• Mycobiology
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• 제33권3호
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• pp.142-146
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• 2005

To produce a novel antihypertensive angiotensin I-converting enzyme (ACE) inhibitor from yeast, a yeast isolate, designated G-14 showing the highest ACE inhibitory activity was obtained and identified as Malassezia pachydermatis based on morphological, biochemical and cultural characteristics. The maximal extracellular ACE inhibitor production was obtained from M. pachydermatis G-14 when the strain was cultured in YEPD medium containing 0.5% yeast extract, 3.0% peptone and 2.0% glucose at $30^{\circ}C$ for 24 h and the final ACE inhibitory activity was 48.9% under the above condition.

• 한국식품영양과학회지
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• 제28권1호
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• pp.172-177
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• 1999

Branched maltodextrin which contains branched sugars as well as linear sugars was produced by Tranzyme L 500. Branched sugar content increased as reaction time between substrate(D.E. 19) and 0.05% of Tranzyme L 500 at pH 5.5, 55oC increased. Branched sugar content was 14.9% at 24 hr of reaction and reached 27% after 60 hr. Total branched sugar content increased regardless of substrate D.E. as enzyme concentration increased. However, when concentrations of enzyme were 0.1, 0.2%, production of branched sugars of which content were 46.6%, 52.6% respectively at those enzyme concentrations, was higher at D.E. 19 than any other conditions.

• 한국응용곤충학회지
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• 제28권2호
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• pp.69-75
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• 1989

B. thuringiensis subsp. kurstaki HD-1을 아밀라제 생산배지에 $32^{\circ}C$로 24시간 배양하였을 때 아밀라제 활성은 0.40 units/ml 였고, 50mM EDTA에 의하여 활성이 억제되었으며, 기본배지에 soluble starch와 $Ca^{2+}$, $Mg^{2+}$, $Mn^{2+}$을 첨가했을 때 활성이 비교적 높았고, pH6.5와 7.0 사이에서, 온도 $55^{\circ}C$에서 비교적 활성이 높았다. 아밀라제 생산을 위한 최적 배지로는 0.2% soluble starch, 1.0% bacto-peptone, 0.3% beef extract, 0.5% NaCl, 0.3% $K_{2-}$$KH_{2}PO_{4}$, 0.012% CaCl.$2H_{2}O$, 0.005% $MnSO_{4}$.$H_{2}O$, 0.03% $MgSO_{4}$.$7H_{2}O$이었다. 효소 용액을 에 $HPO_{4}$, 0.1% 탄올 침전시켜 5ml의 0.1M 인산염 완충액에 용해한 용액의 비활성은 2.01 units/mg였고, starch에 대한 효소의 Km 값은 0.80 mg/ml였다.

• Biotechnology and Bioprocess Engineering:BBE
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• 제2권2호
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• pp.90-93
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• 1997

Recombinant exoinulinase was partially purified form the culture supernatant of S.cerevisiae by(NH4)2SO4 precipitation and PEG treatment. The purfied inulinase was immobilized onto Amino-cellulofine with glutaraldeyde as a cross-linking agent. Immobilization yield based on the enzyme activity was about 15%. Optimal pH and temperature of immobilized enzyme were found to be 5.0 and 6$0^{\circ}C$, respectively. The enzyme activity was stably maintained in the pH ranges of 4.5 to 6.0 at 6$0^{\circ}C$. 100% of enzyme activity was observed even after incubation for 24 hr at 6$0^{\circ}C$. In the operation of a packed-bed reactor containing 412U inulinase, dahalia inulin of 7.5%(w/w) concentration was completely hydrolyzed at flow rate of 2.0mL/min at 6$0^{\circ}C$, resulting in a volumetric productivity of 693 g-reducing sugars/L/h. Under the reaction conditions of 1.0mL/min flow rate with 2.5% inulin at 6$0^{\circ}C$, the reactor was successfully operated over 30 days without loss ofinulinase activity.

• 한국식품영양과학회지
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• 제29권1호
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• pp.49-56
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• 2000

The 2-O-$\alpha$-D-glucopyranosyl L-ascorbic acid (AA-2G) which was enzymatically glucosylated with the cyclodextrin glucanotransferase (CGTase) [EC 2.4.1.19] from Bacillus sp. JK-43 has been reported previously. The presnet experiments examined the optimal conditons for the productio of AA-2G from AA and soluble starch, and characterized the properties of the CGTase from Bacillus sp. JK-43. The reaction mixture for the maximal production of AA-2G was followings; 12% total substrate concentration, 1,400 usits/mL of CGTase and a mixing ratio of 2 : 3(g or AA : g of soluble starch). Under this condition, 1.76mM of AA-2G, which corresponded to 2.53% yield based on AA, was produced after incubation for 24hrs at 45$^{\circ}C$ (pH 5.5). The optimum pH and temperature for the CGTase activity were 6.0 and 45$^{\circ}C$, respectively. The enzyme was stable at pH 5.5 to 9.5, and at temperature up to 5$0^{\circ}C$. The thermostability of the enzyme could be enhanced up to 6$0^{\circ}C$ by the addition of 30mM CaCl2.

• Applied Biological Chemistry
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• 제24권2호
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• pp.85-93
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• 1981

섬유소(纖維素)를 이용(利用)하기 위한 기초연구(基礎硏究)로서 섬유소분해능(纖維素分解能)이 우수(優秀)한 균주(菌株)를 분리(分離)하여 동정(同定)한 결과(結果) Trichoderma spp.로 추정하였으며 사용된 섬유소 기질(基質)은 볏짚을 용제(溶劑)로 전처리(前處理)한 것과 여기에 산, 가열처리(加熱處理)를 더 가(加)한 것을 사용(使用)하였으며 이 미생물(微生物)에 의(依)하여 전처리 및 산 가열처리(加熱處理)에서 생성되는 섬유소 분해 효소(酵素)를 시험한 결과(結果) 0.1% $H_2SO_4$, $120^{\circ}C$, 한시간동안 처리한 것을 기질(基質)로 하였을 때 효소활성(酵素活性)이 높았다. 또한 pH 5.0, 5일(日) 배양(培養)에서 효소활성(酵素活性)이 증가(增加)하였으며 요소첨가시 20%. 인산칼륨첨가시 21%, 육류추출물첨가시 25%, 감귤피첨가시 19%의 증가(增加)를 나타냈다. 48시간(時間) 효소반응(酵素反應)을 시켰을 때 전처리기질(前處理基質)보다 산(酸), 가열처리기질(加熱處理基質)이 효소활성(酵素活性)이 높았으며 24시간후(時間後)에는 활성(活性)이 완만하였다.

• Journal of Microbiology and Biotechnology
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• 제12권2호
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• pp.189-195
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• 2002

Using Streptomyces sp. YU100 isolated from Korean soil, the fermentative production of phospholipase D was attempted along with its purification and characterization studies. When different carbon and nitrogen sources were supplemented in the culture medium, glucose and yeast extract were found to be the best. By varying the concentration of nutrients and calcium carbonate, the optimal culture medium was determined as 2.0% glucose, 1.5% yeast extract, 0.5% tryptone 0.3% calcium carbonate. During cultivation, the strain secreted most of the phospholipase D in the early stage of growth within 24 h. The phospholipase D produced in the culture broth exhibited hydrolytic activity as well as transphosphatidylation activity on lecithin (phosphatidylcholine). In particular, the culture broth showed 8.7 units/ml of hydrolytic activity when cultivated at $28^{\circ}C$ for 1.5 days. The phospholipase D was purified using 80% ammonium sulfate precipitation and DEAE-Sepharose CL-6B column chromatography, which produced a major band of 57 kDa on a 10% SDS-polyacrylamide gel with purity higher than 80%. The enzyme showed an optimal pH of 7 in hydrolytic reaction, and at pH 4 in a transphosphatidylation reaction. The enzyme activity increased until the reaction temperature was elevated to $60^{\circ}C$. The enzyme was relatively stable at high temperatures and neutral pH, but significantly unstable in the alkaline range. Among the detergents tested as emulsifiers of phospholipids, the highest enzyme activity was observed when 1.5% Triton X-100 was employed. However, no inhibitory effect by metal ions was detected. Under optimized reaction conditions, the purified enzyme not only completely decomposed PC to phosphatidic acid within 1 h, but also exhibited higher than 80% conversion rate of PC to PS by transphosphatidylation within 4 h.

• 한국유기농업학회지
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• 제20권3호
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• pp.327-343
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• 2012

In order to develop a high cellulolytic direct-fed microorganism (DFM) for ruminant productivity improvement, this study isolated cellulolytic bacteria from the rumen of Holstein dairy cows, and compared their cellulolytic abilities via DM degradability, gas production and cellulolytic enzyme activities. Twenty six bacteria were isolated from colonies grown in Dehority's artificial (DA) medium with 2% agar and cultured in DA medium containing filter paper at $39^{\circ}C$ for 24h. 16s rDNA gene sequencing of four strains from isolated bacteria showed that H8, H20 and H25 strains identified as Ruminococcus flavefaciens, and H23 strain identified as Fibrobacter succinogenes. H20 strain had higher degradability of filter paper compared with others during the incubation. H8 (R. flavefaciens), H20 (R. flavefaciens), H23 (F. succinogenes), H25 (R. flavefaciens) and RF (R. flavefaciens sijpesteijn, ATCC 19208) were cultured in DA medium with filter paper as a single carbon source for 0, 1, 2, 3, 4 and 6 days without shaking at $39^{\circ}C$, respectively. Dry matter degradability rates of H20, H23 and H25 were relatively higher than those of H8 and RF since 2 d incubation. The cumulative gas production of isolated cellulolytic bacteria increased with incubation time. At every incubation time, the gas production was highest in H20 strain. The activities of carboxymethylcellulase (CMCase) and Avicelase in the culture supernatant were significantly higher in H20 strain compared with others at every incubation time (p<0.05). Therefore, although further researches are required, the present results suggest that H20 strain could be a candidate of DFM in animal feed due to high cellulolytic ability.

• KSBB Journal
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• 제25권5호
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• pp.453-458
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• 2010

본 연구에서는 효소의 재활용성과 안정성을 확보하기 위해 자석으로 분리가 가능한 polyaniline nanofiber를 개발하였다. 개발된 고정화 효소는 상온에서 8일 동안 90% 이상의 활성도를 보유하였으며 온도가 높은 $55^{\circ}C$에서는 60% 이상의 활성도를 보유하여 안정성의 유지현상을 보였다. 개발된 고정화 효소는 자석으로 분리가 가능하였으며 이 효소를 이용하여 curdlan, agarose, cellulose, 및 미역을 분해한 결과 포도당을 생산하였으며 curdlan을 분해시킨 경우에는 분해 속도가 1.2 g/L/h로 나타나 다른 다당류에 비해 3-10배 이상 빠른 속도를 나타내었다. 고정화 효소를 반복하여 사용하는 경우 10번 반복 사용했을 때 75% 이상의 활성도를 유지하는 것으로 측정되었다. 젖은 미역 줄기를 10 g/L를 분해하기 위하여 5 mg의 고정화 효소를 사용한 결과 24시간 만에 1 g/L의 glucose를 생산하였다.

• 한국미생물·생명공학회지
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• 제24권6호
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• pp.652-656
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• 1996

The 80 strains which produce carrageenan degrading enzyme were isolated from soils, mud, seaweed, marine moluscus and echonodermata samples. Among them, one isolated strain, which showed the highest activity to produce carrageenan degrading enzyme, was used for this study. The isolated strain was identified as Pseudomonas alcaligenes through its morphological, biochemical, and physiological characteristics. The best conditions for enzyme production were 0.7% nutrient broth and 0.2% carrageenan as nitrogen and carbon source, respectively. The optimal pH, NaCl, temperature and culture time for carrageenan degrading enzyme were 7.0, 1.5%, 30* and 96hrs, respectively.