• 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.

• 한국잠사곤충학회지
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• 제16권1호
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• pp.57-65
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• 1974

5령기에 있어서 사료중 단백질 함량이 유충의 증체량, 사료방률에 미치는 영향과 간접적으로 유충의 소화액 Amylase 활성에 미치는 영향을 알기 위하여 상엽분말을 넣은 인공사료를 사용해서 단백질 급원으로 Soybean meal함량에 따라 6종의 사료를 만들어 누에를 사육한 결과 다음과 같은 결과를 얻었다. 1. 사료중 단백질 함량의 증가에 비례하여 유충의 증체량도 비례하여 많았다. 2. 사료중 단백질 함량의 증가에 비례하여 전견중 및 견층중도 비례하여 무겁다. 3. 사료중 단백질 함량의 증가에 비례하여 유충의 소화양 및 소화율도 비례하여 높았다. 4. 사료중 단백질 함량의 증가에 비례하여 유충의 사료방률도 비례하여 높았다. 5. 그러나 사료중 단백질 함량의 증가와 유충의 소화액 Amylase 활성 간에는 일정한 상관관계가 없었다.

• 한국작물학회지
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• 제41권5호
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• pp.542-550
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• 1996

알팔파 (Medicago sativa L.)의 예취후 재생 기간중 저장탄수화물의 이용성을 규명하기 위해 수경재배하여 개화초기에 예취한 후 재생 24일간의 뿌리내 비구조탄수화물의 함량 및 전분 분해효소의 활력을 분석한 결과는 아래와 같다. 1. 재생초기 10일간의 잎과 줄기의 재생은 매우 느리게 진행되었으며, 예취후 뿌리의 성장이 억제되었다. 2. 예취후 초기재생 10∼14일간 뿌리내 가용성 당 및 전분의 함량은 다같이 감소하였다가 이후 빠르게 회복하는 경향이었다. 3. 재생기간중 exo-amylase의 평균 활력은endo-amylase에 비해 약 400배 이상 높았다. Exo-amylase의 활력은 재생 6일차(최고수준) 까지 증가하다가 이후 감소하였다. Endo-amylase의 활력은 재생초기 4일 동안 급격히 증가하다가 이후 재생 24일차(최고수준) 까지 서서히 증가하는 경향이었다. 이상의 결과들은 알팔파의 재생초기 동안 전분 분해효소의 활력의 증가와 아울러 뿌리내 저장탄수화물은 활발히 분해되어 새로운 조직의 재생에 이 용됨을 간접적으로 제시한다.

• The Korean Journal of Ecology
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• 제17권2호
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• pp.171-183
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• 1994

Soil condition, total number of bacteria, soil amylase activity and microbial biomass $(CO_2-C)$ were measured at soil of different forest types. And the difference of the allelopathic effect was determined between fresh leaf extract of Quercus acutissima and Pinus rigida to the bacteria isolated from soil of different forest types. 1. Total number of bacteria in Carpinus laxiflora forest soil was 4~7 times larger than that in pinus desiflora forest soil. 2. Soil amylase activity was positively correlated with total number of soil bacteria and soil organic matter content. The amylase activity at F layer was 4~5 times larger than that at H layer, and that at H layer was 2~4 times larger than that at A layer. 3. Seasonal changes of microbial biomass showed a peak in summer, and vertical distribution of microbial biomass decreased with increasing soil depth. The microbial biomass in Pinus densiflora forest soil was larger than that in Quercus serrata forest soil. 4. Fresh leaf extract of Pinus rigida and Quercus acutissima showed an acceleration or inhibition effect on the growth of soil bacteria, and that of !. acutissima inhibited larger number of soil bacterial strains than that of P. rigida. 4.2% and 25% of soil bacterial strains isolated from soil of P. rigida and Q. acutissima forests were inhibited by fresh leaf extract of P. rigida and Q. acutissima, respectively.

• 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.

• 대한약침학회지
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• 제22권2호
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• pp.115-121
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• 2019

Objectives: The objective of this study was to evaluate antidiabetic activity of Chaturmukha rasa based on streptozotocin induced diabetes model, alpha amylase inhibitory activity, alpha Glucosidase inhibitory activity and inhibition of sucrase. Methods: Chaturmukha rasa was prepared as per Ayurvedic formulary. Antidiabetic activity was measured in experimentally streptozotocin induced rats. The dose was taken as 45 mg/kg, i.p. The antidiabetic activity of Chaturmukha rasa was compared Triphala Kwatha, a marketed formulation. Further In vitro $\acute{\alpha}$- Amylase Inhibitory Assay, In vitro salivary amylase Inhibitory Assay, In vitro ${\alpha}-Glucosidase$ Inhibitory Assay and In vitro Sucrase Inhibitory Assay was performed with respect to Chaturmukha rasa. The IC50 value was calculated for all the above activity. Results: Streptozotocin with Acarbose showed significant decrease in blood glucose level whereas streptozotocin with Triphala kwatha showed more decrease in blood glucose level than Streptozotocin with Acarbose. The combination of Streptozotocin + Triphala kwatha + Chaturmukha rasa showed a significant decrease in blood glucose level on 21st day. In vitro $\acute{\alpha}$- Amylase Inhibitory Assay the Chaturmukha rasa showed IC50 value $495.94{\mu}l$ when compared with Acarbose $427.33{\mu}l$, respectively. In the ${\alpha}-Glucosidase$ Inhibitory Assay Chaturmukha rasa showed IC50 value $70.93{\mu}l$ when compared with Acarbose $102.28{\mu}l$, respectively. In vitro Sucrase Inhibitory Assay Chaturmukha rasa showed IC50 value $415.4{\mu}l$ when compared with Acarbose $371.43{\mu}l$, respectively. Conclusion: This study supports that Chaturmukha rasa may inhibit diabetes by inhibition of salivary amylase or alpha Glucosidase or sucrase. This may be the mechanism by which Chaturmukha rasa inhibits diabetes. Further this study supports the usage of Chaturmukha rasa for the management of diabetes.

• 한국미생물·생명공학회지
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• 제14권2호
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• pp.161-168
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• 1986

E. coli-S. cerevisiae shuttle vector인 plasmid YRp7을 이용하여 B. amyloliquefaciens의 $\alpha$-amylase gene을 E. coli 내에 cloning하였다. 이때 제한 효소 Sau 3 AI에 의해 얻어진 $\alpha$-amylase gene의 크기는 약 1.95kb정도였으며 E. coli내에서 비교적 안정하게 유지되고 발현되었다. 재조합 plasmid p-EA24를 함유한 E. coli는 B. amyloliquefaciens의 약 65% 정도의 $\alpha$-amylase를 생성하였으며, 최적온도, pH, CaCl$_2$의 영향등 $\alpha$-amylase의 효소학적인 성질을 비교 조사해 본 결과 B. amyloliquefaciens의 $\alpha$-amylase와 동일하였다. 또한 E. coli에서 생성된 $\alpha$-amylase로 70% 정도가 periplasmic space에 존재하였으며 나머지는 세포 내부에 존재함을 알았다.

• 한국미생물·생명공학회지
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• 제23권5호
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• pp.573-579
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• 1995

A Bacillus strain capable of producing an extracellular malto-oligosaccharides forming $\alpha $-amylase was isolated from soil and designated as Bacillus sp. SUH4-2. The enzyme was purified by ammonium sulfate fractionation, DEAE-Toyopearl and Mono-Q HR 5/5 column chromatographies using a FPLC system. The specific activity of the enzyme was increased by 16.1-fold and the yield was 13.5%. The optimum temperature for the activity of $\alpha $-amylase was 60-65$\circ$C and more than 50% of initial activity was retained after the enzyme was incubated at 60$\circ$C for 40 min. The enzyme was stable over a broad pH range of 5.0-8.0 and the optimum pH was 5.0-6.0. The molecular weight of the enzyme was determined to be about 63.6 kD and isoelectric point was around 5.8. The enzyme activity was strongly inhibited by Mn$^{2+}$, Ni$^{2+}$, and Cu$^{2+}$ ; slightly by Ca$^{2+}$. The purified enzyme produced starch hydrolyzates containing mainly maltose and maltotriose from soluble starch. The starch hydrolyzates were composed of 11% glucose, 59% maltose, 25% maltotriose and 5% maltotetraose.

• Biotechnology and Bioprocess Engineering:BBE
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• 제5권1호
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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.

• 한국식품영양과학회지
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• 제24권4호
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• pp.556-562
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• 1995

The $\alpha$-amylase inhibitor from naked barley was purified by DEAE-cellulose, Concanavalin-A sepharose and superose 6 column chromatography, and confirmed by capillary electrophoresis. The purified $\alpha$-amylase inhibitor showed a single band of 29KD in molecular weight when estimated by the SDS-PAGE. Its purity was increased by 12-fold as compared to its crude extract, and its specific activity was found to be 336.7units/mg. The major amino acids of the $\alpha$-amylase inhibitor from naked barley was appeared to be glutamic acid, asparitic acid and arginine. The inhibitor from naked barley was glycoproteins and carbohydrate content of inhibitor was 1.0%.