• Journal of the Korean Society of Food Science and Nutrition
• /
• v.14 no.2
• /
• pp.188-191
• /
• 1985

A thermophilic and cellulolytic bacterium, Herpetosiphon geysericola CUM 317 isolated from the compost, produced ${\alpha}-amylase,\;{\beta}-amylase$, and glucoamylase. Mutual relationships on the production of the three amylases were studied by changing the cultivation conditions. ${\alpha}-Amylase$ and glucoamylase were produced highly after 40 hrs on wheat bran medium at $50^{\circ}C$ and after 30 hrs on liquid medium at $40^{\circ}C$, though ${\beta}-amylase$ was produced best at 10 hrs of initial cultivation phase. The production of the amylases was generally repressed by the addition of carbon sources in liquid medium containing polypeptone. ${\alpha}-Amylase$ production was enhanced relatively by the addition of cupric sulfate in the liquid medium, ${\beta}-amylase$ was enhanced by cadmium sulfate, and glucoamylase was enhanced by calcium chloride.

• Korean Journal of Microbiology
• /
• v.11 no.2
• /
• pp.89-100
• /
• 1973

Dextrinogenic and saccharogenic amylase activities of Rhizopus isolated from various substrates collected throughout South Korea are measured, and their amylase activities are surveyed from taxnomical, ecological, and physiological viewpoints. Among the 151 strains of Rhizopus, strain number 49 exhibiting most prominent saccharogenic amylase activity is selected as a best strain, and strain number 17 is selected as a best strain for dextrinogenic amylase activity. Amylase activities of Rhizopus are so variable in different strains even in the same species. In general, however, R. japonicus, R. liquefaciens, and R. shanghaiensis show high saccharogenic amylase activities, and R.chiuniang, R.achlamydosporus, and R.bahrnensis show high dextrinogenic amylase activities, while R.nigricans exhibits lower activities for both amylase. The strains isolated from kneaded cereals, such as "meju" and "kockja", exhibited very strong dextrinogenic and saccharogenic amylase activities as compared with the strains isolated from other sunstrates. The mean value of dextrinogenic amylase activities of the strains from southern inland region and saccharogenic amylase activities of the strains from middle coast region are, more or less, higher than those of the strains from the other regions. In the culture at 30.deg.C, those strains which exhibit better mycelial and air mycelial growth than sporangial formation show very high dextrinogenic and saccharogenic amylase activities. amylase activities.

• Microbiology and Biotechnology Letters
• /
• v.10 no.4
• /
• pp.259-265
• /
• 1982

These experiments were conducted to investigate the hydrolysis products on the various oligosaccharides of Bacillus cirulans F-2 $\alpha$-amylase, and the hydrolysis rate on the various raw starches of Bacillus circulans F-2 $\alpha$-amylase, Bacillus amylotiquefaciens $\alpha$-amylase and Rhizopus niveus glucoamylase. The results obtained were as follows : 1. Maltotetraose, maltopentaose, maltohexaose, maltoheptaose and maltooctaose were hydrolyzed, but maltose and maltotriose were not hydrolyzed by Bacillus circulans F-2 $\alpha$-amylase. Among maltotetraose, maltopentaose, maltohexaose, maltoheptaose and maltooctaose, especially maltotetraose was hydrolyzed weakly by Bacillus circulans F-2 $\alpha$-amylase. 2. The Hydrolysis rate of oyster glycogen was slightly lower than soluble starch, amylose and amylopectin. 3. The hydrolysis rate of com starch was higher in shaking incubation than in stationary incubation, but the hydrolysis rate of potato starch was not definite according to kinds of enzyme. 4. On com, rice, arrowroot, high amylose corn, banana, sago, yam and potato starch, Bacillus circulans F-2 $\alpha$-amylase exhibited a remarkably higher hydrolysis rate than Bacillus amyloquefaciems $\alpha$-amylase and Rhizopus niveus glucoamylase.

• Korean journal of food and cookery science
• /
• v.14 no.3
• /
• pp.261-265
• /
• 1998

The activity and characteristics of ${\alpha}$-amylase in soy milk as well as in Jeungpyun batters were determined to investigate the enzyme system related to Jeungpyun preparation. ${\alpha}$-Amylase activity was detected in soy milk as well as in Jeungpyun batters. Soy milk had ${\alpha}$-amylase activity of 0.79 units/mg protein for gelatinized starch and 0.036 units/mg protein for raw starch. ${\alpha}$-Amylase in soy milk showed maximum activities at pH 5.92∼6.87 and at 60$^{\circ}C$ for both gelatinized starch and raw starch. ${\alpha}$-Amylase activities of Jeungpyun batters containing soy milk were 25.59 units/mg protein for gelatinized starch and 1.37 units/mg protein for raw starch. Jeungpyun batters without soy milk demonstrated ${\alpha}$-amylase activities of 3.37 units/mg protein for gelatinized starch and 0.49 units/mg protein for raw starch. ${\alpha}$-Amylase of Jeungpyun batters showed an optimal activity at pH 5.25 and at 60$^{\circ}C$ for both gelatinized and raw starch. The results demonstrated that Jeungpyun batters with soy milk showed significantly higher ${\alpha}$-amylase activity than the ones without soy milk.

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

• Journal of the Korea Academia-Industrial cooperation Society
• /
• v.22 no.6
• /
• pp.341-348
• /
• 2021

Serum amylase is a representative enzyme secreted by the salivary gland and pancreas. This study investigates the clinical significance of serum amylase levels in Sjögren's syndrome (SS). Totally, 70 female subjects were enrolled, who were diagnosed as SS and had no accompanying afflictions that affected the serum amylase levels. Unstimulated salivary flow rate (U-SFR) and stimulated SFR (S-SFR), salivary gland scan, and disease activity markers (ESSDAI and ESSPRI), as well as blood tests including ESR, CRP, and amylase, were evaluated. Serum amylase showed significant positive correlation with the U-SFR and S-SFR, and was increased with higher ejection fraction (EF) of the parotid gland. However, there was no significant correlation with disease activity and inflammatory markers. Based on their average amylase levels, subjects were divided into two groups. The group with higher serum amylase levels showed a statistically significant increase in the S-SFR and EF of the parotid gland. Considering the results of the salivary gland scan, we conclude that serum amylase is significantly correlated with SFR and the EF of the parotid gland, thereby indicating that the salivary gland function remains intact in SS.

• The Korean Journal of Physiology and Pharmacology
• /
• v.4 no.2
• /
• pp.129-135
• /
• 2000

Previously, we have reported that ${\rho}-chlorophenylalanine$ (PCPA), a serotonin depletor, profoundly increased pancreatic fluid and bicarbonate secretion but remarkably inhibited pancreatic amylase secretion in anesthetized rats. The present study was performed to verify the detailed effects of PCPA on pancreatic amylase synthesis that is directly related to amylase exocrine secretion. PCPA significantly decreased pancreatic RNA and protein contents as well as the amylase activity. However, pancreatic DNA content, trypsin and chymotrypsin activities were not influenced by the treatment of PCPA. The rate of pancreatic amylase synthesis, which was assessed by the amount of incorporated $[^{35}S]-methionine$ into amylase for 1 h, was also significantly decreased by 44% in PCPA-treated rats. In order to determine whether the PCPA-induced decrease of amylase synthesis resulted from change in the level of amylase mRNA, Northern blot analysis was performed. The mRNA expression level of amylase was also decreased by 48% in the PCPA-treated rats, indicating that the inhibitory effect of PCPA on the synthesis of pancreatic amylase was mainly regulated at a step prior to translation. It was also revealed in SDS-polyacrylamide gel electrophoresis that the qualitative change of amylase was induced by PCPA. The 54 KDa amylase band seems to be degraded into small molecular weight protein bands in PCPA-treated rats, suggesting that the PCPA- induced decrease of amylase may be partly attributed to the degradation of synthesized amylase.

• Journal of Sericultural and Entomological Science
• /
• v.24 no.2
• /
• pp.73-80
• /
• 1983

1. The varietal difference in amylase activity of the digestive fluid of the 5th instar larvae reared on the artificial diet was investigated, using the parent commercial silkworm varieties of Japanese strain. The amylase activity was large different among silkworm varieties. The activity was strong in Hansaeng-1, Jam 115 and Jam 117, medium in Hansaeng-3, Jam 113, Jam 119, and Jam 201, weak in Jam 107, Jam 121 and Gyeongchu. The amylase of the digestive fluid of ten parent commercial silkworm varieties is possible-(ae) type, compared with ＋(＋$\^$ae/) type of Daizo. 2. To investigate the effect of a-amylase pre-treatment of the artificial diet, larvae were fed with the diet treated by a-amylase during 4th-5th instar periods. The blood sugar content and cocoon qualities were slightly higher in the experimental larvae than those in the control, while showing the slight less body weight, amylase activity and dietary efficient.

• YAKHAK HOEJI
• /
• v.33 no.3
• /
• pp.175-182
• /
• 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
• /
• v.32 no.1
• /
• pp.34-39
• /
• 1994

The gene encoding ${\alpha}$-amylase of Schwanniomyces castellii was cloned in Saccharomyces cerevisiae. The 5.0-kilobase insert was shown to direct the synthesis of ${\alpha}$-amylase. Southern blot analysis confirmed that this ${\alpha}$-amylase gene was derived from the genomic DNA of Sch. castellii. Immunoblot analysis showed that ${\alpha}$-amylase production from S. cerevisiae transformant was less than that of donor strain. The ${\alpha}$-amylase secreted from S. cerevisiae transformant was shown to be indistinguishable from that of Sch. castellii on the basis of molecular weight and enzyme properties.