• Microbiology and Biotechnology Letters
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• v.18 no.6
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• pp.578-584
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• 1990

A microorganism capable of producing high level of extracelluar cyclomaltodextrin glucanotransferase(EC 2.4.1.19; CGTase) was isolated ’rom soil. The isolated strain No. 239 was identified as Bacillusstearothermophilus. The maximal CGTase production (about 7.0 unitslml) was observed in medium containing2% soluble starch, 0.5% defatted soybean meal, 0.1% NaH_2PO_4.2H_2O$ and 0.015% $ CaC_l2 $ with initial pH 7.0. The strain was cultured at $55^{\circ}C$ for 48 hr with reciprocal shaking. At 0.83% substrated concentration potato starch was the optimum substrate with 50.1% conversion to cyciodextrin (CD)after the reaction at $65^{\circ}C$ for 24 hr (CGTase 10 unitlg starch). Using soluble starch as substrate (5% substrate concentration, CGTase 10 unitlg starch), the maximum conversion of 40% was obtained at11 hr reaction, and the ratio of $\alpha-, \beta-$ and $\gamma$-CD production at this time were 1.0:1.3:0.4, respectively., respectively.

• The Korean Journal of Mycology
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• v.15 no.3
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• pp.158-168
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• 1987

Several species of the fungi were isolated from cassava(Manihot esculenta Gruntz) starch which had formed into pellet, those had been stored for a while in southern part of Thailand. The species of Rhizopus, Aspergillus niger, and Aspergillus fumigatus were identified. The experimental results are as follows; Dry weight increases were checked during the static liquid culture with modified Czapek Dox medium to which cassava starch was partly replaced to sugar, Aspergillus niger and Aspergillus fumigatus had grown more than Rizopus species when 6% cassava starch was replaced to sugar and had been cultured for 72 hours. Amounts of mycelial protein of Aspergillus niger were checked, the highest amount was shown in 6% cassava starch involved medium. When nitrogen sources were varied such as ammonium sulfate or urea against sodium nitrate, there was no significant difference in mycelial production. Alpha amylase activity of each fungus isolated here was checked, those of Aspergillus niger have shown the highest peak at 72 hours.

• Journal of Aquaculture
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• v.18 no.4
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• pp.245-251
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• 2005

This study was investigated the condition of their maximum activity to assay the enzymes of rotifer, Brachionus rotundiformis의 $\alpha$-amylase, total alkaline Protease, trypsin and TG-lipase activities of rotifer were higher and more sensitive in phosphate-NaOH buffer than Tris-HCl buffer. $\alpha$-amylase, trypsin and TG-lipase activities were appeared the maximum at pH 8.0, and total alkaline protease activity showed the maximum activity at pH 7.0. $\alpha$-amylase activity showed the highest activity at $40^{\circ}C$, and total alkaline protease and trypsin activities were assayed the highest at $55{\~}60^{\circ}C$. However, TG-lipase activity was appeared the highest at $25{\~}30^{\circ}C$. The optimum substrate concentration of enzyme activity of a-amylase, total alkaline protease, rypsin and TG-lipase were $3.5\%$ starch, $\0.6%$ azo-casein, $87.5{\mu}M$ BApNA and 81.2 mM olive oil, respectively. The optimum reaction time of enzyme activity of $\alpha$-amylase, total alkaline protease, trypsin and TG-lipase were increased up to 40, 60, 30 and 25 min., respectively. The data obtained in this study could be used for the digestive enzyme research of rotifer, B. rotundiformis.

• The Korean Journal of Mycology
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• v.13 no.4
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• pp.203-212
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• 1985

Of 450 strains isolated from the soil microbes collected in various locations in Korea, a strain had a strong inhibitory activity against bacterial ${\alpha}-amylase$ and was named strain DMC-72 of the genus Streptomyces. The amylase inhibitory metabolite produced by this strain was purified by means of acetone precipitation, adsorption on Amberlite IRC-50 and SP-Sephadex C-25. The inhibitor was found to be a derivative of oligosaccharides by spectral and chemical data. The inhibitor was stable at the pH range of $1{\sim}13$ and at $100^{\circ}C$ for half an hour, also inhibited other amylases such as salivary ${\alpha}-amylase$, pancreatic ${\alpha}-amylase$, fungal ${\alpha}-amylase$ and glucoamylase. However, it showed no inhibitory activity against ${\alpha}-glucosidase$, ${\beta}-glucosidase$, dextranase, and ${\beta}-amylase$. The kinetic studies of the inhibitor showed that its inhibitory effects on starch hydrolysis by ${\alpha}-amylase$ were noncompetitive.

• Journal of Life Science
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• v.8 no.4
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• pp.387-394
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• 1998

A thermophilic bacterium (strain DG0303) producing a thermostable $\alpha$-glucosidase was isolated from manure and identified as Bacillus sp. Strain DG0303 produced high level of $\alpha$-glucosidase compared with other thermophilic Bacillus strains. The cellular protein patterns were also compared with other Bacillus strains by sodium dodecyl sulfatepolyacrylamide gel electrophoresis(SDS-PAGE). On the basis of 16S rDNA analysis the Bacillus sp. DG0303 was found to be a member of Bacillus rDNA group 5. The optimum temperature for growth was 65$\circ$C and no growth was obtained at 40$\circ$C or 75$\circ$C. The optimum pH for growth was 5.5 to 8.5. $\alpha$-glucosidase activity was produced during growth and most activity was detected in the culture supernatant. The $\alpha$-glucosidase production was constitutive in the absence of carbohydrates. High level of enzyme activity was detected when the culture was grown on medium containing starch. Addition of glucose resulted in the repression of the $\alpha$-glucosidase production. The optimum pH and tempoerature for enzyme activity were pH 5.0 and 65$\circ$C, respectively. When analyzed by zymogram, the culture supernatant showed a single $\alpha$-glucosidase band with a molecular weight of approximately 60,000.

• 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.

• Journal of the Korean Graphic Arts Communication Society
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• v.7 no.1
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• pp.5-15
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• 1989

제지공정에서 전분의 처리에 대하여 고찰하였다. 고찰결과 표면처리제와 안료 coating 제에는 습윤강도가 높고 침투성이 좋은 산화전분, 효소변성전분이 이용되고, 내부첨가제는 전분, ${\alpha}-전분$, 산화전분, cation 전분등이 이용되고 있으나 cellulose와 전분유출을 막아 폐수처리가 용이하며 종이의 강도, 인쇄적성을 위해 cation 전분을 PVA와 함께 처리한다.

• Korean Journal of Food Science and Technology
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• v.31 no.6
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• pp.1421-1426
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• 1999

Sixteen domestic barley varieties and subsequently produced malts were evaluated for quality characteristics. Diastatic power(DP), complementary actions of amylases in malt, had a wide $variation(139{\sim}220^{\circ}L)$ among the barley varieties. Some 6-row barley varieties demonstrated significantly high DP values. ${\beta}-\;and\;{\alpha}-amylase$ activities in malts were also significantly influenced by barley varieties. Diastatic power was highly correlated with ${\beta}-amylase$ activity, indicating that the ${\beta}-amylase$ activity was a predominant factor determining saccharifying action in malt. Amylograph was used to indirectly estimate starch-degrading enzymatic activity, and the reduction in amylograph viscosity was associated with ${\alpha}-amylase$ activity. Barley quality factors in relation to enzymatic activity of malt were analyzed, and the barley variety with lower kernel weight and less plumper kernels tended to produce higher starch-degrading enzyme activity. Potential diastatic power, an estimate of bound ${\beta}-amylase$ in raw barley, was associated with diastatic power in the final malt. Potential diastatic power turned out to be an important factor for predicting good malting barley.

• Journal of Life Science
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• v.28 no.4
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• pp.421-428
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• 2018

Postprandial hyperglycemia plays an important role in the development of Type 2 Diabetes and diabetic complications. Controlling postprandial hyperglycemia is the most important factor for reducing the risks of diabetic complications in Type 2 diabetic patients. This study was designed to determine whether Portulaca oleracea L. extract suppresses the activation of carbohydrate-digesting enzymes, and lowers postprandial hyperglycemia in diabetic mice through streptozotocin. P. oleracea was extracted with either 80% ethanol (PEE) or water (PWE), and the extract solutions were concentrated. The ${\alpha}$-glucosidase and ${\alpha}$-amylase inhibition assays were performed using the chromogenic method. Normal mice and STZ-induced diabetic mice were orally treated with PEE, PWE (300 mg/kg of body weight) or acarbose (100 mg/kg of body weight), with soluble starch (2 g/kg of body weight). The ${\alpha}$-glucosidase and ${\alpha}$-amylase inhibitory effectiveness by PEE were markedly more effective than PWE, and both extracts indicated a higher effectiveness than the acarbose (positive control). The rise in postprandial blood glucose due to starch loading was markedly inhibited in the PEE group when compared to the control group in diabetic and normal mice. Furthermore, the area under the concentration-time curve values were markedly declined by the PEE injection in the diabetic group when compared to that exerted for the control group. These results demonstrate that P. oleracea extracts lower postprandial hyperglycemia by inhibiting carbohydrate-digesting enzymes, and that the ethanol extract is more efficacious than the water extract.

• Journal of the Korean Society of Food Science and Nutrition
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• v.37 no.1
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• pp.42-47
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• 2008

Prevention of postprandial hyperglycemia is important, as it is implicated in the development of macro- and microvascular complications associated with diabetes. An inhibitor of ${\alpha}$-amylase which acts in the first step of carbohydrate digestion, is expected to be a suppressor of postprandial hyperglycemia. This study investigated the porcine pancreatic ${\alpha}$-amylase inhibitory activity of the extracts from buckwheat (Fagopyrum esculentum) flower, leaf, stem and grain. Flower, leaf, stem and grain of buckwheat were extracted by water and ethanol (40%, 70%, 100%), respectively. Flower and leaf extracts were more effective ${\alpha}$-amylase inhibitors than stem and grain extracts in all tested solutions. Ethanol extracts were more effective than water extracts or powders on the ${\alpha}$-amylase inhibitory activities. At concentrations of $0.5%{\sim}10%$ (w/w, starch basis), the flower extracts of 40%, 70% and 100% ethanol lowered the enzyme activity by about 90% and the results were similar to the values of acarbose. At the same concentrations, the leaf extracts of 100% ethanol lowered the enzyme activity by about 90%. These results suggest that buckwheat flower and leaf ethanol extracts may delay carbohydrate digestion and lower postprandial hyperglycemia.