• Korean Journal of Food Science and Technology
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• v.33 no.2
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• pp.226-230
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• 2001

High hydrostatic pressure was applied to Foxtail Millet Takju to investigate the effects of high pressure on inactivation of microorganisms and enzymes. Total bacteria, lactic acid bacteria and yeast in untreated Takju were $6.8{\times}10^7,\;1.3{\times}10^8\;and\;8.4{\times}10^7\;CFU/mL$, respectively. Total bacterial count in Takju reduced to $2.2{\times}10^5\;CFU/mL$, while lactic acid bacteria and yeast were sterilized completely when heated at $65^{\circ}C$ for 30 min. Lactic acid bacteria and yeast decreased with the increase of treatment pressure, and pressurization of 400 MPa for 10 min at room temperature sterilized completely the lactic acid bacteria and yeast in Takju. Total bacteria were not sterilized with pressurization of even 600 MPa at room temperature. Total bacteria were completely sterilized at $66^{\circ}C/400\;MPa/60\;min\;and\;66^{\circ}C/600\;MPa/10\;min$. Pressurization of Takju caused a partial inactivation of ${\alpha}-amylase$, and after pressurization at 600 MPa for 10 min at room temperature, 73.2% of the original activity remained. The activity of glucoamylase increased with the increase of treatment pressure. Treatment at $66^{\circ}C/400\;MPa/10\;min$ reduced the activity of ${\alpha}-amylase$ by 59.7% and glucoamylase by 20.5%. ${\alpha}-Amylase$ was inactivated to less than 1.2% of the original activity at $66^{\circ}C/600\;MPa/30\;min$.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.44 no.6
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• pp.791-795
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• 2011

This study examined the inhibitory activity of Ecklonia cava (EC) against ${\alpha}$-amylase to evaluate the availability of EC extract as a functional food agent. To verify the inhibitory activity of EC against porcine pancreatic ${\alpha}$-amylase, potato starch was used as a substrate. This analysis revealed that EC ethanol extract exhibited high ${\alpha}$-amylase inhibitory activity. For potential application within the food industry, the stability of the activity of EC ethanol extract under various heat and pH conditions was examined. The ${\alpha}$-amylase inhibitory activity of EC ethanol extract was not affected by the heat and pH treatment conditions used in this study. These results suggest that EC has the potential for development as a functional food agent.

• Food Science and Biotechnology
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• v.16 no.4
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• pp.655-658
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• 2007

Bacillus polyfermenticus SCD was transformed by the recombinant shuttle vector for Bacillus and Escherichia coli containing 3 antibiotic resistant genes and an ${\alpha}$-amylase gene from Bifidobacterium adolescentis Int57. The ${\alpha}$-amylase gene fused to a secretion sequences was expressed under the control of the promoter of amylase gene from B. subtilis var. natto. The recombinant plasmid was maintained stably in the transformants producing the ${\alpha}$-amylase. The enzyme was secreted to outside of the cell and showed the similar enzyme activity as that of Bacillus subtilis BD170 under the same conditions of pH and growth temperature. Because of the relatively easy transformation and the secretion of the enzyme, the transformants of B. polyfermenticus SCD may give a new strategy in the production of foreign genes.

• Journal of the Korean Applied Science and Technology
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• v.26 no.1
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• pp.10-17
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• 2009

This study investigated the effect of kilning condfition on the diastatic power and activities of protease, $\alpha$-amylase, and $\beta$-amylase in rice malt. Common rice (Oryza sativa) was steeped at $30^{\circ}C$ for 50 h, germinated at $30^{\circ}C$ for 7 days, and kilned at $50^{\circ}C$ for 24 h. The moisture content and enzymatic activities were determined under various kilning times. As a result, the moisture content was reduced from 42.1 % to 3.9% after 24 h of kilning at $50^{\circ}C$. The protease activity of rice malt showed lower value than that of barley malt. All enzymatic activities were decreased during the kilning stage. Results indicated that after prolonged kilning at $50^{\circ}C$, the inactivation of hydrolytic enzymes might be occurred. Even though the amylolytic activity of malted rice showed low value, the rice malt shows the potential characteristics as ingredient for the brewing and cereal industries.

• Proceedings of the Korean Society of Crop Science Conference
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• 2000.04a
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• pp.252-253
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• 2000

• Proceedings of the Korean Society of Crop Science Conference
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• 1999.05a
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• pp.51-52
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• 1999

• Food Science and Preservation
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• v.18 no.6
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• pp.923-929
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• 2011

For the purpose of investigating the in vitro antidiabetic activity of a medicinal herb mixture prepared through traditional antidiabetic prescription, the study analyzed the existence of insulin-similar components and examined ${\alpha}$-amylase and ${\alpha}$-glucosidase inhibition activity. As a result of arranging the medicinal herb mixture extracts over the 3T3-L1 fibroblast in the concentration of $10{\mu}g/mL$, which confirmed that it included much of insulin sensitizer components as 151.7% in the differentiation of 3T3-L1 fibroblast. The inhibition activity against ${\alpha}$-amylase of the medicinal herb mixture extracts as hypoglycemic agent were 38.4, 31.5 and 16.6% in the concentration of 10.0, 1.0 and 0.1 mg/mL, respectively. The inhibition activity against ${\alpha}$-glucosidase of the medicinal herb mixture extracts were 81.3, 35.8 and 26.7% in the concentration of 10.0, 1.0 and 0.1 mg/mL, respectively. The inhibition activity against ${\alpha}$-glucosidase in the ethyl acetate fractions of the water and 80% ethanol extracts were 66.9% and 55.1%, respectively, the highest levels in the various solvent extracts.

• Korean Journal of Microbiology
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• v.6 no.4
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• pp.141-146
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• 1968

Takjoo mashes which were collected from the Takjoo breweries in Seoul area were studied on the purpose of detection for the reciprocal actions between amylase activity and saccharifying ability. The results obtained are as follows. Amylase activity was found to be usually high in the primary brewing process as well as the main brewing process. And especially, .alpha.-amylase in the primary brewing process showed remarkably high activity, more than 5.0 D.P. per/ml of mash comparing with 3.8 D.P. per ml of mash in the main brewing process. However, it was revealed that the reducing sugar contents in the primary brewing process were much higher in its average contents, 5.5%, than 1.1% in the main brewing process.

• Mycobiology
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• v.51 no.1
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• pp.60-66
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• 2023

In this study, the α-amylase inhibitory activity, α-glucosidase inhibitory activity, pancreatic lipase inhibitory activity, and Xanthine Oxidase inhibitory activity of the fruiting body extracts of 5 varieties of Agaricus bisporus (AB) were confirmed. First, the α-amylase inhibitory activity of AB12, AB13, AB18, AB34, and AB40 methanol extracts was lower than that of acarbose, a positive control, in all concentration ranges. The α-glucosidase inhibitory activity of the AB40, AB13, and AB12 methanol extracts at the extract concentration of 1.0 mg/mL was 80.5%, 81.3%, and 78.5%, respectively, similar to that of acarbose, a positive control. The pancreatic lipase inhibitory activity of the methanol extract of Agaricus bisporus fruiting body was significantly lower than that of the positive control orlistat in the concentration range of 50~1.000 (mg/mL). The Xanthine Oxidase inhibitory activity was 0.5~8.0 mg/mL of each extract, which was significantly lower than that of the positive control allopurinol in the same concentration range. However, the Xanthine Oxidase inhibitory activity of AB13 and AB40 at 8.0 mg/mL was about 70%, which was higher than that of other mushrooms. In conclusion, five kinds of Agaricus bisporus fruiting bodies seem to have inhibitory effects on enzymes such as α-amylase, α-glucosidase, pancreatic lipase, and Xanthine Oxidase that degrade starch and protein. In particular, it has an inhibitory effect and a reduction effect on xanthine oxidase that causes gout, so it is expected that it can be developed and used as a food or health supplement with health functional properties through future research.

• Korean Journal of Microbiology
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• v.36 no.2
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• pp.112-118
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• 2000

A new gene encoding an acidophilic TEX>$\alpha$-amylase of Bacillus cil-culans KCTC3004 was cloned into Eschericlzia coli using pUC19 as a vector. The gene localized in the 5.8 kb PstI DNA fragment was expressed independently of its orientation in the cloning vector showing enzyme activity about 40 times greater than that produced by the original B, circulans The optimum pH and temperature of the cloned enzyme were pH 3.6 and 45^{\circ}C.$ respectively. The enzyme hydrolyzed starch to produce maltotriose and maltooligosaccharides. The SDS-PAGE and zymopram of the enzyme produced in E coli(p.4L850) indicated a molecular weight of 55,000.