• Journal of the Korean Wood Science and Technology
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• v.32 no.6
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• pp.36-42
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• 2004

Inhibitors of α-amylase are important for the treatment of diabetes and obesity. Using enzyme inhibitor's activity, ethanolic extracts of 87 species in 12 families were screened and compared their inhibitory effect on α-amylase, As a results, we can find that extracts of Distylium racemosum, Acer tegmentosum, Corylapsis veitchiana, Cornus walteri and Corylapsis spicata showed higher α-amylase inhibitory activities than the others and have potential possibility of using control agents for carbohydrate-dependent disease.

• The Korean Journal of Physiology
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• v.29 no.2
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• pp.243-250
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• 1995

A possible potentiation between cholecystokinin (CCK) and secretin in amylase secretion from isolated rat pancreatic acini was investigated. Combined treatment of acini with secretin and CCK at low concentrations, which are known to be physiological, resulted in enzyme secretion larger than the arithmetic sum of their separate effects. Such a potentiating effect also occurred between secretin and A23187 (Ca ionophore), between forskolin (adenylate cyclase activator) and CCK, and between forskolin and A23187. Staurosporin (protein kinase C inhibitor) and W7 (calmodulin antagonist) inhibited markedly the potentiated amylase release induced by the agonists, but KT5720 (protein kinase A inhibitor) did not affect the potentiated amylase release. Therefore, we concluded that the action of CCK in a physiological concentration is potentiated by secretin in a physiological concentration range and vice versa, and that the intracellular mechanism necessary for the potentiation is associated with $Ca^{2+}$. However, it is uncertain what mechanisms are involved in potentiation of amylase release after CAMP and $Ca^{2+}$.

• 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.

• Korean Journal of Soil Science and Fertilizer
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• v.31 no.1
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• pp.56-60
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• 1998

Radish and Chinese cabbage were cultivated under hydrophonic culture to investigate the effect of chromium on germination, cell elongation, ${\alpha}$-amlyase activity, contents of chlorophyll and protein. With increasing concentration of cromium, germination, cell elongation, ${\alpha}$-amlyase activity were decreased in both radish and Chinese cabbage, the rate was higher in radish than in Chinese cabbage. Contents of chlorophyll a and b were also decreased and chlorophyll a was higher than chlorophyll b. As the concentration of chromium was increased inhibited in the order of protein> ${\alpha}$-amylase activity>chlorophyll a>chlorophyll b.

• Microbiology and Biotechnology Letters
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• v.9 no.3
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• pp.145-152
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• 1981

Microorganisms from the waste water of starch industry, were isolated and a strain, Y-124, possessing a powerful enzymic activity was selected and identified as a member of the genus Bacillus. The ideal cultural condition for the formation of $\alpha$-amylase form Bacillus Y-124 and its preservation was investigated in connection with the biotechnological and industrial approach to the bulk enzyme production. High yield of $\alpha$-amylase was observed in medium containing casein as well as calcium pantothenate in this work. Calcium ions were found to have an effect in forming this particular enzyme. Ammonium phosphate dibasic was an important inorganic nitrogen source for the formation of $\alpha$-amylase. And preservation of this enzyme was greatly affected by calcium or sodium salts. The addition of calcium carbonate or sodium sulfate presented the most effective result for the prevention of its denaturation to various factors. The above data was obtained with crude enzyme preparation.

• Korean Journal of Soil Science and Fertilizer
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• v.31 no.2
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• pp.158-161
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• 1998

The study was carried out to examine changes of ${\alpha}$-amylase activity and free proline contents during rice germination under low temperature($13^{\circ}C$). The plant height, root length, and germination rate were investigated during seed germination under the low temperature. Those growth chracteristics were the highest in Dongjin cultiver compared with other rice cultivars. The ${\alpha}$-amylase activity of the 9 days after germination was higher in Dongjin than those of Sangju and Koshihikari cultivars. The content of free proline was increased in all rice cultivars, when the germination of rice seeds was prolonged. As a result, it was concluded that ${\alpha}$-amylase activity and free proline content of Donjin cultivar were relatively increased higher under low temperature stress than those of other rice cultivars.

• KSBB Journal
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• v.11 no.1
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• pp.86-91
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• 1996

Optimal reaction condition for the starch hydrolysis by ${\alpha}$-amylase was determined and the sugar produced under the optimal condition was measured for estimating the biodegradation of strach-filled polyethylene film. Optimal ranges of temperature and pH were 70~$80^{\circ}C$ and 6.3~7.3, respectively. The 100 units of ${\alpha}$-amylase per mg starch were enough for the enzyme reaction. Reaction with polyethylene film containing 5%, 10%, 15% and 20% starch in the above condition showed that the sugar produced was proportional to the starch content in film. This relationship provides a calibration curve for determining the starch content of search-filled polyethylene film. The average amount of hydrolyzed starch was about 40% of total starch in film. The rest of the starch is considered to be still dispersed in the film and not to be attacked by ${\alpha}$-amylase. In this experiment, we could obtain the higher biodegradability through the $\alpha$-amylase reaction in the above optimal condition than the reported one which had been Improved by adding surfactant.

• Microbiology and Biotechnology Letters
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• v.18 no.4
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• pp.352-359
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• 1990

The synergistic effect of glucoamylase and a -amylase on the hydrolysis of raw corn starch in an agitated bead reaction system was studied by investigating the changes of sugar profiles, the granular structure, particle size distribution, and X-ray diffraction pattern of residual raw corn starch. The enzymatic hydrolysis of raw corn starch was greatly enhanced by synergistic effect of glucoamylase and $\alpha$ -amylase. Even though the sugar profiles were mainly determined by the mixing ratio of glucoamylase and $\alpha$-amylase; raw starch was mainly converted to glucose directly without accumulation of any significant amount of oligosaccharides. The cavity formation and fragmentation phenomena of raw corn starch granule subjected to enzyme reaction were analyzed by means of SEM and the particle size distribution. The X-ray diffraction pattern of raw starch was not changed at the initial stage of reaction but slightly changed at the late stage of hydrolysis, which may be caused by the preferential degradation of amorphous region by enzymatic reaction, not by the destruction of microcrystalline structure of raw corn starch.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.8
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• pp.1164-1173
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• 2006

Cellulase from Aspergillus niger, (${\alpha}$-amylase from Bacillus sp. and protease from Bacillus globigii were used as enzyme sources in this study to examine how their respective substrates protect them in two kinds of simulated gastrointestinal tract digesting processes. Avian total digest tract simulation test showed that filter paper, Avicel and cellulose resulted in 7.7, 6.4 and 7.4 times more activity than of unprotected cellulose, respectively. Protease with addition of casein, gelatin or soybean protein showed no significant protection response. Starch protected amylase to be 2.5 times activity of the unprotected one. Monogastric animal total tract digestion simulation test showed that filter paper, Avicel and cellulose resulted in 5.9, 9.0 and 8.8 times activity of unprotected cellulase, respectively. Casein, gelatin and soybean protein resulted in 1.2, 1.3 and 2.0 times activity of unprotected protease, respectively. Starch did not protect amylase activity in monogastric animal total tract simulation. Protection of mixed enzymes by substrates in two animal total tract simulation tests showed that filter paper in combination with soybean protein resulted in 1.5 times activity of unprotected cellulose, but all substrates tested showed no significant protection effect to protease. Soybean protein and starch added at the same time protected the amylase activity to be two times of the unprotected one. Test of non-purified substrate protection in two animal total digest tract simulation showed that cellulase activity increased as BSA (bovine serum albumin) concentration increased, with the highest activity to be 1.3 times of unprotected enzyme. However, BSA showed no significant protection effect to protease. Amylase activity increased to 1.5 times as BSA added more than 1.5% (w/v). Cellulase activity increased to 1.5 times as soybean hull was added higher than 1.5%. Amylase had a significant protection response only when soybean hull added up to 2%. Protease activity was not protected by soybean hull to any significant extent.

• Microbiology and Biotechnology Letters
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• v.18 no.3
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• pp.260-267
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• 1990

The mechanism of enzymatic hydrolysis of raw corn starch by the purified glucoamylase and a - amylase in an agitated bead reaction system was studied by investigating the changes of sugar profiles produced by each enzyme, the granular structure of raw corn starch, the amount of enzyme adsorption on residual starch, and the amylose content in residual raw starch. The sugar profiles produced by the action of exo-type glucoamylase or endo-type $\alpha$ -amylase in an agitated bead system were not recognizably differed with those produced in reaction system without bead. Without enzyme the intergenic microcrystalline structure of starch granule was not changed by the simple mechanical impact of solid media, but it was cleaved. However, starch granule was fragment into large number of small particles by the synergistic action of enzyme and attrition-milling media, identified to be the major saccharification enhancing mechanism along with the increased amount of enzyme adsorption. The amylose content decreased more readily in an agitated bead reaction system, especially by $\alpha$ -amylase.