• 생약학회지
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• 제35권4호통권139호
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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.

• 한국미생물·생명공학회지
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• 제13권1호
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• pp.7-11
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• 1985

인삼(人蔘) saponin의 생물학적(生物學的) 활성(活性)을 조사(調査)하기 위하여 세균(細菌) v{\alpha}$-amylase의 작용(作用)에 미치는 인삼(人蔘) saponin의 영향(影響)을 조사(調査)한 결과(結果)를 요약(要約)하면 다음과 같다. Protopanaxadiol계(系), triol계(系) 및 total saponin 모두 ${\alpha}$-amylase의 활성(活性)을 25, 12, 13%정도(程度) 촉진(促進)시켰다. Diol계(系) saponin첨가(添加)경우 $40^{\circ}C$에서 3분간(分間) 전처리(前處理)함으로서 ${\alpha}$-amylase의 활성(活性)을 20%정도(程度) 촉진(促進)시켰으며 酵素(효소)의 열변성(熱變性)에 대(對)한 보호작용(保護作用)은 protopanaxariol계(系) saponin은 $60^{\circ}C$에서 5분(分)까지는 보호작용(保護作用)이 있었으나 protopanaxadiol계(系) saponin은 오히려 열실활(熱失活)을 촉진(促進)하는 경향이었다. Diol 및 triol계(系) saponin의 산가수분해물(酸加水分解物)이 ${\alpha}$-amylase의 활성(活性)을 diol 및 triol계(系) saponin보다 더 촉진(促進)시켰으며 diol, triol계(系) saponin의 첨가(添加)는 고농도(高濃度)의 기질(基質)이 존재(存在)할 때 기질저해(基質沮害)를 막아주었다.

• Asian-Australasian Journal of Animal Sciences
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• 제19권12호
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• pp.1749-1754
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• 2006

Two slaughter experiments were conducted to determine the effects of rumen escape starch, by altering dietary starch concentration and corn particle size, on ${\alpha}$-amylase activity in the pancreas and the small intestinal digesta of lambs. In experiment 1, 18 wether lambs (28.5${\pm}$1.6 kg) were fed low, medium or high starch diets for 35 d and slaughtered. Dietary starch concentrations linearly increased rumen escape starch (p<0.05). Pancreatic ${\alpha}$-amylase activity was lower (p<0.05) in lambs fed the low starch diet. When expressed per gram of digesta, ${\alpha}$-amylase activity was lower in lambs fed the low starch diet. However, expressed as total activity, ${\alpha}$-amylase in the digesta was greater in lambs fed the medium starch diet. In experiment 2, 12 wether lambs (23.5${\pm}$0.3 kg) were fed diets with finely cracked corn, coarsely cracked corn and whole corn. These dietary treatments continued for 35 d before tissue collection. Rumen escape starch increased with increasing corn particle size (p<0.05). ${\alpha}$-amylase activity in the pancreas and the small intestinal digesta was significantly greater (p<0.05) in lambs fed the coarsely cracked corn. These data suggest that increasing rumen escape starch results in a quadratic increase in total ${\alpha}$-amylase activity in the pancreas and the small intestinal digesta. Maximum ${\alpha}$-amylase activity is reached when rumen escape starch is about 100-120 g/d in 25-30 kg lambs.

• Journal of Microbiology and Biotechnology
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• 제7권5호
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• pp.293-298
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• 1997

A 4.6-kb HindIII fragment encompassing the complete 140-kDa ${\alpha}$-amylase gene of Lactobacillus amylovorus B 4540 was cloned into pBR322 by the shot gun method. Southern blotting and restriction mapping for the insert were performed. The recombinant 9.0-kb plasmid, pFML1, conferred ${\alpha}$-amylase activity to E. coli and Lactococcus lactis hosts when introduced by electroporation. SDS-PAGE and zymography confirmed the production of 140-kDa ${\alpha}$-amylase and its proteolytic degradation products with enzyme activity in transformants. Total ${\alpha}$-amylase activity of E. coli $DH5{\alpha}$ cells harboring pFML1 was 1.8 units and most activity was detected from cell pellets. Total enzyme activity of L. lactis subsp. lactis MG1363 transformant was five to ten-fold lower than that of E. coli cell but more than half of the activity was detected in the culture supernatant.

• 한국양식학회지
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• 제18권4호
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• pp.245-251
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• 2005

본 연구는 rotifer, B. rotundiformis를 대상으로 소화효소 실험을 하기 위해 이들이 가지고 있는 소화효소의 최고 활성 조건을 확인하기 위해 수행하였다. rotifer, B. rotundiformis의 $\alpha$-amylase, total alkaline Protease, trypsin 및 TG-lipase는 Tris-HCl buffer 보다 phosphate-NaOH buffer 안정적인 효소활성을 보였다. $\alpha$-amylase, trypsin 및 TG-lipase는 pH 8.0에서, total alkaline proteaset pH 7.0에서 높은 효소 활성을 나타내었다. $\alpha$-amylase 활성은 $40^{\circ}C$에서 가장 높은 활성을 보였으며, total alkaline pretense와 trypsin은 $55{\~}60^{\circ}C$의 온도에서 높은 활성을 나타내었다. 반면 TG-lipase 활성은 $25{\~}30^{\circ}C$의 낮은 온도에서 활성이 높았다. $\alpha$-amylase, total alkaline pretense, trypsin 및 TG-lipase의 활성의 적정 기질 농도는 $3.5\%$ starch, $\0.6%$ azo-casein, $87.5{\mu}M$ BApNA and 81.2 mM olive oil이었다. $\alpha$-amylase, total alkaline protease, trypsin 및 TG-lipase의 활성의 적정 반응시간은 40, 60, 30 and 25 min으로 나타났다. 본 연구 결과에서 얻어진 자료는 rotifer, B. rotundiformis의 소화효소 연구를 위한 기초 자료로 이용될 것이다.

• Nutrition Research and Practice
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• 제8권5호
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• pp.602-606
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• 2014

BACKGROUND/OBJECTIVES: We investigated total 26 ingredients of Saengshik which will be commercially produced as an anti-diabetic dietary supplement. SUBJECTS/METHODS: Thirteen vegetables, nine cereals, three legumes and one seed were extracted with aqueous ethanol for 2 h at $60^{\circ}C$, and evaluated for their inhibitory effects against ${\alpha}$-amylase and ${\alpha}$-glucosidase and for total phenolic and flavonoid contents. RESULTS: All ingredients inhibited ${\alpha}$-amylase activity except cabbage. Strong inhibitory activity of ${\alpha}$-amylase was observed in leek, black rice, angelica and barley compared with acarbose as a positive control. Stronger inhibition of ${\alpha}$-glucosidase activity was found in small water dropwort, radish leaves, sorghum and cabbage than acarbose. All Saengshik ingredients suppressed ${\alpha}$-glucosidase activity in the range of 0.3-60.5%. Most ingredients contained total phenols which were in the range of 1.2-229.4 mg gallic acid equivalent/g dried extract. But, total phenolic contents were not observed in carrot, pumpkin and radish. All ingredients contained flavonoid in the range of 11.6-380.7 mg catechin equivalent/g dried extract. CONCLUSIONS: Our results demonstrate that Saengshik containing these ingredients would be an effective dietary supplement for diabetes.

• Journal of Pharmaceutical Investigation
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• 제21권3호
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• pp.143-147
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• 1991

${\alpha}-amylase$ was immobilized on the surface of polyethylene glycol(M.W. 2000) grafted polyurethane film using diisocyanate in an attemp to develop enzyme immobilized polymeric materials. The surface morphology of the modified polyurethane film was examined by SEM. Effects of pH and temperature on the activity of the immobilized ${\alpha}-amylase$ were investigated. The optimal pH range of the activity was $7.0{\sim}7.5.$ The immobilized ${\alpha}-amylase$ demonstrated high thermal stability and maintained consistent activity during long-term storage.

• Journal of Plant Biology
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• 제34권2호
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• pp.159-163
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• 1991

합성 식물생장조절제인 dimethipin의 작용기작을 밝히고자 보리 무배부 종자 시스템에서 gibberellic acid(GA3)에 의해 유도되는 ${\alpha}-amylase$ 활성에 미치는 dimethipin의 영향을 조사하였다. Dimethipin은 mRNA와 단백질 함량 및 GA3에 의해 유도되는 ${\alpha}-amylase$ 활성을 뚜렷하게 억제하였다. 그러나 억제효과는 GA3 처리 후 dimethipin 첨가시간 간격이 커질수록 점점 감소하였다. Dimethipin을 GA3 처리후 18시간 이내에 첨가하였을 때 mRNA 함량증가를 억제하였다: 그러나 GA3 처리 18시간 경과 후에 첨가하였을 경우에도 수용성 단백질 함량 및 ${\alpha}-amylase$ 활성 증가를 억제하였다. 이러한 결과로 미루어보아 dimethipin은 mRNA 합성과 ${\alpha}-amylase$ 단백질 합성을 공히 억제하는 것으로 사료된다.

• Journal of Microbiology and Biotechnology
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• 제2권3호
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• pp.166-173
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• 1992

The expression of Bacillus subtilis $\alpha$-amylase from the phoA-amyE fusion gene in recombinant E. coli was investigated under various environmental conditions. The overexpression of cloned $\alpha$-amylase caused retardations in cell growth and synthesis of alkaline phosphatase (AP) from the chromosomal phoA gene. The change of culture temperature from $37^\circ{C}$ to $30^\circ{C}$ increased the specific activities of both $\alpha$-amylase and $\beta$-lactamase by six and two times, respectively, whereas the AP activity remained unchanged. The experiments with chlorampenicol (a translation inhibitor) suggested the enhancement of $\alpha$-amylase activity at $30^\circ{C}$, and this was partly due to the stability of $\alpha$-amylase itself. The further decrease of the temperature to $25^\circ{C}$ slowed down both the cell growth and cloned-gene expression rate. The $\alpha$-amylase activity showed a maximum at pH of 7.4 while alkaline phosphatase was most effectively produced at pH of 8.3.

• Journal of Microbiology and Biotechnology
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• 제14권6호
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• pp.1196-1199
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• 2004

A bacterium, isolated from rabbit's waste and identified as Cellulomonas sp., had cellulase and thermostable $\alpha$-amylase activity when grown on wheat bran. Maximum activity of thermostable $\alpha$-amylase was obtained by adding $3\%$ soluble starch. However, soybean oil (1 ml $1^{-1}$) could increase the production of $\alpha$-amylase and cellulase in 'wheat bran. The $\alpha$-amylase was characterized by making a . demonstration of optimum activity at $90^{\circ}C$ and pH 6- 9, with soluble starch as a substrate. The effect of ions on the activity and the stability of this enzyme were investigated. This strain secreted carboxymethyl cellulase (CMCase), cellobiase ($\beta$­glucosidase), and filter paperase (Fpase) during growth on wheat bran. Carboxymethy1cellulase, cellobiase, and Fpase activities had pH optima of 6, 5.5, and 6, respectively. CMCase and cellobiase activities both had an optimum temperature of $50^{\circ}C$, whereas Fpase had an optimum temperature of $45^{\circ}C$.