• Microbiology and Biotechnology Letters
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• v.6 no.1
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• pp.9-16
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• 1978

Effects of the addition of Ginseng extract and it's incubation time on enzyme activity (${\alpha}$-amylase, ${\beta}$-amylase, protease) of Aspergillus app. was investigated. 1. ${\alpha}$-Amylase activity of Asp. oryzae was higher for 48 hours than control, however, the same after 48 hours. ${\beta}$-Amylase activity was stimulated at the concentration of 0.1 to 1.0％, and decreased at the concentration of 3.0 to 5.0％. The acid protease activity was higher than control for 72 hours and in the medium of 120 hours was decreased significantly. The alkaline protease activity was lower than control. However, alkaline protease activity was higher than acid protease activity. 2. ${\alpha}$-Amylase of Asp. niger was increased in proportion to increasing of the extract concentration. ${\beta}$-Amylase was increased at the concentration from 0.5 to 3.0％ and it's activity was depressed in proportion to increasing of the extract concentration for 48 hours and on the contrary it was improved in proportion to increasing of the extract concentration for 72 hours except for 5.0％ concentration with marked decreasing. Alkaline protease activity was increased at lower concentration (0.1∼0.5％) for 24 to 48 hours and it was depressed at higher concentration (1.0 to 5.0), however after 48 hours incubated, it's activity was decreased in preparation to increasing of the extract concentration.

• Korean Journal of Pharmacognosy
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• v.47 no.1
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• pp.24-28
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• 2016

This study was to evaluate the effect of ginseng (Panax ginseng) seed oil on the ${\alpha}$-glucosidase and ${\alpha}$-amylase. Each ginseng seed oils (HE, SE, EE) exhibited a significant inhibitory effect (p<0.001) at all concentrations (10 and 20 mg/ml) on ${\alpha}$-glucosidase activity. HE is the highest inhibitory activity (86.92%) at a concentration of 20 mg/ml, SE and EE showed an inhibitory effect of 77.13% and 65.83%, respectively. And also, Each ginseng seed oils (HE, SE, EE) exhibited a significant inhibitory effect (p<0.001) at all concentrations (1 and 2 mg/ml) on ${\alpha}$-amylase activity. HE is the highest inhibitory activity (89.68%) at a concentration of 2 mg/ml, SE and EE showed an inhibitory effect of 76.99% and 65.70%, respectively.

• Korean Journal of Food Science and Technology
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• v.31 no.6
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• pp.1421-1426
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• 1999

Sixteen domestic barley varieties and subsequently produced malts were evaluated for quality characteristics. Diastatic power(DP), complementary actions of amylases in malt, had a wide $variation(139{\sim}220^{\circ}L)$ among the barley varieties. Some 6-row barley varieties demonstrated significantly high DP values. ${\beta}-\;and\;{\alpha}-amylase$ activities in malts were also significantly influenced by barley varieties. Diastatic power was highly correlated with ${\beta}-amylase$ activity, indicating that the ${\beta}-amylase$ activity was a predominant factor determining saccharifying action in malt. Amylograph was used to indirectly estimate starch-degrading enzymatic activity, and the reduction in amylograph viscosity was associated with ${\alpha}-amylase$ activity. Barley quality factors in relation to enzymatic activity of malt were analyzed, and the barley variety with lower kernel weight and less plumper kernels tended to produce higher starch-degrading enzyme activity. Potential diastatic power, an estimate of bound ${\beta}-amylase$ in raw barley, was associated with diastatic power in the final malt. Potential diastatic power turned out to be an important factor for predicting good malting barley.

• Biotechnology and Bioprocess Engineering:BBE
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• v.5 no.1
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• pp.7-12
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• 2000

The expression of the mouse $\alpha-amylase$ gene in the methylotrophic yeast, P pastoris was investigated. The mouse $\alpha-amylase$ gene was inserted into the multi-cloning site of a Pichi a expression vector, pPIC9, yielding a new expression vector pME624. The plasmid pME624 was digested with SalI or BglII, and was introduced into P. pastoris strain GSl15 by the PEG1000 method. Fifty-three transformants were obtained by the transplacement of pME624 digested with SaiII or BglII into the HIS4locus $(38\;of\;Mut^+\;clone)$ or into the AOX1 locus $(15\;of\;Mut^s\;clone)$. Southern blot was carried out in 11 transformants, which showed that the mouse $\alpha-amylase$ gene was integrated into the Pichia chromosome. When the second screening was performed in shaker culture, transformant G2 showed the highest $\alpha-amylase$ activity, 290 units/ml after 3-day culture, among 53 transformants. When this expression level of the mouse $\alpha-amylase$ gene is compared with that in recombinant Saccharomyces cerevisiae harboring a plasmid encoding the same mouse $\alpha-amylase$ gene, the specific enzyme activity is eight fold higher than that of the recombinant S. cerevisiae.

• Advances in Traditional Medicine
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• v.4 no.4
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• pp.227-234
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• 2004

An ${\alpha}-Amylase$ was purified to apparent homogeneity from germinating soybean seeds (Glycine max). Enzyme showed high specificity for starch. ${\alpha}-Amylase$ from soybean has optimum pH at 7.6 in the pH range 4.0-10.6. At this pH, the $K_m$ of starch was 2.63 mg/ml and the $V_{max}$ was equal to 52.6 mg/ml/min protein. Optimum temperature of the enzyme was found to be $55^{\circ}C,\;Q_{10}$ equal to 1.85 and energy of activation equal to 12 kcal/mol. Additives like, EDTA reduced the activity of ${\alpha}-amylase$ whereas PMSF enhanced the activity. ${\alpha}-Amylase$ was inhibited by several heavy metal ions.

• Journal of the Korean Society of Food Science and Nutrition
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• v.40 no.2
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• pp.308-315
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• 2011

We investigated ${\alpha}$-amylase, ${\alpha}$-glucosidase and lipase inhibitory activity of extracts collected from wild plants in Gangwon-do. 90 wild plants were collected and their water and ethanol extracts were obtained. Results of measuring ${\alpha}$-amylase inhibitory activity indicated more than 80% of activity inhibition in 10 mg/mL concentration for ethanol extracts of three plants and water extracts of two plants. For ${\alpha}$-glucosidase inhibitory activity, ethanol extracts of thirteen plants and water extracts of three plants showed more than 80% of activity inhibition in 10 mg/mL concentration. In the experiment of inhibiting lipase activity, ethanol extracts of seven plants and water extracts of one plants showed above 80% of activity inhibition in 10 mg/mL concentration. These results suggest that the selected extracts could be potentially used as a resource of bioactive materials for health functional foods.

• Journal of Applied Biological Chemistry
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• v.50 no.2
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• pp.70-73
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• 2007

Antioxidant and anti-diabetic activities of acorn were evaluated by its potential for scavenging stable DPPH free radical, inhibition of lipid peroxidation, reducing power, and inhibiton of ${\alpha}-glucosidase\;and\;{\alpha}-amylase$. The water extract of acorn exhibited strong antioxidant and antidiabetic related activities in the tested model systems. Solvent fractionation of the water extract revealed that the water fraction and the EtOAc fraction had strong antioxidant activity, and inhibitory activity on ${\alpha}-glucosidase\;and\;{\alpha}-amylase$. The water fraction exhibited higher DPPH radical scavenging activity ($EC_{50}=7.19{\mu}g/mL$) than that of ${\alpha}-tocopherol\;(EC_{50}=7.59{\mu}g/mL)$. It is considered that water extract of acorn has the potential for natural antioxidant and anti-diabetic products.

• The Korean Journal of Food And Nutrition
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• v.3 no.1
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• pp.29-34
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• 1990

This study carried out to changes $\alpha$-amylase activity and isozymes in barley during germination in the dark and red light The specific activity of u-amylase was increased during the germination periods in the dark, giving 355.0 and 523.7 units/mg protein at 3 and 5 day, and the activity was increased by the red light up to 48 and 15% at 3 and 5 days of germination, respectively. The ratio of $\alpha$-amylase I and II was approximately 95:5 at both 3 and 5 days of germination in the dark while the different ratio was found by the red light i. e. 60 : 40 and 90 : 10 at 3 and 5 days of germination, respectively.

• Korean Journal of Food Science and Technology
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• v.27 no.5
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• pp.762-767
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• 1995

The ${\alpha}-Amylase$ inhibitor from black bean(Phaseolus vulgaris) was purified to homogeneity using 70% saturated ammonium sulfate, DEAF-cellulose, Concanavalin-A sepharose chromatography and gel filtration with Superose 6. The purified α-amylase inhibitor showed a single band of 25 KD in molecular weight on the SDS-PAGE. The specific activity of the inhibitor was 544.0 units/mg and the purity was enhanced about 18-fold. The amino acids of ${\alpha}-Amylase$ inhibitor from black bean was mainly glutamic acid, aspartic acid and lysine. The inhibitor was glycoproteins and its carbohydrate contents was 3.2%.

• Journal of Nutrition and Health
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• v.9 no.1
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• pp.104-109
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• 1976

Condiments such as welsh onion, garlic, ginger, black pepper, red pepper, japanese pepper, mustard, horse radish, monosodium glutamate and sugar were ground by a homogenizer, and 0%, 1%, 5%, and 10% of each of the ground condiments were put into 0.2% ${\alpha}-amylase$ solution for storage at the temperature of $15^{\circ}C$. ${\alpha}-amylase$ activity then was measured by the Wohlgemuth method at 48-hour interval, and the following results were obtained. 1) Among the condiments, black pepper and sugar checked the ${\alpha}-amylase$ activity most, about 80% in comparison with control. 2) Welsh onion, garlic, mustard, and ginger checked the ${\alpha}-amylase$ activity, about 50% in comparison with control, irrespective of the time stored. 3) The low concentration of red pepper, horse radish, japanese pepper and mono-sodium glutamate checked the ${\alpha}-amylase$ activity about 50%, while the high one did below 75% in comparison with control. To conclude: all the condiments used in the experiment checked ${\alpha}-amylase$ activity.