• 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.

• Journal of Microbiology and Biotechnology
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• v.21 no.5
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• pp.470-476
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• 2011

A potent fungus for amylase production, Chrysosporium asperatum, was isolated from among 30 different cultures obtained from wood samples collected in the Junagadh forest, India. All of the isolated cultures were screened for their ability to produce amylase by submerged fermentation. Among the selected cultures, C. asperatum (Class Euascomycetes; Onygenales; Onygenaceae) gave maximum amylase production. In all of the different media tested, potato starch was found to be a good substrate for production of amylase enzyme at $30^{\circ}C$ and pH 5.0. Production of enzyme reached the maximum when a combination of starch and 2% xylose, and organic nitrogen (1% yeast extract) and ammonium sulfate were used as carbon and nitrogen sources, respectively. There was no significant effect of metal ions on enzyme activity. The enzyme was relatively stable at $30^{\circ}C$ for 20 min, and no inhibitory effect of $Ca^{+2}$ ions on amylase production was observed.

• 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.

• Applied Biological Chemistry
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• v.41 no.1
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• pp.18-22
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• 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
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• v.13 no.3
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• pp.231-235
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• 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
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• v.17 no.4
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• pp.237-239
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• 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.

• The Korean Journal of Mycology
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• v.13 no.4
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• pp.203-212
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• 1985

Of 450 strains isolated from the soil microbes collected in various locations in Korea, a strain had a strong inhibitory activity against bacterial ${\alpha}-amylase$ and was named strain DMC-72 of the genus Streptomyces. The amylase inhibitory metabolite produced by this strain was purified by means of acetone precipitation, adsorption on Amberlite IRC-50 and SP-Sephadex C-25. The inhibitor was found to be a derivative of oligosaccharides by spectral and chemical data. The inhibitor was stable at the pH range of $1{\sim}13$ and at $100^{\circ}C$ for half an hour, also inhibited other amylases such as salivary ${\alpha}-amylase$, pancreatic ${\alpha}-amylase$, fungal ${\alpha}-amylase$ and glucoamylase. However, it showed no inhibitory activity against ${\alpha}-glucosidase$, ${\beta}-glucosidase$, dextranase, and ${\beta}-amylase$. The kinetic studies of the inhibitor showed that its inhibitory effects on starch hydrolysis by ${\alpha}-amylase$ were noncompetitive.

• Journal of Chest Surgery
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• v.16 no.1
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• pp.83-90
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• 1983

During the period of March 1981 to September 1982 a series of survey has been done on the value of amylase in blood and urine of 24 patients who went through the operation of heart surgery, for congenital and acquired heart diseases, with extracorporeal circulation at the Department of Thoracic _ Cardiovascular Surgery, School of Medicine, Hanyang University. In order to analyze the iteration and inter-relation of the value of amylase in blood and urine and the extra corporeal circulation time. The duration of extra-corporeal circulation time up to 60 minutes was classified as Group A while above 60 minutes was classified as Group B. The results are as follow; 1. 3 patients [23.07%] among 13 patients of Group A and 3 patients [27.27%] among 11 patients, showed increased amylase value after the surgery. 2. The average value in blood after operation was 120.3190.71 unit in Group A and 130.90113.15 unit in Group B. It was 11.59 units [9.63%] higher in Group A than in Group B. 3. 1 patient [7.7%] among 13 patients of Group A and 2 patients[18.18%] among 11 patients of Group B, the frequency of Group B was 10.48% higher. 4. The average Value of amylase in urine after the surgery was 111.9254.87 unit in Group A and 151.54111.17 unit in Group B. It was 39.62 unit [32.72%] higher in Group A than in Group B. 5. The longer the duration of extra corporeal circulation time showed the higher the amylase value in blood and urine after the operation. 6. Although the value of amylase in blood and urine was increased after operation, no patients Were found to have developed clinical pancreatitis.

• Restorative Dentistry and Endodontics
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• v.38 no.3
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• pp.141-145
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• 2013

Objectives: Assessment of dental pain severity is very challenging in dentistry. Previous studies have suggested that elevated salivary alpha amylase may contribute to increased physical stresses. There is a close association between salivary alpha amylase and plasma norepinephrine under stressful physical conditions. The aim of this study was to evaluate the relationship between pain severity and salivary alpha amylase levels in patients with symptomatic irreversible pulpitis. Materials and Methods: Thirty-six patients (20 females and 16 males) with severe tooth pain due to symptomatic irreversible pulpitis were selected. The visual analogue scale (VAS) score was used to assess the pain severity in each patient. Unstimulated whole saliva was collected, and the level of alpha amylase activity was assessed by the spectrophotometric method. Statistical analysis was performed using SPSS 13. Results: The level of alpha amylase was significantly increased in the saliva in association with pain severity assessed by VAS. The salivary alpha amylase was also elevated with increased age and in males. Conclusions: There was a significant correlation between the VAS pain scale and salivary alpha amylase level, which indicates this biomarker may be a good index for the objective assessment of pain intensity.

• Korean Journal of Pharmacognosy
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• v.35 no.4 s.139
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• pp.271-275
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• 2004

Distylium racemosum Sieb. Et Zucc contains some compounds inhibit -amylase activity in experimental conditions. The inhibitory test showed that 50% acetone extracts from the bark and leaves of the plant strongly inhibited salivary -amylase activity. Proanthocyanidin(PA) which has strong inhibitory activity was extracted from the leaves by chromatography on Sephadex LH-20. The inhibitory activities and the inhibition kinetics of the PA were studied against three kinds of enzymes: human salivary ${\alpha}-Amylase$ (SAA), pork pancreatin ${\alpha}-Amylase$ (PAA) and yeast ${\alpha}-Glucosidase$ (AG). Then the activities of PA against SAA, PAA and AG were compared with those of acarbose, a commercial agent. The inhibitory activities of PA were stronger than those of acarbose. Inhibition kinetics of the PA showed competitive inhibition for SAA and PAA, and non competitive inhibition for GA.