• 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.

• The Korean Journal of Food And Nutrition
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• v.9 no.1
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• pp.85-91
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• 1996

B-amylase(EC 3.2.1.2) was isolated from the root of arrowroot(Peuria thunbergiana Bentham) with distilled water and then fractionated with ammonium sulfate. Crude extract was partially purified by ion exchange chromatography and gel filtration. The enzymatic properties of partially purified $\beta$-amylase were as follows, the enzyme was fractionated with ammonium sulfate between 0.2 and 0.4 saturation, and showed the typical reaction properties of B-amylase producing only maltose from starch. Optinum pH and temperature were pH 6.5, $50^{\circ}C$ respectively. The activity of the enzyme had proportional relations with enzyme protein concentration below 4mg, and had Michaelis constant of 66.7mg% for soluble starch. The enzyme was inhibited by some metal louts such as silver, cadmium, mercury, aluminum, iron and copper.

• Journal of Microbiology
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• v.42 no.4
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• pp.319-327
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• 2004

An additional amylase, besides the typical $\alpha-amylase,$ was detected for the first time in the cytoplasm of B. subtilis SUH4-2, an isolate from Korean soil. The corresponding gene (bbmA) encoded a malto­genic amylase (MAase) and its sequence was almost identical to the yvdF gene of B. subtilis 168, whose function was unknown. Southern blot analysis using bbmA as the probe indicated that this gene was ubiquitous among various B. subtilis strains. In an effort to understand the physiological function of the bbmA gene in B. subtilis, the expression pattern of the gene was monitored by measuring the $\beta-galactosidase$ activity produced from the bbmA promoter fused to the amino terminus of the lacZ struc­tural gene, which was then integrated into the amyE locus on the B. subtilis 168 chromosome. The pro­moter was induced during the mid-log phase and fully expressed at the early stationary phase in defined media containing $\beta--cyclodextrin\;(\beta-CD),$ maltose, or starch. On the other hand, it was kept repressed in the presence of glucose, fructose, sucrose, or glycerol, suggesting that catabolite repression might be involved in the expression of the gene. Production of the $\beta-CD$ hydrolyzing activity was impaired by the spo0A mutation in B. subtilis 168, indicating the involvement of an additional regu­latory system exerting control on the promoter. Inactivation of yvdF resulted in a significant decrease of the $\beta-CD$ hydrolyzing activity, if not all. This result implied the presence of an additional enzyme(s) that is capable of hydrolyzing $\beta-CD$ in B. subtilis 168. Based on the results, MAase encoded by bbmA is likely to be involved in maltose and $\beta-CD$ utilization when other sugars, which are readily usable as an energy source, are not available during the stationary phase.

• KSBB Journal
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• v.22 no.2
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• pp.114-118
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• 2007

In this study, an amylase-producing fungus, strain 15 was isolated from soil in order to saccharify food wastes with cellulolytic and amylolytic enzymes. The amylase production cultures were performed in Mandel's medium with 1% rice straw and 1% paper wastes as carbon sources. The strain produced various cellulolytic (FPase 0.25, xylanase 20.09, CMCase 3.15 U/mL-supernatant) and amylolytic ($\alpha$-amylase 1.20, gluco-amylase 0.70, $\beta$-amylase 2.40 U/mL-supernatant) enzymes in Mandel's medium. In 10 L jar fermenter, maximum amylase and FPase activities, 3.25 and 0.23 U/mL, were obtained when the culture was grown at 30$^{\circ}C$, 200 rpm and 0.6 vvm for 3 days. In 100 mL flask level and 10 L jar fermenter, amylase produced by the strain 15 showed similar cellulolytic and amylolytic enzyme activities with Trichoderma inhamatum KSJ1 isolated from rotten woods by previous researcher. The ability of saccharification to food wastes also showed similar degree. However, the isolate 15 appeared to be yellowish in YMEA plate comparing to Trichoderma inhamatum KSJ1 in greenish.

• Korean Journal of Microbiology
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• v.40 no.3
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• pp.230-231
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• 2004

The mycelia of Sparassis crispa DSMZ 5201 were cultivated at $24^{\circ}C$ for 15 days in yeast-malt extract-glucose broth (pH 4.0) and the filtrate was used as crude enzyme solution to determined the extracellular enzyme activity. The specific activity of $\alpha$-amylase was 44.27 unit/protein. The specific activities of protease, CMCase, $\beta$-glucosidase, chitinase, exo-$\beta$-l,4-glucanase were relatively high. However, a very little activity of xylanase was found.

• YAKHAK HOEJI
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• v.6 no.2
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• pp.18-22
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• 1962

Purified preparation of .betha.-amylase is obtained from radish root by the means of fractional precipitation with ammonium sulfate. Purified preparation saccharifies the starch, .betha.-maltose being formed. Dextrinization in the true sense does not take place. Hydrolysis ceases when approximately 50% of the theoretical yield of maltose is obtained and there remains a substance (to be .betha.-limit dextrin) which gives a blue-violet with iodine, no glucose being formed. Stability of preparation is optimal at pH 4-9 and more completely inactivated at 65.deg. in fifteen minutes. .betha.-Amylase of radish exhibits optimal activity at and near pH 5.0, which varied depending upon the buffer. Calcium and chloride ions do not effect the activities of enzyme. The results of experiments with oxidizing, alkylating and mercaptide-forming reagents which have been reported to be specific for sulfhydryl groups confirm that free sulfhydryl groups are essential to the activity of .betha.-amylase from radish.

• Food Science and Biotechnology
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• v.17 no.3
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• pp.519-526
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• 2008

To improve the quality of traditional kochujang, strains with high protease and amylase activity were isolated and identified from Sunchang traditional kochujang. Twenty-three strains strongly producing protease and 16 strains strongly producing $\alpha$- and $\beta$-amylase were isolated by using 1% isolated soy protein agar medium and 2% starch agar medium, respectively. Protease activities of the IA7, I5, and IA2 strain were 22.5, 21.2, and 20.6 unit/mL, respectively, and were higher than those of the other strains. Stains with high $\alpha$-amylase activity included K9 (967.8 unit/mL), K14 (828.3 unit/mL), K13 (662.5 unit/mL), K8 (601.5 unit/mL), and K11 (405.9 unit/mL). The $\beta$-amylase activity of the K11 strain was the highest, 34.3 unit/mL, among the isolated strains. Based on morphological, physiological properties, and API 50CHB-kit test for assimilation of 49 carbohydrates, 8 strains selected according to protease, $\alpha$-amylase, and $\beta$-amylase activities were tentatively identified as Bacillus megaterium (IA2), Bacillus subtilis (IA7, 15), Bacillus amyloliquefaciens (K8, K9, K11, and K13), and Bacillus stearothermophillus (K14). The IA7, 15, and K11 strains were finally identified as B. subtilis (99% ID) based on 16S rDNA sequencing.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.39 no.2
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• pp.139-145
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• 1994

This study was intended to obtain the basic information on the germination status, changes of $\beta$-amylase activity and reducing sugar contents during seed germination of barley after an imposition of water stress by adding Polyethylene glycol solution. The effects of water deficit on germination were to be decreased in germination rate and velocity. Respiratory Quotient was increased as the osmotic potential in culture solution was decreased. But $\beta$-amylase activity and reducing sugar contents were decreased and the ratio of dry to fresh weight of germinated seeds was increased as the osmotic potential of the culture solution was decreased.

• Journal of Microbiology and Biotechnology
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• v.9 no.5
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• pp.619-623
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• 1999

The C-terminal starch-binding domain of Bacillus cereus $\beta$-amylase expressed in Escherichia coli was purified and crystallized using the vapor diffusion method. The crystals obtained belong to a space group of $P3_2$ 21 with cell dimensions, a=b=60.20${\AA},\; c=64.92{\AA},\; and \; \gamma = 120^{\circ}$ The structure was determined by the molecular replacement method and refined at 1.95 ${\AA}$, with R-factors of 0.181. The final model of the starch-binding domain comprised 99 amino acid residues and 108 water molecules. The starch-binding domain had a secondary structure of two 4-stranded antiparallel p-sheets similar to domain E of cyclodextrin glucanotransferase and the C-terminal starch-binding domain of glucoamylase. A comparison of the structures of these starch-binding domains revealed that the separated starch-binding domain of Bacillus cereus $\beta-Amylase$had only one starch-binding site (site 1) in contrast to two sites (site 1 and site 2) reported in the domains of cyclodextrin glucanotransferase and glucoamylase.

• Journal of the East Asian Society of Dietary Life
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• v.25 no.1
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• pp.139-145
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• 2015

This study evaluated the functional characteristics of saccharified buckwheat (Fagopyrum esculentum) following ${\alpha}$-amylase, ${\beta}$-amylase or glucoamylase treatment based on changes in soluble solid contents, rutin and quercetin contents, total polyphenols and DPPH radical scavenging activity. The results showed that the amylase treatments significantly influenced the saccharification time. Additionally, total polyphenol, rutin, and quercetin contents increased during the saccharification process; increase in phenolic compounds induced antioxidant activity. The present study demonstrated that buckwheat has a higher amount of functional compounds and higher antioxidant activity after saccharification. These results show that buckwheat saccharification can be used to increase antioxidant capacity and functional value for applications in functional food industries.