• KOREAN JOURNAL OF CROP SCIENCE
• /
• v.7 no.1
• /
• pp.123-127
• /
• 1969

The studies were conducted to know the relationship between $\beta$-amlyase activities and hardiness for the germinated seedlings of, winter wheat varieties which were classified with eye estimated cold resistance in field as, susceptible, moderate and resistant. These varieties were tested in continued five days from germination in four replicated split plot design. For the measurement of $\beta$-amylase, improved A. K. Balls method (2) was employed. Result obtained will be summarized as follows. 1. Tested varieties showed highly significant differences in $\beta$-amylase activity, while no differences were obtained between dates after germination. 2. Winter hardy varieties, Yukseung ＃3, Chin Kwang and Suwon＃85 showed higher amylase activities than the moderate hardy varieties, Jukdalma, Kangdosinryuk and Norin ＃4, while lower activities were measured in susceptible varieties, Norin ＃6, Kangdo and Norin＃12. 3. With measurement of $\beta$-amylase activity, rurther detail classification to cold resistance is seemed available than eye-estimating in the field condition. 4. In accordance with testing dates, amylase activities were not so clear on 1st, 2nd, 4th and 5th days from germination, while clear differences were found on 3rd day from germination. 5. Amylase activity obtained on 3rd day after germination is considered easy and effective method to estimate cold resistance of wheat varieties with a classification standard.

• KSBB Journal
• /
• v.19 no.4
• /
• pp.301-307
• /
• 2004

The characteristics of the a-amylase of Aspergillus coreanus NR 15-1 isolated from traditional Korean Nuruk have been carried out. The a-amylase of A. coreanus NR 15-1 was purified by ammonium sulfate precipitation followed by column chromatographies on CM-cellulose, DEAE-cellulose, Sephadex G-100 gel filtration and hydroxyapatite. The a-amylase was purified 78-fold with a yield of 8.7%. The molecular weight of the a-amylase was estimated to be 49 kDa by Sephadex G-100 gel filtration and 51 kDa by SDS-polyacrylamide gel eletrophoresis. These experimental results suggested that the purified enzyme might be monomer. The enzyme was stable between pH 4 and 11. The optimum pH was 5.0. The optimum temperature for enzyme was 45$^{\circ}C$ and the enzyme was stable up to 50$^{\circ}C$. The enzyme was significantly inhibited by 1 mM N-bromosuccinimide. These results suggested that tryptophan residue was involved in the active site of a-amylase. The enzyme was identified as a-amylase because the reaction products of soluble starch hydrolyzed by the purified enzyme was oligosaccharide by thin layer chromatography.

• Applied Biological Chemistry
• /
• v.48 no.1
• /
• pp.103-108
• /
• 2005

${\alpha}-Amylase$ inhibitor is used to control blood glucose level by inhibiting starch digestion in the small intestine and delaying the absorption of glucose. In this study, we investigated the effect of the ethanol extracts from more than 1400 species of plants against ${\alpha}-amylase$ with the aim of developing a new ${\alpha}-amylase$ inhibitor. In the results, Cornus walteri extracts showed the highest inhibition activity. The inhibitory effect of Cornus walteri extract on the carbohydrate hydrolysis enzymes has different sensitivities against ${\alpha}-amylase$ from salivary and pancreatin and against ${\alpha}-glucosidase$ from yeast and porcine small intestine. In the study of inhibition kinetics of ${\alpha}-amylase$ and ${\alpha}-glucosidase$, Cornus walteri extract showed competitive inhibition against salivary and pancreatin while showing the combination of uncompetitive and noncompetitive inhibition against ${\alpha}-glucosidase$. The Cornus walteri extract was stable at acidic and thermal conditions. As for the blood glucose and body weight levels of Cornus walteri extract, we confirmed anti-hyperglycemic and anti-obesity effects. Also, in the investigation of the mRNA lever, Cornus walteri extract upregulated the level of GLUT4 mRNA in the quadriceps muscle.

• Microbiology and Biotechnology Letters
• /
• v.14 no.6
• /
• pp.479-485
• /
• 1986

A 5200 basepair DNA fragment containing the Bacillus amyloliquefaciens amyE gene, encoding liquefying $\alpha$-amylase (1,4-$\alpha$-1)-glucan glucanohydrolase, EC 3.2.1.1), has been inserted into BamHI site of the pUB110 and the hybrid plasmid was designated as pSKS3. The pSKS3 was transformed into the Bacillus subtilis KM2l3 as a host which is a saccharifying $\alpha$-amylase deficient mutant of Bacillus subtilis NA64, and the plasmid in the transformed cell was expressed $\alpha$-amylase production and kanamycin resistance. The $\alpha$-amylase production of the transformed cell was reduced to one fifth of that of the donor strain. The Bacillus subtilis KM2l3 tarring pSKS3 indicated that the amyE gene product is a polypeptide which has the same electrophoretic mobility with that of the Bacillus amyloliquefaciens, but different from the saccharifying $\alpha$-amylase of Bacillus subtilis NA64. It means that the amyE gene of pSKS3 originales from the Bacillus amyloliquefaciens.

• Microbiology and Biotechnology Letters
• /
• v.45 no.4
• /
• pp.277-283
• /
• 2017

To produce sweet liquor without artificial sweeteners, 8 traditional rice pre-treatment methods (juk, beombeok, seolgitteok, gumeongtteok, mulsongpyeon, injeolmi, gaetteok, and godubap) were analyzed in this study. The formation of sugars with the help of ${\alpha}$-amylase, ${\beta}$-amylase, and glucoamylase using nuruk as a substrate has been previously confirmed. During the early stages of the pre-treatment processes, the amount of maltose produced (in descending order of its concentration) by ${\alpha}$-amylase was observed to be as follows: gaetteok > seolgitteok > beombeok > mulsongpyeon > juk > injeolmi > gumeongtteok > godubap. However, changes in maltose concentrations with respect to the pre-treatment processes after 48 hours were observed to be as follows: injeolmi > beombeok = godubap > gumeongtteok > gaetteok = mulsongpyeon > seolgitteok > juk. Maltose produced using either ${\alpha}$-amylase or ${\beta}$-amylase showed similar results. Glucoamylase produced 10 mg/ml of glucose during the godubap process, which was the highest amount of glucose among all the methods. Moreover, when ${\alpha}$-amylase, ${\beta}$-amylase, and glucoamylase were used concurrently, glucoamylase increased glucose production in the later stages. Therefore, the possibility of producing sweet liquor without employing artificial sweeteners was confirmed, even if the amount of sugar in the liquor varied with the pre-treatment process.

• Food Science and Preservation
• /
• v.21 no.2
• /
• pp.286-293
• /
• 2014

In this study, one GRAS strain was screened from doenjang, a traditional Korean fermented food, as a microorganism producing amylase due to the formation of a clear zone on the medium including soluble starch. From the analysis of the gene sequence of 16S ribosomal RNA, the strain was identified as Bacillus subtilis and was therefore named Bacillus subtilis CBD2. When the nutrient broth medium was prepared with 3% NaCl, 5% glucose, and the initial medium pH 7.0, the B. subtilis CBD2 showed maximum growth. Among soluble starch, corn starch, maize amylopectin, and wheat starch, soluble starch was the most effective carbon source in the production of amylase by B. subtilis CBD2. The amylase from B. subtilis CBD2 showed the highest activities at pH 8.0 and $50^{\circ}C$, and corn starch was the most proper substrate for the enzyme activity. When corn starch was used as a substrate, the production of sugars through enzyme activity increased for 24 h, and then the enzyme activity became constant.

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

• Applied Biological Chemistry
• /
• v.41 no.1
• /
• pp.18-22
• /
• 1998

A mutant strain which hyperproduced thermostable ${\alpha}-amylase$ was obtained by chemical mutagenesis of Bacillus licheniformis. The mutant strain, SK-5, produced the enzyme about 50 times higher than the original strain. The mutant was longer and slimmer in shape, slower in growth compared to the original strain. Nucleotide sequence analysis of the SK-5 ${\alpha}-amylase$ gene revealed no changes in the the structural gene. The changes found in the promoter region might be responsible for the hyperproduction of the enzyme by the mutant. No structural changes in the enzyme structure could be observed when the secreted enzymes at various culture times were analyzed by Western blot.

• Applied Biological Chemistry
• /
• v.13 no.3
• /
• pp.231-235
• /
• 1970

1. Purification of amylase system produced from Humicola sp. by a submerged culture eras carried out. 2. By DEAE-Cellulose column chromatography amylase system was separated into two fractions eluted at 0.05M and 0.5M phosphate buffer solution of pH 6.0. 3. The saccharogenic amylase was mostly composed of. the fraction of 0.05M phosphate buffer solution of pH 6.0 while the dextrinogenic amylase was perseted in fraction of 0.5M phosphate buffer solution of pH 6.0 4. It was found that the optimum pH of this saccharogenic amylase was within the range of from 4.5 to 5.5, stable pH was within the range of from 4.0 to 9.0 and optimum temperature was $60-65^{\circ}C$. This amylase was stable at $70^{\circ}C$ for ten minutes but completely inactivated $80^{\circ}C$ above.

• Korean Journal of Food Science and Technology
• /
• v.17 no.4
• /
• pp.237-239
• /
• 1985

The effects of red light on the $\alpha$-amylase activity of barley during germination was studied. The $\alpha$-amylase activity was highest at 5th day on germination, showing rapid increase from the 3rd-day of germination. The highest activity of $\alpha$-amylase was shown among the groups treated by red light at 100 Lux luminous intensity for 3 hours a day. The $\alpha$-amylase activity of barley during germination under the red light increased to 44% compared with that of barley during germination under the dark. The protein content was not increased by red light.