• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.160-164
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• 1989

A 5.7Kb EcoRI fragment containing alkaline amylase gene of Bacillus sp. AL-8 obtained in the previons experiment (10) was transformed in B. subtilis via plasmid pUB110. The enzymatic proper-ties of the amylase produced by the transformants were Identical to those of the donor strain. Thus, the alkaline amylase activity from the transformant was maximum at pH 10 and 5$0^{\circ}C$. And the enzyme was very stable over the ranges of alkaline pH. In order to determine the location of the alkaline amylase gene within the 5.7Kb DNA fragment, the fragment was subcloned in E. coli. It was found that the alkaline amylase gene was located k EcoRI fragment of 3.7Kb.

• Preventive Nutrition and Food Science
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• v.20 no.3
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• pp.210-214
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• 2015

Grape pomace is an abundant source of underutilized winery by-products. Polyphenols were extracted from grape pomace using cellulase and gluco-amylase enzymes. 2,2-diphenyl-1-picrylhydrazyl (DPPH) and Folin-Ciocalteu's assays were used to measure antioxidant activity and total polyphenolic contents. Both cellulase, and gluco-amylase digested grape pomace showed efficient radical scavenging activity. In addition, the total polyphenolic contents of cellulase digested grape pomace showed lower concentrations were effective compared to higher concentrations, whereas glucoamylase enzyme did not show remarkable variations. The DPPH radical scavenging activity and total polyphenolic contents were significantly higher in the cellulase digested grape pomace compared to the gluco-amylase digested and the not digested grape pomace. It is notable that enzymatic digestions were efficient for extracting polyphenols from grape pomace. The underutilized grape pomace polyphenols can be further used for food safety as a natural antioxidant.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.44 no.6
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• pp.791-795
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• 2011

This study examined the inhibitory activity of Ecklonia cava (EC) against ${\alpha}$-amylase to evaluate the availability of EC extract as a functional food agent. To verify the inhibitory activity of EC against porcine pancreatic ${\alpha}$-amylase, potato starch was used as a substrate. This analysis revealed that EC ethanol extract exhibited high ${\alpha}$-amylase inhibitory activity. For potential application within the food industry, the stability of the activity of EC ethanol extract under various heat and pH conditions was examined. The ${\alpha}$-amylase inhibitory activity of EC ethanol extract was not affected by the heat and pH treatment conditions used in this study. These results suggest that EC has the potential for development as a functional food agent.

• 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.

• 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.

• Journal of Microbiology and Biotechnology
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• v.9 no.3
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• pp.260-264
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• 1999

The combined activities of dextranase and amylase(DXAMase) from Lipomyces starkeyi KSM 22 produced from starch fermentation inhibited or prevented dental plaque formation. The activities were stable in commercial mouthwash products; DXAMase activity retained over 93％ of original activity after 6 months at 23℃. We examined the effects of enzyme inhibitors and active ingredients in mouthwash on DXAMase activity. The DXAMase was stable with 0.29％(w/v) EDTA, 20％ (v/v) ethanol, 0.05％ (w/v) fluoride, and 0.05％ (w/v) SDS. Among the active ingredients of mouthwash, sodium benzoate (up to 1 ％, w/v) had no inhibitory effect on either dextranase or amylase activity. In the case of cetylpyridinium chloride, the addition of 0.05％ (w/v) inhibited 6％ of dextranase activity and 13％ of amylase activity. Propylene glycol (up to 1％, w/v) showed no inhibitory effect on either enzyme activity. DXAMase (5 IU/㎖) in mouthwash could remove pre-formed films of glucan-bound S. mutans cells. The addition of 0.1 IU/㎖ DXAMase in mouthwash prevented the formation of insoluble-glucan. These in vitro properties of L. starkeyi KSM 22 DXAMase are desirable for its application as a dental plaque control agent.

• Journal of Microbiology and Biotechnology
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• v.23 no.4
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• pp.489-498
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• 2013

A new Bacillus strain degrading starch, named Bacillus sp. UEB-S, was isolated from a southern Tunisian area. Amylase production using solid-state fermentation on millet, an inexpensive and available agro-resource, was investigated. Response surface methodology was applied to establish the relationship between enzyme production and four variables: inoculum size, moisture-to-millet ratio, temperature, and fermentation duration. The maximum enzyme activity recovered was 680 U/g of dry substrate when using $1.38{\times}10^9$ CFU/g as inoculation level, 5.6:1 (ml/g) as moisture ratio (86%), for 4 days of cultivation at $37^{\circ}C$, which was in perfect agreement with the predicted model value. Amylase was purified by Q-Sepharose anion-exchange and Sephacryl S-200 gel filtration chromatography with a 14-fold increase in specific activity. Its molecular mass was estimated at 130 kDa. The enzyme showed maximal activity at pH 5 and $70^{\circ}C$, and efficiently hydrolyzed starch to yield glucose and maltose as end products. The enzyme proved its efficiency for digesting raw cereal below gelatinization temperature and, hence, its potentiality to be used in industrial processes.

• Journal of environmental and Sanitary engineering
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• v.23 no.1
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• pp.25-31
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• 2008

A bacterial strain, Bacillus megaterium L-49 has been isolated and identified that produces alkaline ${\alpha}$-amylase. The cell is ellipsoidal, about $1.0-1.2{\times}3.0-3.6{\mu}m$ in diameter, Gram-positive, motile, and central partial central. Growth occurs in media containing 7% of NaCl. This strain could utilize D-glucose, lactose, xylose, sucrose, mannose, and maltose, and but it does not utilize D-fructose, and glycogen. Among the various concentrations of saturated ammonium sulfate, the retractation ratio in range of 70 to 100% was about 93%. However, in the case of acetone, it was about 98.7%. EDTA has activating effect and Ca2+ has no effect on alkaline ${\alpha}$-amylase activity. The alkaline ${\alpha}$-amylase has low thermal stability. The optimal temperature for reaction is $50^{\circ}C$. The alkaline ${\alpha}$-amylase activity maintained stabilizing at pH 6-11 and the optimal pH for reaction was 9-10.

• Journal of the Korean Society of Food Science and Nutrition
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• v.44 no.5
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• pp.681-686
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• 2015

The purpose of this study was to measure total phenolic compounds as a measure of antioxidant activity as well as ${\alpha}$-amylase inhibitory and ${\alpha}$-glucosidase inhibitory activities as a measure of anti-diabetic efficacy in methanol extracts from 23 kinds of medicinal plants. Extracts of three medicinal plant species showing high total polyphenol contents were selected (Euonymus alatus stem, Taxus cuspidata fruit, and Eucommia ulmoides leaf). Extracts of six medicinal plant species showing over 60% DPPH radical scavenging activity were also selected [Eucommia ulmoides barks (80.10%), Lycium chinense roots (64.25%), Euonymus alatus stem (73.59%), Lespedeza cuneata (78.20%), Taxus cuspidata fruits (70.52%), and Tilia taquetii leaf and stem (67.81%)]. Regarding ${\alpha}$-glucosidase and ${\alpha}$-amylase inhibitory activities acarbose showing approximately 80% inhibitory activity was selected as a control group, and six species (Eucommia ulmoides heartwood, Eucommia ulmoides bark, Euonymus alatus stem, Dioscorea batatas, Coix lachryma-jobi, and Phaseolus radiatus) showed greater than 80% ${\alpha}$-glucosidase inhibitory activity. Extracts of nine medicinal plant. species showing over 80% ${\alpha}$-amylase inhibitory activity (Pueraria thunbergiana root, Eucommia ulmoides bark, Eucommia ulmoides leaf, Lycium chinense fruits, Euonymus alatus leaf and stem, Euonymus alatus stem, Sasa borealis whole, Dioscorea batatas leaf and stem, and Tilia taquetii leaf and stem). Based on these results, medicinal plants showing high antioxidant and antidiabetic activities can be used as fundamental products in developing new medicines, as well as functional foods to prevent adult disease.

• Journal of Microbiology and Biotechnology
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• v.2 no.2
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• pp.85-91
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• 1992

The intestinal microflora of humans is an extraordinarily complex mixture of microorganisms, the majority of which are anaerobic microorganisms. The distribution of amylolytic microorganisms in the human large intestinal tract was investigated in various individuals of differing ages using anaerobic culture techniques. A large percentage of the amylolytic microorganisms present belonged to the Genus Bifidobacteria. The number of Bifidobacteria increased significantly at two years of age. Adults and children above 2 years old carried about $0.8{\times}10^9-2.0{\times}10^{10}$ colony forming units (CFU/gram) of amylolytic Bifidobacteria. Among these amylolytic Bifidobacteria, Int-57 was chosen for further studies. Between 65% and 85% of the amylase produced was secreted and the remaining amylase was bound to the cell wall facing the outside. Amylase production could be induced by starch in a stable form. When cells were grown on maltose or glucose, amylase production was much lower than on starch and amylase activity disappeared after 24 hours growth on these media. Partially purified enzymes showed optimum activity at a temperature of $50^{\circ}C$ and at an optimum pH of 5.5, respectively. Heat treatment at $70^{\circ}C$ for 30 minutes almost completely inactivated amylase. The hydrolysis products of starch were mainly maltose and maltotriose. Soluble starch, amylose, amylopectin, and $\gamma$-cyclodextrin($\gamma$-CD) were easily hydrolyzed. The rate of hydrolysis of $\alpha$-CD and $\beta$-CD was slower than that of $\gamma$-CD. Carboxymethyl cellulose, $\beta$-1, 3-glucan and inulin were not hydrolyzed.