• 한국미생물·생명공학회지
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• 제17권2호
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• pp.160-164
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• 1989

알카리성 Bacillus sp. AL-8의 알카리성 amylase 유전자를 포함하는 5.7Kb의 EcoRI 단편을 pUB 110을 vector로 하여 amylase를 생산하지 못하는 B. subtilis sta-1에서 발현시켰다. 재조합 plasmid pMB802와 pMB809는 숙주세포인 B. subtilis에서 매우 안정하게 유지되었으며 amylase 생산이 공여균 주에서 보다 1.8배 증가하였다. 형질전환주에서 생산된 amylase는 공여균주와 같은 효소적 성질을 나타내었다. 5.7Kb 단편을 E. coli에 subcloning한 결과 3.7Kb의 EcoRI 단편에 알카리성 amylase 유전자가 존재하였다.

• Preventive Nutrition and Food Science
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• 제20권3호
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• pp.210-214
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• 2015

Grape pomace is an abundant source of underutilized winery by-products. Polyphenols were extracted from grape pomace using cellulase and gluco-amylase enzymes. 2,2-diphenyl-1-picrylhydrazyl (DPPH) and Folin-Ciocalteu's assays were used to measure antioxidant activity and total polyphenolic contents. Both cellulase, and gluco-amylase digested grape pomace showed efficient radical scavenging activity. In addition, the total polyphenolic contents of cellulase digested grape pomace showed lower concentrations were effective compared to higher concentrations, whereas glucoamylase enzyme did not show remarkable variations. The DPPH radical scavenging activity and total polyphenolic contents were significantly higher in the cellulase digested grape pomace compared to the gluco-amylase digested and the not digested grape pomace. It is notable that enzymatic digestions were efficient for extracting polyphenols from grape pomace. The underutilized grape pomace polyphenols can be further used for food safety as a natural antioxidant.

• 한국수산과학회지
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• 제44권6호
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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.

• 한국약용작물학회지
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• 제17권5호
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• pp.357-362
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• 2009

Compounds of isolated from roots extract of Pueraria thunbergiana were tested their inhibitory effects on $\alpha$-glucosidase and $\alpha$-amylase. Inhibitory activity of methylene chloride (MC) fraction and ethyl acetate (EA) fraction against $\alpha$-glucosidase showed more than 60% at a concentration of $500{\mu}g/m{\ell}$. Among the nine compounds tested on $\alpha$-glucosidase, biochanin A, (-)-tuberosin and calycosin from MC fraction and daidzein from EA fraction were stronger inhibitors than acarbose ($IC_{50}=530{\mu}g/m{\ell}$), and their $IC_{50}$ were 9, 144, 328 and $20{\mu}g/m{\ell}$, respectively. Biochanin A and (-)-tuberosin also inhibited $\alpha$-amylase activity as like as acarbose $IC_{50}=20.5{\mu}g/m{\ell}$), and their $IC_{50}$ were 22 and $348{\mu}g/m{\ell}$, respectively. Although daidzein was already known $\alpha$-glucosidase inhibitory effects, it was newly evaluated that biochanin A and (-)-tuberosin inhibited $\alpha$-glucosidase as well as $\alpha$-amylase, and that calycosin did $\alpha$-glucosidase.

• 한국잡초학회지
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• 제2권1호
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• pp.13-19
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• 1982

${\alpha}$-chloroactamide 계(系)의 제초제(除草劑) Metolachlor의 수도(水稻)의 생육(生育) 및 생리적(生理的) 작용(作用)에 대하여 어떠한 영향(影響)을 미치는 가를 조사(調査)하여 수도용(水稻用) 제초제(除草劑)로 이용(利用)키 위한 기초자료(基礎資料)를 얻고져 본(本) 시험(試驗)을 수행(遂行)하였던 바 얻어진 결과(結果)는 다음과 같다. 1, Metolachlor $10^{-6}$M과 $GA_310^{-3}$M의 동시처리구(同時處理圖)가 무처리구(無處理區)에 비하여 189.7%, Metolachlor처리(處理) 24시간(時間)전(前)의 $GA_310^{-3}$M 처리구(處理區)에서 135.4%, 48 시간전(時間前) 處理(처리)는 117.5%로 Metolachlor $10^{-6}$M 단독처리구(單獨處理區)에서의 29%에 비하여 $GA_3$ 처리구(處理區)는 공(共)히 第1本葉(제1본엽)이 신장(伸長)되어 Metolachlor의 억제작용(抑制作用)을 극복(克服)하는 효과(効果)를 나타내었으며 뿌리에서 보다 신초(新鞘)에서의 반응도(反應度)가 컸다. 2. 벼 종자내(種子內)의 주된 저장물질(貯藏物質)인 전분(澱粉)과 단백질(蛋白質)은 Metolachlor 처리(處理)에 의해서 분해(分解)가 크게 억제(抑制)되었으며 동시(同時)에 전분(澱粉)의 분해(分解)에서 생성(生成)왼 당(糖)의 함량(含量)도 처리구(處理區)에서 적었다. 3. ${\alpha}$-amylase의 total activity는 Metolachlor 처리구(處理區)와 무처리구간(無處理區間)에 5%의 유의(有意)한 차(差)가 인정(認定)되었으며 처리후(處理後) 시일(時日)이 경과(經過)할수록 차(差)는 컸다. ${\alpha}$-amylase의 specific activity는 시일(時日)에 관계(關係)없이 처리구(處理區)와 무처리구간(無處理區間)에 유의(有意)한 차(差) 인정(認定)되지 않아 Metolachlor은 ${\alpha}$-amylase의 생성(生成)에 억제영향(抑制影響)을 마치는 것 같다.

• Journal of Microbiology and Biotechnology
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• 제9권3호
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• pp.260-264
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• 1999

The combined activities of dextranase and amylase(DXAMase) from Lipomyces starkeyi KSM 22 produced from starch fermentation inhibited or prevented dental plaque formation. The activities were stable in commercial mouthwash products; DXAMase activity retained over 93％ of original activity after 6 months at 23℃. We examined the effects of enzyme inhibitors and active ingredients in mouthwash on DXAMase activity. The DXAMase was stable with 0.29％(w/v) EDTA, 20％ (v/v) ethanol, 0.05％ (w/v) fluoride, and 0.05％ (w/v) SDS. Among the active ingredients of mouthwash, sodium benzoate (up to 1 ％, w/v) had no inhibitory effect on either dextranase or amylase activity. In the case of cetylpyridinium chloride, the addition of 0.05％ (w/v) inhibited 6％ of dextranase activity and 13％ of amylase activity. Propylene glycol (up to 1％, w/v) showed no inhibitory effect on either enzyme activity. DXAMase (5 IU/㎖) in mouthwash could remove pre-formed films of glucan-bound S. mutans cells. The addition of 0.1 IU/㎖ DXAMase in mouthwash prevented the formation of insoluble-glucan. These in vitro properties of L. starkeyi KSM 22 DXAMase are desirable for its application as a dental plaque control agent.

• Journal of Microbiology and Biotechnology
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• 제23권4호
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• pp.489-498
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• 2013

A new Bacillus strain degrading starch, named Bacillus sp. UEB-S, was isolated from a southern Tunisian area. Amylase production using solid-state fermentation on millet, an inexpensive and available agro-resource, was investigated. Response surface methodology was applied to establish the relationship between enzyme production and four variables: inoculum size, moisture-to-millet ratio, temperature, and fermentation duration. The maximum enzyme activity recovered was 680 U/g of dry substrate when using $1.38{\times}10^9$ CFU/g as inoculation level, 5.6:1 (ml/g) as moisture ratio (86%), for 4 days of cultivation at $37^{\circ}C$, which was in perfect agreement with the predicted model value. Amylase was purified by Q-Sepharose anion-exchange and Sephacryl S-200 gel filtration chromatography with a 14-fold increase in specific activity. Its molecular mass was estimated at 130 kDa. The enzyme showed maximal activity at pH 5 and $70^{\circ}C$, and efficiently hydrolyzed starch to yield glucose and maltose as end products. The enzyme proved its efficiency for digesting raw cereal below gelatinization temperature and, hence, its potentiality to be used in industrial processes.

• 환경위생공학
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• 제23권1호
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• pp.25-31
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• 2008

A bacterial strain, Bacillus megaterium L-49 has been isolated and identified that produces alkaline ${\alpha}$-amylase. The cell is ellipsoidal, about $1.0-1.2{\times}3.0-3.6{\mu}m$ in diameter, Gram-positive, motile, and central partial central. Growth occurs in media containing 7% of NaCl. This strain could utilize D-glucose, lactose, xylose, sucrose, mannose, and maltose, and but it does not utilize D-fructose, and glycogen. Among the various concentrations of saturated ammonium sulfate, the retractation ratio in range of 70 to 100% was about 93%. However, in the case of acetone, it was about 98.7%. EDTA has activating effect and Ca2+ has no effect on alkaline ${\alpha}$-amylase activity. The alkaline ${\alpha}$-amylase has low thermal stability. The optimal temperature for reaction is $50^{\circ}C$. The alkaline ${\alpha}$-amylase activity maintained stabilizing at pH 6-11 and the optimal pH for reaction was 9-10.

• 한국식품영양과학회지
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• 제44권5호
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• pp.681-686
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• 2015

약용식물 23종 메탄올 추출물의 폴리페놀 함량을 측정한 후 항산화 활성을 측정하고, 항당뇨 활성으로는 ${\alpha}$-amylase 저해 활성, ${\alpha}$-glucosidase 저해 활성을 검정하여 혈당강하 활성을 나타낼 수 있는 약용식물을 선발하고자 한다. 약용식물의 폴리페놀 함량을 분석한 결과 1.50~15.25 mg GAE/g의 다양한 함량 범위로 나타났으며 가장 높은 함량은 주목열매(15.25 mg GAE/g), 화살나무줄기(15.12 mg GAE/g), 두충잎(14.24 mg GAE/g)으로 3종이 나타났다. 60% 이상 DPPH 라디칼 소거능을 본 약용식물로는 두충 줄기수피(80.10%), 구기자나무 뿌리(64.25%), 화살나무 줄기(73.59%), 비수리(78.20%), 주목열매(70.52%), 뽕잎나무 잎줄기(67.81%) 부위 추출물로 6종이 선발되었다. ${\alpha}$-Glucosidase를 80% 이상 저해한 약용소재로는 두충 줄기심재, 두충 줄기수피, 화살나무 줄기, 마, 율무, 녹두 6종이 선발되었다. ${\alpha}$-Amylase를 80% 이상 저해한 약용식물로는 칡뿌리, 두충 줄기수피, 두충잎, 구기자 열매, 화살나무 잎줄기, 화살나무 줄기, 조릿대 지상부, 마, 뽕잎나무 잎줄기 추출물 등 9종이 선발되었다. 항산화 및 항당뇨 활성이 우수했던 약용식물들은 향후 새로운 의약품 개발 및 성인병 예방의 건강기능식품으로 개발하는 데 있어 좋은 기초자료로 활용될 것으로 기대된다.

• Journal of Microbiology and Biotechnology
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• 제2권2호
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• pp.85-91
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• 1992

The intestinal microflora of humans is an extraordinarily complex mixture of microorganisms, the majority of which are anaerobic microorganisms. The distribution of amylolytic microorganisms in the human large intestinal tract was investigated in various individuals of differing ages using anaerobic culture techniques. A large percentage of the amylolytic microorganisms present belonged to the Genus Bifidobacteria. The number of Bifidobacteria increased significantly at two years of age. Adults and children above 2 years old carried about $0.8{\times}10^9-2.0{\times}10^{10}$ colony forming units (CFU/gram) of amylolytic Bifidobacteria. Among these amylolytic Bifidobacteria, Int-57 was chosen for further studies. Between 65% and 85% of the amylase produced was secreted and the remaining amylase was bound to the cell wall facing the outside. Amylase production could be induced by starch in a stable form. When cells were grown on maltose or glucose, amylase production was much lower than on starch and amylase activity disappeared after 24 hours growth on these media. Partially purified enzymes showed optimum activity at a temperature of $50^{\circ}C$ and at an optimum pH of 5.5, respectively. Heat treatment at $70^{\circ}C$ for 30 minutes almost completely inactivated amylase. The hydrolysis products of starch were mainly maltose and maltotriose. Soluble starch, amylose, amylopectin, and $\gamma$-cyclodextrin($\gamma$-CD) were easily hydrolyzed. The rate of hydrolysis of $\alpha$-CD and $\beta$-CD was slower than that of $\gamma$-CD. Carboxymethyl cellulose, $\beta$-1, 3-glucan and inulin were not hydrolyzed.