• Microbiology and Biotechnology Letters
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• v.38 no.2
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• pp.183-189
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• 2010

In the course of screening for anti-acidosis and anti-diabetes agent from natural products, the inhibitory activities of Nepales plant extracts against microbial $\alpha$-amylase and $\alpha$-glucosidase were evaluated. Among the 100 different kinds of ethanol extracts, Cedrus deodara (Roxb.) G. Don and Myrica nagi Thunb showed strong inhibition activities against $\alpha$-amylase. The $IC_{50}$ values of C. deodara (Roxb.) G. Don, M. nagi Thunb and acarose, a commercial available anti-diabetes agent, were 44.5, 47.5 and $50.5\;{\mu}g/mL$, respectively. Considering the crude extract of C. deodara (Roxb.) G. Don, and M. nagi Thunb, these extracts have strong potentials as anti-acidosis or anti-diabates agent. In a while, Cleistocalyx operculatus (Roxb.) extract showed a good inhibition activity to $\alpha$-amylase and $\alpha$-glucosidase, even it was recently reported. The selected three extracts did not show any hemolysis activity against human red blood cell up to 1 mg/mL, and the inhibition activities were maintained by heat or acid treatment. Moreover, treatment of HCl (0.01N) for 1 h into C. operculatus (Roxb.) and M. nagi Thunb increased the inhibition activity from 50% to 70%. Our results suggest that C. deodara (Roxb.) G. Don, M. nagi Thunb, and C. operculatus (Roxb.) are potential as anti-acidosis and anti-diabetes agents.

• Korean Journal of Medicinal Crop Science
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• v.17 no.5
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• pp.357-362
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• 2009

Compounds of isolated from roots extract of Pueraria thunbergiana were tested their inhibitory effects on $\alpha$-glucosidase and $\alpha$-amylase. Inhibitory activity of methylene chloride (MC) fraction and ethyl acetate (EA) fraction against $\alpha$-glucosidase showed more than 60% at a concentration of $500{\mu}g/m{\ell}$. Among the nine compounds tested on $\alpha$-glucosidase, biochanin A, (-)-tuberosin and calycosin from MC fraction and daidzein from EA fraction were stronger inhibitors than acarbose ($IC_{50}=530{\mu}g/m{\ell}$), and their $IC_{50}$ were 9, 144, 328 and $20{\mu}g/m{\ell}$, respectively. Biochanin A and (-)-tuberosin also inhibited $\alpha$-amylase activity as like as acarbose $IC_{50}=20.5{\mu}g/m{\ell}$), and their $IC_{50}$ were 22 and $348{\mu}g/m{\ell}$, respectively. Although daidzein was already known $\alpha$-glucosidase inhibitory effects, it was newly evaluated that biochanin A and (-)-tuberosin inhibited $\alpha$-glucosidase as well as $\alpha$-amylase, and that calycosin did $\alpha$-glucosidase.

• KSBB Journal
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• v.11 no.2
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• pp.125-131
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• 1996

In this study, Bucillus amyloliquefaciens was adopted as bacterial source to investigate the concentration of carbon source by adding inhibitors in the batch culture. By adding acetic acid at $10g/\ell$ of initial glucose concentration, maximum dry cell density was obtained with the highest value of /$\3.9gell$ at $1.0g/\ell$ of initial acetic acid concentration. By adding acetic acid al 10g/$\ell$ of initial glucose concentration, maximum ${\alpha}$-amylase production was obtained with 331.55unit/m1 at $2.0g/\ell$ of initial acetic acid concentration. ${\alpha}$-Amylase production was decreased with the increase of initial acetic acrid concentration. By adding acetic acid to the medium, cell growth and ${\alpha}$-amylase production was higher in glucose than in maltose. By adding lactic acid to the medium, cell growth was decreased.

• Applied Biological Chemistry
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• v.24 no.4
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• pp.252-259
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• 1981

The effects of tunicamycin (TM) on the growth and ${\alpha}-amylase$ productivity of B. amyloliquefaciens K were studied. The minimal growth inhibitory concentration was $0.25{\mu}\textrm{g}/m\ell$ and its ${\alpha}-amylase$ was stable up to $50^{\circ}C$. When the saking culture with $1{\mu}\textrm{g}/m\ell$ of Tunicamycin caused the change of cell shape from form rod to irregular circular form and the mycelium lysis. the grow th of His-, $TM^{\tau}$ mutant obtained by treatment of TM and ultraviolet ray was similar to that of the parent strain, but the productivity of ${\alpha}-amylase$, protease, and RNase was lower than that of the parent.

• 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.

• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.5
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• pp.831-838
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• 1996

This study was undertaken in order to elucidate the effects of raw, roast and steamed buckwheat on fecal protein, Pancreas weight, the activities of $\alpha-amylase,$ chymotrypsin and lipase 91 the pancreas, and $\alpha-amylase,$ chymotrypsin and trypsin activities of the feces in streptozotocin-induced diabetic rats. Fecal proteins of raw, roast and steamed buckwheat diabetic groups were increased up to 99%, 91%, 103%, respectively compared to those of the diabetic control group. Feeding of buckwheat diet increased pancreas weight, especially raw buckwheat diabetic group(p<0.05). Pancreatic chymo-trypsin activity was decreased in buckwheat diabetic groups compared to diabetic control group, wheres any significant difference was observed in $\alpha-amylase$ and lipase activities. Fecal chymotrypsin activi-ty was significantly increased in all buckwheat diabetic groups. Fecal trypsin activity was increased in roast buckwheat diabetic groups compared to diabetic control group and fecal $\alpha-amylase$ activity in buckwheat diabetic group was not significantly different. These results suggest that feeding of buckwheat diet enhances the impaired exocrine pancreatic function of diabetic rat.

• Journal of Environmental Science International
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• v.13 no.9
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• pp.827-833
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• 2004

The biodegradability of vinyl acetate acrylate resin and com starch blend was studied by determination of the reduced sugars produced after enzymatic hydrolysis. The starch hydrolysis reaction by $\alpha-amylase$ was achieved within 5 minutes. Optimal ranges of temperature and pH for the starch hydrolysis by $\alpha-amylase$ were around $80^{\circ}C$ and 6.5-7.2, respectively. The biodegradability of the starch-filled acrylate films increased as the content of starch increased. The biodegradation of starch in the starch-filled acrylate film by $\alpha-amylase$ was about 48.6% of that of pure starch. This value of biodegradable starch-filled acrylate film gave a good result with enzymatic shortcut test. The surface morphologies of the starch-filled acrylate film after enzymatic hydrolysis were investigated by scanning electron microscopy (SEM).

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1196-1199
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• 2004

A bacterium, isolated from rabbit's waste and identified as Cellulomonas sp., had cellulase and thermostable $\alpha$-amylase activity when grown on wheat bran. Maximum activity of thermostable $\alpha$-amylase was obtained by adding $3\%$ soluble starch. However, soybean oil (1 ml $1^{-1}$) could increase the production of $\alpha$-amylase and cellulase in 'wheat bran. The $\alpha$-amylase was characterized by making a . demonstration of optimum activity at $90^{\circ}C$ and pH 6- 9, with soluble starch as a substrate. The effect of ions on the activity and the stability of this enzyme were investigated. This strain secreted carboxymethyl cellulase (CMCase), cellobiase ($\beta$­glucosidase), and filter paperase (Fpase) during growth on wheat bran. Carboxymethy1cellulase, cellobiase, and Fpase activities had pH optima of 6, 5.5, and 6, respectively. CMCase and cellobiase activities both had an optimum temperature of $50^{\circ}C$, whereas Fpase had an optimum temperature of $45^{\circ}C$.

• Korean Journal of Food Science and Technology
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• v.20 no.5
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• pp.644-649
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• 1988

The inhibitory activities against bacterial ${\alpha}-amylase$of oriental drugs from animals, plant and mineral origin were investigated. In final screening test, it was found that Areca catechu L., Cinnamomum cassia Pres 1. and Ephedra sinica Stapf had stronger inhibitory activities against ${\alpha}-amylase$ than other oriental drugs used in this experiment.

• Journal of Microbiology and Biotechnology
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• v.1 no.4
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• pp.256-260
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• 1991

In B. subtilis, $\alpha$-amylase synthesis is regulated by amyR located directly on the upstream of amyE. Three different amyR alleles have been reported, amyR1, amyR2 and amyR3. Strains bearing the gra-10 mutation which confers derepression for catabolite repression has GlongrightarrowA transition mutation at ＋5 of amyR1. S1 nuclease mapping demonstrated that transcription initiated at 8 bases downstream from the -10 region of putative E$\sigma^{A}$ promoter P1 in amyR1 and gra-10. In amyR2, the major transcription initiatd at the same place and the minor, 10 bases downstream from -10 of P2. The transcript from P2 contributed approximately 15-20% of total amyE mRNA. S1 nuclease protection experiment indicated that amyE mRNA levels corresponded to the rate of synthesis assumed by specific activities of $\alpha$-amylase in culture supernatants, suggesting that $\alpha$-amylase synthesis is regulated at the level of transcription.n.