal activity at pH 3.0, 8.7% at pH 2.4. The optimum pH of the enzyme was around pH 4. The purified-enzyme with optimum temperature of $40^{\circ}C$ was more heat-stable than the commercial product. The enzyme retained 80% of its original activity when heated to $60^{\circ}C$ for 30 minutes while the commercial amylase lost its acitivity completely within 30 minutes at $50^{\circ}C$.

• The Korean Journal of Food And Nutrition
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• v.10 no.2
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• pp.180-185
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• 1997

Sikye was produced from glutinous rice. The glutinous rice Sikhye was found to contain 7.3% of limit dextrin, 10.1% of maltose, 1.3% of maltotriose and 1.75% of rice residue. Limit dextrin in glutinous rice Sikhye was purified by ethanol fractionation followed by gel chromatography on Biogel P-2. The purified limit dextrin showed both signal of $\alpha$-1,4- and $\alpha$-1,6-glucosidic linkage with its estimation ratio of 5:1 by 1H-NMR analysis. Limit dextrin was digested with enzymes(30units/ml) of $\alpha$-amylase, $\alpha$-glucosidase and glucoamylase from Aspergillus awamori, sweet potato $\beta$-amylase and human salivary $\alpha$-amylase at 37$^{\circ}C$ for 1 hour, respectively. Hydrolysis rates of these amylases on it were similar that of rice Sikhye. $\alpha$-Glucosidase plus human salivary $\alpha$-amylase hydrolyzed it to 18%. The results suggest that glutinous rice is more effective to produce high level of branched maltooligosaccharide compared with rice as raw material for Sikye making.

• Journal of Pharmaceutical Investigation
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• v.20 no.4
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• pp.209-215
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• 1990

The activities of s-amylase, ${\alpha}-amylase$ and protease of three combination products containing digestive enzymes, antacids and herbal drugs on the Korean market were estimated. The effects of antacids and herbal drugs on the activities of digestive enzymes were investigated. Starch-saccarifying activity of s-amylase, starch-dextrinizing activity of ${\alpha}-amylase$ and protein-peptic activity of protease were estimated by Somogy, Mc'Credy, and Casein-Folin method, respectivley. The optimal pH of s-amylase, ${\alpha}-amylase$ and protease were pH 5.0, 4.8 and 7.0, rcspectively. The digestive activities at optimal pH continued about eight hours. The digestive activities of individual enzymes were reduced to 40-90% by antacids and were affected somewhat positively or negatively by herbal drugs. Enzyme activities of the combination products were also affected by pH and reaction time.

• Journal of Life Science
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• v.18 no.7
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• pp.1005-1010
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• 2008

In this study, we investigated the inhibitory effect of four solvent fractions of Alnus firma on ${\alpha}-amylase$, ${\alpha}-glucosidase$ and aldose reductase activities. The inhibitory test showed that methanol (MeOH) extract and hexane (HX) fraction strongly inhibited pork pancreatin and salivary ${\alpha}-amylase$ activity. The MeOH extract and HX fraction of Alnus firma at the concentration of 4 mg/ml inhibited more than 70% of pancreatin and salivary ${\alpha}-amylase$ activity. The inhibitory effect of fractions has different specificities against ${\alpha}-amylase$ from pancreatin and salivary. In addition, the MeOH extract and butanol (BuOH) fraction showed the highest inhibitory activity on yeast ${\alpha}-glucosidase$ at values of $IC_{50}$ $137.36\;{\mu}g/ml$ and $115.14\;{\mu}g/ml$ respectively. The MeOH extract and BuOH fraction showed the highest inhibitory activity on yeast ${\alpha}-glucosidase$ than commercial agent such as 1-deoxynorjirimycin and acarbose. Inhibition kinetics of solvent fractions showed that ${\alpha}-glucosidase$ has been inhibited noncompetitively by the MeOH, EA and BuOH fraction. The aldose reductase from human muscle cell had been inhibited strongly by the MeOH extract and EA fraction at 57.996% and 83.293% at the concentration of $50\;{\mu}g/ml$, respectively. These findings may contribute to biological significance in that ${\alpha}-amylase$, ${\alpha}-glucosidase$ and aldose reductase inhibitory compounds could be used as a functional food and a drug for the symptomatic treatment of antidiabetic disease in the future.

• Proceedings of the Korean Society of Life Science Conference
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• 2003.05a
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• pp.23-37
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• 2003

A novel inhibitor against maltose-producing a-amylase was prepared via stepwise degradation of a high molecular weight acarbose (HMWA) using Thermus maltogenic amylase (ThMA). The structure of the purified inhibitor was determined to be ${\alpha}$-D-glucopyranosyl-${\alpha}$-acarviosinyl-D-glucopyranose (GlcAcvGlc). Progress curves of p-nitrophenyl-${\alpha}$-D-maltoside (PNPG2) hydrolysis by various amylolytic enzymes, including maltogenase (MGase), ThMA, and cyclodextrinase(CDase) I-5, in the presence of acarbose or GlcAcvGlc indicated a slow-binding mode of inhibition. The inhibition potency of GlcAcvGlc for MGase, ThMA, and CDase I-5 was 3 orders of magnitude higher than that of acarbose.

• Applied Biological Chemistry
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• v.30 no.3
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• pp.250-257
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• 1987

The most active strain for the amylase activity from the native Youngkwang koji, was isolated and identified as Aspergjllus awamori. The optimal conditions for the production of ${\alpha}-amylase$ and glucoamylase were investigated and the properties of these enzymes were also examined. Maximum yields of ${\alpha}-amylase$ and glucoamylase were obtained at $30^{\circ}C$, pH 5.0 for days. The production of these two enzymes were increased with the addition of maltose, urea, $K_2HPO_4$, $MgSO_4{\cdot}7H_2O$, and $CaCl_2{\cdot}2H_2O$. The activities of these enzymes were maximized at $50^{\circ}C$, $pH\;5{\sim}6$. The heat stabilites of ${\alpha}-amylase$ and glucoamylase were maintained at $50^{\circ}C$ for 20min and 40min, respectively. Also, the addtion of $MgSO_4{\cdot}7H_2O$, $K_2HPO_4$, and $CaCl_2{\cdot}2H_2O$ salt increased the heat stabilities of these enzymes.