• 한국식품영양학회지
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• 제9권3호
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• pp.247-252
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• 1996

$\beta$-Amylase was purified from sweet potato by acetone fractlonatlon, Sephadex A-50 ion exchange chromatography and Sepgadex G-200 gel chromatographyl The higher enzyme concentration was, the higher heat stability of enzyme became. After 1 hour 30 minute. At 6$0^{\circ}C$ in pH 5, enzyme under concentration of 30$\mu$l/ml lost its activity completely and over the concentration of 100$\mu$g/ml remained 25% of activity. The enzyme was stabilized at range of pH 4~10 and pH stability was increased by glycerol. Five moles of NaCl inhibited completely of the enzyme activity. SDS of 0.05% inhibited the enzyme completely after 12 hours at 37$^{\circ}C$ in pH5. One mole guanidine-HCl and 8M urea inhibited the entire enzyme after 13 hours at 37$^{\circ}C$ in pH 5.

• Archives of Pharmacal Research
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• 제13권1호
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• pp.33-37
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• 1990

The effects of pH values, temperature and some elements on the amylolytic activity and stability of the purified S. aureofacienc 77 amylase were studied in this investigation. The purified enzyme showed its maximum activity at pH 6 within 8 min incubation at $40^{\circ}C$. None of the tested 6 metals showed on stimulatory effect on the enzymatic activity, $Fe^{+++}$, $Cu^{++}$ and $Hg^{++}$ at high dose inhibited the enzyme activity to great extent as compared with $Zn^{++}$, $Mn^{++}$ and $Fe^{++}$ whih gave less effect in this respect. The enzyme liquor was found to be thermolabile, since it lost completely its activity after 4 days incubation under room temperature and showed maximum activity during this period as a result of additions of $Ca^{++}$and NaCl, Gradual reduction was however recorded until activity reached 30% after 60 days of incubation.

• 한국식품영양과학회지
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• 제38권6호
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• pp.812-815
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• 2009

소화 촉진 작용이 있다고 알려진 무의 건조방법, 온도, pH 등의 가공조건이 ${\alpha}$-amylase 활성에 미치는 영향을 검토하였다. 동결건조 한 무 뿌리와 무 줄기의 ${\alpha}$-amylase의 활성을 비교한 결과 무 뿌리가 무 줄기의 3.1배 높은 수준의 활성을 보였다. 무를 pH와 온도를 달리하여 안정성을 측정한 결과, pH 범위가 $4{\sim}7$이며 온도가 $25{\sim}40^{\circ}C$일 때 ${\alpha}$-amylase 활성이 높았다. 무의 ${\alpha}$-amylase는 산성이나 중성 조건에서 처리하고 $60^{\circ}C$ 이하의 온도로 가열처리하여야 활성을 유지하였다. 무를 깍두기와 단무지의 형태로 가공하였을 때 무의 ${\alpha}$-amylase 잔류활성은 각각 15.39%와 19.193%이었고 초절임무에서는 ${\alpha}$-amylase의 활성이 대부분 소실됨을 보였다. 결과적으로, 무의 소화효소인 ${\alpha}$-amylase 활성은 열과 pH등의 가공조건에 의해 크게 영향을 받는 것을 알 수 있었으며 $60^{\circ}C$ 이하의 온도에서 열처리하는 것과 중성이나 약산성에서 ${\alpha}$-amylase 효소의 활성도가 유지되는 것으로 판단된다.

• 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 $45^{\circ}C$.

• 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.

• 한국식품영양과학회지
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• 제19권6호
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• pp.591-595
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• 1990

인삼saponin이 Saccharomyces rouxii의 생육속도나 고온충격으로부터의 정상회복속도를 크게 증가시킨다는 사실을 확인한 바 있다. 이러한 촉진효과의 원인을 추정하기위해 인삼saponin이 S. rouxii가 생산한 amylase의 활성에 미치는 영향이나 그 효소의 열변성에 미치는 보호효과를 조사해 본 결과는 다음과 같다. S. rouxii가 생산한 amylase의 환성은 pH 6.5에서 5$0^{\circ}C$로 반응시킴으로써 가장 크게 나타났다. 인삼saponin을 0.01% 첨가한 경우 amylase의 활성이 무첨가구에 비해 23% 정도 촉진되었으며, 인삼saponin 0.01%를 첨가한 경우 7$0^{\circ}C$로 가열처리시켜도 amylase의 활성이 무첨가 처리구에 비해 그 잔존활성 기준으로 28%나 열변성으로 부터 보호될 수 있었다. 이 결과로 미루어 보아 heat stress 받은 효모의 정상회복은 인삼saponin이 효소의 환성이나 효소의 열안정성에 기여하기 때문인 것으로 판단되었다.

• 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.

• 한국식품영양학회지
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• 제9권3호
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• pp.253-258
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• 1996

Stabilities of sweets potato f-amylase on various reagents were studied. The enzyme was stabilized by bovine serum albumin, Triton X-100 and 2-mercaptoethanol of 0.04%. Among them, bovine serum albumin was the most effective. And enzyme stability was increased by using the deairated solution. The enzyme activity was remained 0% in the absence of glycerol, 25% in the presence of 20% glycerol and 50% in the presence of 40% glycerol at 37$^{\circ}C$, for 15 hours in pH 11. SDS inhibited the enzyme, and 2-mercaptoethanol and dithiothreitol stabilized it.

• Applied Biological Chemistry
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• 제21권2호
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• pp.103-108
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• 1978

Paecilomyces subglobosum이 생산하는 내산성 ${\alpha}-amylase$를 Sephadex G-150으로 정제한 결과 순수정제가 되지 않았으나 glucoamylase와 분리되었다. 조효소를 사용하여 내산성 amylase의 일반 성질을 조사한 결과 최적 pH는 4.0이었고 최적온도는 $38^{\circ}C$이었다. 이 효소는 보통 ${\alpha}-amylase$와 비교하여 pH에 대한 안정성은 매우 좋았으나 열 안정성은 비슷하였다. 전분에 대한 가수분해력이 좋았으며 생성물을 박충 크로마토그라피로 조사한 결과 말토스도 분해하는 것을 알았다.

• 약학회지
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• 제6권2호
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• pp.18-22
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• 1962

Purified preparation of .betha.-amylase is obtained from radish root by the means of fractional precipitation with ammonium sulfate. Purified preparation saccharifies the starch, .betha.-maltose being formed. Dextrinization in the true sense does not take place. Hydrolysis ceases when approximately 50% of the theoretical yield of maltose is obtained and there remains a substance (to be .betha.-limit dextrin) which gives a blue-violet with iodine, no glucose being formed. Stability of preparation is optimal at pH 4-9 and more completely inactivated at 65.deg. in fifteen minutes. .betha.-Amylase of radish exhibits optimal activity at and near pH 5.0, which varied depending upon the buffer. Calcium and chloride ions do not effect the activities of enzyme. The results of experiments with oxidizing, alkylating and mercaptide-forming reagents which have been reported to be specific for sulfhydryl groups confirm that free sulfhydryl groups are essential to the activity of .betha.-amylase from radish.