• 한국식품영양학회지
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• 제11권3호
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• pp.319-322
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• 1998

본 실험에서는 GI 활성이 높은 alkalophilic Streptomyces sp.를 사용하여 2% $ extsc{k}$-carrageenan에 균체를 고정화 균체의 효소학적 특성을 살펴보았다. pH stability는 pH가 7.5~8.5에서 GI 활성이 가장 높았으며, reaction temperature는 7$0^{\circ}C$, Co2+는 10-3M, Mg2+는 10-3M일 때 GI 활성이 가장 높은 것으로 나타났다.

• 한국미생물·생명공학회지
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• 제28권4호
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• pp.219-222
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• 2000

To produce and utilize microbial cyclomaltodextrinase being industrially useful, we isolated an alkalophilic Bacillus strain from soil which was capable of degrading cyclodextrins. The newly isolated strain was aerobic, gram-positive, spore-forming, motile, rod shape(0.2~0.4$\times$1.4~4.4 $\mu\textrm{m}$), and 35.8 mol% of DNA base composition. Based on its morphological, phisiological, and biochemical properties, it was identified as alkalophilic Bacillus sp. KJ-133 and cultivated well in the ranges of $30~40^{\circ}C$ and pH 8.0~9.0 . The cyclomaltodextrinase of the strain showed maximal production after 48h of cultivation at $37^{\circ}C$, and the activity was inhibited by Ag2+, Hg2+, Cu2+, and p-chloromercuribenzoate.

• 펄프종이기술
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• 제31권5호
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• pp.12-17
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• 1999

This study was to evaluate applications of the alkalophilic enzymes from Coprinus cinereus 2249 with old newsprint(ONP). A enzymatic deinking process based on alkalopholic enzymes was investigated . It was found that alkalophilic enzymes could effectively deink old newsprint. When applied on deinking of the old newsprint, it increases the freeness and brightness due to effect of hydrolysis at 0.1% enzyme concentration . Also, the physical properties of deinked pulp were improved.

• 동아시아식생활학회지
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• 제7권1호
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• pp.35-39
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• 1997

Studies on the glucose isomerase produced by alkalophilic Streptomyces sp. B-2. Glucose Isomerase (E. C. 5.3.1.5) which reversibly catalyzes reaction between D-glucose and D-fructose was demonstrated in cell free extracts of alkalophilic Streptomyces sp. B-2 isolated form soil. The maximum enzyme activity was found at glucose concentration 4(g/$\ell$) , xylose concentration 6(g/$\ell$), magnesium ion 1.0(g/$\ell$), yeast extract concentration 2.0(g/$\ell$), peptone concentration 3(g/$\ell$).

• Journal of Microbiology and Biotechnology
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• 제1권4호
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• pp.251-255
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• 1991

A 16 kilobase (kb) HindIII fragment of alkalophilic Bacillus sp. YC-335 containing a gene for xylanase synthesis was inserted at the HindIII site of pBR322 and cloned in Escherichia coli HB101. After subcloning of recombinant plasmid pYS52, the 1.5 kb fragment was found to code for xylanase activity, and the hybrid plasmid was named pYS55. The DNA insert of the plasmid was subjected to restriction enzyme mapping, which showed that pYS55 had single site for PuvII and SstI in the 1.5 kb insert fragment. Southern hybridization analysis revealed that the cloned gene was hybridized with chromosomal DNA from alkalophilic Bacillus sp. YC-335. About 64% of the enzyme activity was observed in the extracellular and periplasmic space of E. coli HB10l carrying pYS55.

• 한국미생물·생명공학회지
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• 제17권3호
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• pp.178-182
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• 1989

고온, 호알칼리성 Bacillus K-17 균주에서 한가지 xylanase 유전자를 pBR322를 벡터로 이용하여 클로닝시켰다. Xylan을 함유하는 LB 한천배지에서 분해환을 형성하는 대장균 형질전환주에서 재조합 플라스미드 pAXl13을 분리하였으며, 본 pAXl13 은 pBR322와 고온, 호알칼리성 Bacillus K-17균주 염색체 DNA의 4.3Kb HindIII 절편으로 구성되어 있었다. Biotin으로 표식된 pAXl13을 probe로 하여 상동성시험을 하여 본 결과, pAXl13에 존재하는 4.3Kb Hind III 절편은 고온, 호알칼리성 Bacillus K-17 균주 유래임을 확인하였다. pAXl13 을 가지는 E. coli 균주가 생성하는 xylanase는 균체외에 존재하였으며 그 효소학적 성질은 고온, 호알칼리성 Bacillus K-17 균주의 xylanase I 과 II중에서 xylanase I과 동일하였다.

• 생명과학회지
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• 제7권2호
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• pp.95-106
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• 1997

전분의 효율적인 이용을 목적으로 토양으로부터 균체외 플루탄아제효소를 대량분비하는 약알칼리성균주 Bacillus sp. S-1를 분리하였다. 본 균주의 풀루란아제효소 생샨의 최적 pH는 6-10 사이였으며, 조효소의 가용성전분과 플루란에 대한 주요반응 최종산물은 말토트리오스로, 본 효소가 ${\alpha}$-1,6-glycosidic 결합에 특이적임을 알 수 있었다. 본 균주는 지금까지 알려진 알칼리성균주들의 플루란아제 생산성보다 월등히 높은 7.0U/ml를 생산하였으며, 정제효소의 최적 pH와 온도는 각각 8.0-10.0와 50-60$^{\circ}$C로서 알칼리성 및 호열성의 특성을 나타났었다. 또한 정제효소는 pH12에서도 약 10%의 활성을 유지하며, 넓은 pH범위에서도 안정하였다. 이러한 결과들은 본 균주가 플루란아제 생산균주로서의 이용가능한 잠재력을 보유하고 있음을 시사하였다.

• Journal of Microbiology and Biotechnology
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• 제11권4호
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• pp.558-563
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• 2001

A new alkalophilic strain of Bacillus pumilus JB¬05 producing bleach-stable and halo-tolerant alkaline protease was isolated from cement industry effluents in Karnataka, India. The effects of carbon and nitrogen sources on protease production by this alkalophilic strain were observed after a 30-h incubation. A high level of alkaline protease activity was obtained in the presence of starch as the carbon and peptone as the nitrogen sources. The partially purified enzyme showed an optimum temperature and pH activity at $58^{\circ}C$ and 10.5, respectively. The enzyme was completely inhibited by PMSF (95.0%) indicating it as a serine protease. It is bleach-stable as it retained 35% original activity in the presence of 10% (v/v) hydrogen peroxide at $30^{\circ}$C after 2 h and is halo-tolerant as it retained 70% original activity in the presence of 2.5 M sodium chloride at $30^{\circ}C$ after 2 h incubation.

• 한국식품영양학회지
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• 제8권3호
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• pp.253-261
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• 1995

A strain of alkalophilic Bacillus sp. C-21 has been Isolated from sold. The strain was capable of producing large amount of cyclodextrin glycosyltransferase (CGTase) in the high alkaline pH medium. The preferable medium composition was determined to be as follows : 1.0% soluble starch, 1.0% peptone, 0.5% yeast extract, 0.1% K2HP04, 0.02% MgSO4.7H2O and 1.0% Na2CO3(pH 10.0) The highest enzyme production was observed after 30hours of cultivation at 33$^{\circ}C$. The optimum temperature and pH for the activity of crude enzyme were 6$0^{\circ}C$ and 6.0, respectively. The enzyme was stable between pH 6.0 and 9.6, and up to 55$^{\circ}C$.

• 미생물학회지
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• 제31권2호
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• pp.175-178
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• 1993

Alkaline .alpha.-amylase expressed in the transformant, Baciollus subtills MB809, containing alkaline amylase gene cloned from alkalophilic Bacillus sp. AL-8, was purified through for step separation processes. The purified alkaline .alpha.-amylase had molecular weight of app[roximately 59, 000 daltons on SDS-PAGE and Sephaex G-100 gel filtration. Amino acid sequence of terminal portion of the enzyme was analyzed with pure amylase eluted form the SDS-PAGE gel. N-terminal amino acid sequence of .alpha.-amylase was determined by the Edman degradation method and resulted in $NH_{2}$-ser-thr-ala-pro-ser-(ile)-lys-ala-gly-thr-(ile)-leu. For C-terminal amino acid sequencing, purified .alpha.-amylase was digested with carboxypuptidase A and B, and reverse-phase HPLC gradient elution system resulted in -thr-trp-pro-lys-COOH.