• Microbiology and Biotechnology Letters
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• v.31 no.1
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• pp.36-41
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• 2003

In order to increase the production and secretion rate of mouse salivary $\alpha$-amylase from Saccharomyces cerevisiae, various experiments were attempted. A plasmid pCNNinv (AMY) was constructed by the substitution of ADCl promoter and native signal sequence of mouse salivary $\alpha$-amylase cDNA gene with PRBI promoter and yeast invertase leader sequence, which resulted in 25% increase in the production of $\alpha$-amylase in the culture medium. The respiratory deficient transformant carrying pCNNinv (AMY) were obtained by treating yeast cells with ethidium bromide, and the $\alpha$-amylase activities in the culture brothes of the respiratory-deficient transformants were 5-8 times higher than that of parental wild type strain. $\alpha$-Amylase activity was also increased 3 times when the 0.015% (w/v) of 2-mercaptoethanol was added to the culture medium.

• Applied Biological Chemistry
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• v.48 no.1
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• pp.103-108
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• 2005

${\alpha}-Amylase$ inhibitor is used to control blood glucose level by inhibiting starch digestion in the small intestine and delaying the absorption of glucose. In this study, we investigated the effect of the ethanol extracts from more than 1400 species of plants against ${\alpha}-amylase$ with the aim of developing a new ${\alpha}-amylase$ inhibitor. In the results, Cornus walteri extracts showed the highest inhibition activity. The inhibitory effect of Cornus walteri extract on the carbohydrate hydrolysis enzymes has different sensitivities against ${\alpha}-amylase$ from salivary and pancreatin and against ${\alpha}-glucosidase$ from yeast and porcine small intestine. In the study of inhibition kinetics of ${\alpha}-amylase$ and ${\alpha}-glucosidase$, Cornus walteri extract showed competitive inhibition against salivary and pancreatin while showing the combination of uncompetitive and noncompetitive inhibition against ${\alpha}-glucosidase$. The Cornus walteri extract was stable at acidic and thermal conditions. As for the blood glucose and body weight levels of Cornus walteri extract, we confirmed anti-hyperglycemic and anti-obesity effects. Also, in the investigation of the mRNA lever, Cornus walteri extract upregulated the level of GLUT4 mRNA in the quadriceps muscle.

• Applied Biological Chemistry
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• v.21 no.2
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• pp.103-108
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• 1978

Acid-stable ${\alpha}-amylase$ was partially purified from Paecilomyces subglobosum by Sephadex G-150 gel filtration. About 7.7-fold purification was obtained and the partially purified preparation has 5.0 U of ${\alpha}-amylase$ activity per mg of protein. Using this partially purified ${\alpha}-amylase$, general properties were studied and it showed the maximal activities at the conditions of pH 4.0 and $38^{\circ}C$. High stability of the acid-stable ${\alpha}-amylase$ in acidic condition was observed, whereas thermal stability was similar to the conventional ${\alpha}-amylase$.

• Microbiology and Biotechnology Letters
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• v.27 no.3
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• pp.203-207
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• 1999

V. alginolyticus 138-2, a marine halophilic bacterium, produced an extracellular amylase with a molecular weight of ca. 56,000. The analysis of the digestion products of soluble starch by thin layer chromatography(TLC) revealed that the extracellular amylase of V. alginolyticus 138-2 is a saccharifying-type alpha-amylase. The alpha-amylase activity of the culture supernatant of soluble starch was optimal at pH 6.0 and 45$^{\circ}C$. Ca2+ slightly increased the alpha-amylase activity, whereas Hg2+, An2+, Cu2+, Ni2+, Fe2+, and Mn2+inhibited the enzymatic activity. Alkylating thiol group agent, iodoacetic acid did not affect the alpha-amylase activity, but reduced thiol reagents such as dithiothreitol, cysteine, and beta-mercaptoethanol stimulated theenzymatic activity. On the other hand, even if V. alginolyticus 138-2 is a marine halophilic bacterium, its alpha-amylase activity was significantly inhibited by NaCl.

• Archives of Pharmacal Research
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• v.8 no.2
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• pp.67-75
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• 1985

To find emylase inhibitors produced by microorganisms from soil, a strain which had a strong inhibitory activity against bacteria .alpha.-amylase was isolated from the soil smaple collected in Seoul. The morphological and physiological characteristics of this strain on several media and its utilization of carbon sources showed that it was one of Streptomyces specties according to the international Streptomyces Project method. The amylase inhibitor of this strain was purified by means of acetone precipitation, adsorption on Amberlite XAD-2, and column chromatography on Amberlite CG-50 and SP-Sephadex C-25. The inhibitor was stable at the pH range of 1-10 and at 100.deg.C for half an hour, and had inhibitory activities against other amylases such as salivary .alpha.-amylase, pancreatic .alpha.-amylase, fungal .alpha.-amylase and glucoamylase. The kinetic studies of the inhibitor showed that its inhibitory effect on starch hydrolysis by .alpha.-amylase was non-competitive.

• Journal of the Korean Society of Food Science and Nutrition
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• v.14 no.2
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• pp.188-191
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• 1985

A thermophilic and cellulolytic bacterium, Herpetosiphon geysericola CUM 317 isolated from the compost, produced ${\alpha}-amylase,\;{\beta}-amylase$, and glucoamylase. Mutual relationships on the production of the three amylases were studied by changing the cultivation conditions. ${\alpha}-Amylase$ and glucoamylase were produced highly after 40 hrs on wheat bran medium at $50^{\circ}C$ and after 30 hrs on liquid medium at $40^{\circ}C$, though ${\beta}-amylase$ was produced best at 10 hrs of initial cultivation phase. The production of the amylases was generally repressed by the addition of carbon sources in liquid medium containing polypeptone. ${\alpha}-Amylase$ production was enhanced relatively by the addition of cupric sulfate in the liquid medium, ${\beta}-amylase$ was enhanced by cadmium sulfate, and glucoamylase was enhanced by calcium chloride.

• The Korean Journal of Food And Nutrition
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• v.11 no.5
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• pp.561-564
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• 1998

The stabilizatio of amaylolytic enzyme such as $\beta$-amylase of barley, $\beta$-amylase of wheat, $\beta$-amylase of sweet potato, $\alpha$-amylase of Bacillus licheniformis, $\alpha$-amylase of Aspergillus sp. and $\alpha$-glucosidase of Aspergillus awamori was attained by modification with periodate-oxidized soluble starch. The pH stability of modified enzyme was increased at pH 9 for $\beta$-amylase of sweet potato, pH 3~5 and 8~11 for $\beta$-amylase of barley, pH 2~3 and 7~12 for $\beta$-amylase of wheat and pH 6 for $\alpha$-glucosidase of Aspergillus awamori. Thermal stability increased 17.6% for $\alpha$-amylase of Aspergillus sp. at 6$0^{\circ}C$ for 10min, 30% for $\alpha$-amylase of Bacillus licheniformis at 10$0^{\circ}C$ for 5min and 4.5% for $\alpha$-amylase of sweet potato at 6$0^{\circ}C$ for 10min compared with those of native enzymes.

• Korean Journal of Environmental Agriculture
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• v.22 no.4
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• pp.290-293
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• 2003

To measure an effects of strontium on secretion of ${\alpha}$-amylase and RNase, wheat aleurone layers were isolated after the pre-incubation in a solution with or without 10 mM $SrCl_2$ or $CaCl_2$ for 3 days at $25^{\circ}C$ in the dark under aseptic conditions. The secretion of ${\alpha}$-amylase reached a maximum at 72 h after incubation. $Sr^{2+}$ induced more effectively secretion of ${\alpha}$-amylase than $Ca^{2+}$. The ${\alpha}$-amylase secretions by $Sr^{2+}$ or $Ca^{2+}$ ware about $2 (Ca^{2+})$ to $2.5 (Sr^{2+})$ fold higher than it without divalent ions, When aleurone layers were incubated without divalent ions, however, the ${\alpha}$-amylase was remarkably retained in the tissues. Total ${\alpha}$-amylase synthesis (ie. tissues + media) was slightly lowered by 10mM $SrCl_2$ addition. It seemed that the RNase secretion begins at 18 h after incubation. This meaned that the RNase secretion may process slower than ${\alpha}$-amylasee secretion. $Ca^{2+}$ effect on RNase secretion is stronger than $Sr^{2+}$ unlikely to ${\alpha}$-amylase. The secretion process is likely to be suddenly induced between 72 hand 96 h. These results suggested that the secretion was enhanced after the accumulation in aleurone layers.

• Journal of Pharmaceutical Investigation
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• v.19 no.4
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• pp.185-190
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• 1989

The release of angiotensin and ${\alpha}-amylase$ from monolithic devices of different molecular weight of polyethylene glycol (PEC) grafted polyurethane copolymer was investigated. Water-soluble PEG grafted polymer provided a controlled release of angiotensin and ${\alpha}-amylase$. The release rate of angiotensin and ${\alpha}-amylase$ could be controlled by varying the molecular weight of PEC grafted. The release mechanism may be associated with the creation of pore or domain through the devices following the gel swelling and self-aggregation by PEC grafted polymer. Hydrophobic polyurethane grafted with PEG can provide a biomaterial for prolonged release of angiotensin and ${\alpha}-amylase$ from angiotensin and ${\alpha}-amylase$ blended system.

• Applied Biological Chemistry
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• v.41 no.1
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• pp.18-22
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• 1998

A mutant strain which hyperproduced thermostable ${\alpha}-amylase$ was obtained by chemical mutagenesis of Bacillus licheniformis. The mutant strain, SK-5, produced the enzyme about 50 times higher than the original strain. The mutant was longer and slimmer in shape, slower in growth compared to the original strain. Nucleotide sequence analysis of the SK-5 ${\alpha}-amylase$ gene revealed no changes in the the structural gene. The changes found in the promoter region might be responsible for the hyperproduction of the enzyme by the mutant. No structural changes in the enzyme structure could be observed when the secreted enzymes at various culture times were analyzed by Western blot.