• Microbiology and Biotechnology Letters
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• v.13 no.3
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• pp.223-232
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• 1985

To find microorganisms of producing $\alpha$-amylase inhibitors, actinomycetes were isolated from soil samples that were collected at different locations in Korea and screened for enzyme inhibitory activity. A strain of these microbes had a high inhibitory activity and was identified as one of the genus Streptomyces by morphological, biochemical and physiological studies according to the methods of the International Streptomyces Project (ISP). The medium used consisted of 3 ％ corn starch, 0.2％ yeast extract and 0.8％ peptone (pH 7.0). When this strain was aerobically cultured in the medium on a rotary shaker, the highest inhibitory activity was obtained after four days. This inhibitor had inhibitory activities on various $\alpha$-amylases and glucoamylase, but not on $\beta$-amylase.

• Journal of Plant Biology
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• v.21 no.1_4
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• pp.21-27
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• 1978

The effect of tannic acid on GAs and cyclic-AMP promoted amylase induction in barley aleurone layers was examined. Of a variety of adenine compounds, only cyclic-AMP and ADP showed significant activity, and these activities were promoted by addition of theophylline to the incubation medium. When aleurone layers of barley endosperm tissues were incubated with GAs in the presence of tannic acid, the amylase activity in the incubation medium was reduced. Cyclic-AMP induced amylase activity was also reduced by additiion of tannic acid. The cyclic-AMP response promoted was more sensitive to tannin inhibition than GAs response. The inhibitory effect of tannic acid shwoed reversibility by addition of higher concentration of GAs or cyclic-AMP. The tannic acid effect on GAs response was also recovered by addition of a higher concentration of cyclic-AMP. Experiment with polyacrylamide disc electrophoresis showed different isozyme patterns according to the additions in the incubation medium. Inhibitory effects of decursinol and coumarin was compared with that of tannic acid. They showed different zymogram patterns.

• Journal of Sericultural and Entomological Science
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• v.15 no.1
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• pp.1-7
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• 1973

his study has been carried out to investigate amylase activity of digestive juice in the 5th day of the 5th instar influenced by the dietary composition (quantitative ratio between carbohydrate and protein) and the rearing temperature during the 4th moulting period. The larvae grew on three kinds of semi-synthetic diets. The A-diet has more carbohydrate than the others, the B-diet has carbohydrate in 1 : 2 with protein, and the C-diet has more protein than the others. All the diets were kept at 16$^{\circ}C$, 25$^{\circ}C$ and 32$^{\circ}C$ during the 4th moulting period. Amylase activity of digestive juice at the 5th day of the 5th instar was analyzed by Fuwa's method. The results were as follows. 1. Both A and C-diets were worse than B-diet in the larval growth and development. 2. The dietary composition influencing amylase activity of digestive juice was not related to the rearing temperature during the 4th moulting period. Amylase activity was stronger in C-diet, B-diet and A-diet order. 3. It was found that amylase activity at 32$^{\circ}C$ was stronger than that at 16$^{\circ}C$ in all kinds of diets. 4. There was an inter-action in amylase activity of male larval digestive juice between the dietary composition and the rearing temperature during 4th the moulting period.

• Journal of Microbiology and Biotechnology
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• v.20 no.3
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• pp.563-568
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• 2010

The Val289 residue in the $\alpha$-amylase of Bacillus amyloliquefaciens, which is equivalent to the Ala289 and Val286 residues in the $\alpha$-amylases of B. stearothermophilus and B. licheniformis, respectively, was studied by site-directed mutagenesis. This residue was substituted with 10 different amino acids by random substitution of the Val codon. In these mutant $\alpha$-amylases, Val289 was substituted with Ile, Tyr, Phe, Leu, Gly, Pro, Ser, Arg, Glu, and Asp. Compared with the wild-type $\alpha$-amylase, the mutant $\alpha$-amylase Val289Ile showed 20% more hydrolytic activity, whereas Val289Phe and Val289Leu showed 50% lesser activity. On the other hand, the mutant $\alpha$-amylases Val289Gly, Val289Tyr, Val289Ser, and Val289Pro showed less than 15% activity. The substitution of Val289 with Arg, Asp, or Glu resulted in complete loss of the $\alpha$-amylase activity. Interestingly, the mutant $\alpha$-amylase Val289Tyr had acquired a transglycosylation activity, which resulted in the change of product profile of the reaction, giving a longer oligosaccharide.

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.1
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• pp.67-73
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• 1999

In order to increase the enzymatic activity of malt used as a source of traditional processing foods, the enzymatic activities of various barley were examined and the effects of ozone and light illumination treatment on the enzymatic activities of amylase, amylase, and glucanase in malt during man ufacture were also examined. Barley didn't show amylase activity prior to soaking, but the activity of barley increased quickly after soaking. Glutinous barley showed the highest amylase activity among Duru barley, Ol barley, two rowed barley and naked barley. Naked barley showed the lowest activity. The amylase activity was the highest in Duru barley and decreased in the order of in glutinous barley, naked barley and two rowed barley. It was showed that the enzymatic activity of malt was higher than that of control when malt was soaked for 24hr at the concentration of 0.3ppm of ozone. The enzymatic activity of malt treated with light illumination was higher than that of control. The bud and root of light illuminated malt was much stronger than that of control. The root of light illuminated malt was much shorter than that of control. In addition, light illuminated malt showed a little green color which matches the demand of consumer. These studies demonstrated that both ozone and light illumination treatment increased the enzymatic activity of malt to result in high quality of malt manufacture.

• YAKHAK HOEJI
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• v.33 no.3
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• pp.175-182
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• 1989

To find ${\alpha}-amylase$ inhibitors produced by microorganisms from soil, a strain which had a strong inhibitory activity against bacterial ${\alpha}-amylase$ was isolated from the soil sample collected in Korea. The morphological and physiological characteristics of this strain on several media and its utilization of carbon sources showed that it was one of Streptomyces species according to the International Streptomyces Project method. The amylase inhibitor of this strain was purified by active carbon adsorption, silicagel column chromatography, SP-Sephadex C-25 column chromatography, adsorption on Amberlite XAD-2. The inhibitor was oligosaccharide which was composed of glucose. The inhibitor had inhibitory activity against other amylase such as salivary ${\alpha}-amylase$, pancreatic ${\alpha}-amylase$, fungal ${\alpha}-amylase$ and gluco-amylase.

• Korean Journal of Microbiology
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• v.15 no.2
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• pp.63-76
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• 1977

Irradiation with high doses of gamma rays induced the reduction of mycelial weight and anaylase activity, and increased relative amylase activity in surface cultures. Biphase in growth curves was shown in aeration-agitation cultures but the behavior of the first phase of growth could be eliminated by replacing the amylasehydrolysed starch substrates, so that enzyme production was shortened ca. 40 hours and relative amylase activity was increased about 3 times higher before onset of autolysis. In the effect of gibberellin on amylase production, the positive stimulation was appeared to only surface culturs of the liquid medium and the negative effect to shake-cultures in a mutant. Trials of various continuous culture were resulted not only the approalch to the value of amylase activity in surface cultures of liquid medium, but also higher productivity than in batch cultures. The culture-degeneration was observed in two-stage continuous culture, but did not appear in continuous elevation culture.

• 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 $45^{\circ}C$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.6
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• pp.812-815
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• 2009

The effects of processing conditions on the ${\alpha}$-amylase activity of radish were investigated at various temperatures, pHs and drying conditions. The ${\alpha}$-amylase activity of radish root was 3.1-fold higher than that of radish trunk. As the freeze-dried radish was incubated at various temperatures and pHs, ${\alpha}$-amylase activity was stably maintained at pH range of $4{\sim}7$ and temperature of $25{\sim}40^{\circ}C$. When radish was processed to kakdugi and danmooji, the residual ${\alpha}$-amylase activity was 45.39% and 19.19%, respectively. Consequently, the ${\alpha}$-amylase activity was greatly affected by processing conditions such as heat treatment and pH. It is suggested that radish should be processed at below $60^{\circ}C$ and at neutral to acidic pH condition.

• Microbiology and Biotechnology Letters
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• v.13 no.1
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• pp.7-11
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• 1985

In order to investigate the biological activity of ginseng saponins, the effects of ginseng saponins on the reaction catalyzed by bacterial a-amylase were studied and the results obtained were summerized as follows. Bacterial ${\alpha}$-amylase activity was increased by the addition of protopanaxadiol (diol), protopanaxatriol (triol) and total saponin. Preincubation of ${\alpha}$-amylase with diol saponin at $40^{\circ}C$ for 3 min increased ${\alpha}$-amylase activity to the degree of 120%. In the protective effect on the heat denaturation of the enzyme, triol saponin protected the heat denaturation for 5 min at $60^{\circ}C$, but diol saponin accelerated the heat denaturation. The hydrolyzates of diol and triol saponin increased the enzyme activity more than the intact diol and triol saponin. In the catalysis system of bacterial ${\alpha}$-amylase, the addition of diol and triol saponin reduced the substrate inhibition in the presence of high concentration of the substrate.