• 한국환경보건학회지
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• 제18권1호
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• pp.84-94
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• 1992

In an attempt to develop the immobilized biocatalysts based on immobilized Saccharomyces cerevisiae, immobilized yeast was investigated with respect to the conditions affected to ethanol productivities. Saccharomyces cerevisiae was immobilized in the form of the beads by magnetic-calcium alginate, non magnetic-calcium alginate and acrylamide polymerization. Magnetic immobilized yeast, nonmagnetic immobilized yeast and polyacrylamide immobilized yeast were compared in respect of their pH stability, thermostability, heat tolerance, the relation between the concetration of native yeast and retained activity of immobilized yeast, the activity depending on bead size of immobilized yeast, and the effects of magnesium and cobalt on the activities. The more small bead had retained the higher activity for the three kinds of immobilized yeast. In case of 1.0mm diameter of beads, the retained activity was 40~50% for the all groups. The pH stability profile for the immobilized yeast showed a broad range of optimun activity while the native yeast gave a sharp pick for its optimun pH value. The thermostability was at the range of 25~55$^{\circ}$C for the immobilized yeast groups. It was investigated that the influent magnesium and cobalt concentration, and the relative activity have an influent on heat tolerance at steady state. Both protein content released from immobilized yeast and activity of immobilized yeast were changed after activation of immobilized yeast cell.

• 한국환경보건학회지
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• 제17권1호
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• pp.120-128
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• 1991

Saccharomyces cerevisiae was immobilized by incubating iron oxides with calcium alginate, and by polyacrylamide entrapment to use repeatedly for the conversion of glucose to ethanol. Magnetic and non-magnetic immobilized yeast and polyacrylamide immobilized yeast were compared with the native yeast a batch-fermentation of ethanol from glucose. Three kinds of immobilized yeast tended almost identically, having ethanol productivity as well as the final yield about the same to what was found for the native yeast. The long-term operational stability of three kinds of immobilized yeast were significant difference according as immobilized yeast activation or non-activation before ethanol fermentation. In the non-activation they lost their activity of fermentation rapidly in the beginning stage an slower at a later stage. On the other hand, in the activation with nutrient media, their activities were increased to some extent and stable in the later stage. The cell count of three kinds of immobilized yeast after activiation by incubating nutrient media, increased by a factor of about 45 to 48, whereas the fermenting capacity increased by a factor of 174 to 178. In the prearation of immobilized biocatalysts, magnetic matter does not seem to have any adverse affect on the properties of the microorganism. The immobilized biocatalysts by utilizing magnetic matter have some advantages, especially in application of viscous media or insoluble particle-containing media, for this work was linked with microbial utilization of environmental wastes and elimination of envirnmental pollutant.

• 한국식품영양학회지
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• 제2권2호
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• pp.14-20
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• 1989

A strain of Saccharomyces cerevisiae BY-366 was isolated to produce a strong sucrose-hydrolyzing enzyme. After entrapment of yeast cell invertase with alginate, enzymatic properties of immobilized cells were investigated. The results are as follows. 1. The optimum pH of invertase in immobilized cells and non- immobilized cells was 6.0 and 5.0, and pH stability of invertase in immobilized cells and non- immobilized cells was 6.0 and 5.0, respectively. 2 Activation energy of immobilized cells was 4.7 kcal/mol. 3 The immobilized preparation exhibited high resistance to heat and urea Induced denaturation. 4, The bead size less than 2 mm in diameter was desirable. 5. In spite of repeated use, the enzyme activity of immobilized cells was inhibited slightly in batch reaction, and a small column of the immobilized preparation could hydrolyze relatively high concentration of sucrose almost quantitatively to more than 6 days.

• Biotechnology and Bioprocess Engineering:BBE
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• 제1권1호
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• pp.18-21
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• 1996

A continuous production of fructooligosaccharides from sucrose was investigated by fructosyltransferase immobilized on a high porous resin, Diaion HPA25. The optimum pH(5.5) and temperature(55$^{\circ}C$) of the enzyme for activity was unaltered by immobilization, and the immobilized enzyme became less sensitive to the pH change. The optimal operation conditions of the immobilized enzyme column for maximizing the productivity were as follows: 600g/L of sucrose feed concentration, flow rate of superficial space velocity 2.7h-1. When the enzyme column was run at 50$^{\circ}C$, about 8% loss of the initial activity of immobilized enzyme was observed after 30 days of continuous operation, during which high productivity of 1174g/L$.$h was achieved. The kinds of products obtained using the immobilized enzyme were almost the same as those using soluble enzymes or free cells.

• Journal of Microbiology
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• 제44권3호
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• pp.354-359
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• 2006

This study examined the capacity of immobilized bacteria to degrade petroleum hydrocarbons. A mixture of hydrocarbon-degrading bacterial strains was immobilized in alginate and incubated in crude oil-contaminated artificial seawater (ASW). Analysis of hydrocarbon residues following a 30-day incubation period demonstrated that the biodegradation capacity of the microorganisms was not compromised by the immobilization. Removal of n-alkanes was similar in immobilized cells and control cells. To test reusability, the immobilized bacteria were incubated for sequential increments of 30 days. No decline in biodegradation capacity of the immobilized consortium of bacterial cells was noted over its repeated use. We conclude that immobilized hydrocarbon-degrading bacteria represent a promising application in the bioremediation of hydrocarbon-contaminated areas.

• 한국식품과학회지
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• 제46권3호
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• pp.315-322
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• 2014

본 연구는 미생물로부터 유래된 5종(AH, AK, AY, PS와 R)의 lipase들을 Amberlite XAD 7에 흡착법으로 고정화 시킨 후 각 immobilized lipase들의 특성을 알아보았다. 고정화 전과 후의 단백질 함량 및 각 free lipase들과 immobilized lipase들을 이용한 interesterification 반응물의 지방산과 TAG 조성을 분석하였다. 또한, immobilized lipase에 있어 중요한 요인인 reusability를 확인하였다. Free lipase의 단백질 함량은 2.22-11.41%로 AH가 가장 높았던 반면, immobilized lipase에서는 AH, PS와 AK가 mg protein/g support이 높았다. 한편, 반응 특성을 알아보기 위해 카놀라유, PEE와 StEE를 기질로 하여 batch type interesterification을 진행하였을 때, free lipase의 경우 free lipase R을 제외한 다른 free lipase들은 반응시간이 1시간에서 72시간으로 증가함에 따라 총 포화지방산 함량이 증가하였으며 그 중 free lipase AH가 반응성이 가장 높았다. 또한, RP-HPLC를 통해 free lipase AK 반응물을 분석한 결과, 반응시간이 길어질수록 카놀라유(0시간)에서 볼 수 있었던 57.49 area%의 ${\bigcirc}{\bigcirc}{\bigcirc}$가 6.53 area%로 감소하였다. 이는 각 free lipase들이 PEE와 StEE를 효소적 반응에 이용했기 때문이라고 판단된다. 한편, immobilized lipase AY와 R의 경우 반응시간이 1시간에서 48시간으로 증가하여도 카놀라유(0시간)의 총 포화지방산 함량과 큰 차이가 없었으나 immobilized AK의 경우 48시간에서 38.3 area%의 포화지방산 함량으로 가장 높은 활성을 보였다. 또한, 이를 사용하여 continuous type으로 반응하였을 때 유속이 느릴수록 효소와 기질 사이의 접촉 시간이 길어져 반응물의 총 포화지방산 함량이 증가함을 알 수 있었다. Reusability는 immobilized AK, AH와 PS 모두에서 두 번째 반복 반응을 하였을 때, 첫 번째 반응보다 총 포화지방산이 120-196.5% 증가하였다. 그러나 bounding protein 함량이 가장 높았던 immobilized AK는 support에 흡착되었던 free lipase AK의 탈착이 일어나 2번째 반응 후부터 활성이 감소한 반면, immobilized AH와 PS는 활성이 비교적 유지되었다.

• Journal of Microbiology and Biotechnology
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• 제17권9호
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• pp.1430-1436
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• 2007

[ ${\alpha}$ ]-Galactosidase was immobilized in a mixture of k-carrageenan and locust bean gum. The properties of the free and immobilized enzyme were then determined. The optimum pH for both the soluble and immobilized enzyme was 4.8. The optimum temperature for the soluble enzymes was $50^{\circ}C$, whereas that for the immobilized enzyme was $55^{\circ}C$. The immobilized enzyme was used in batch, repeated batch, and continuous modes to degrade the raffinose-family sugars present in soymilk. Two hours of incubation with the free and immobilized ${\alpha}$-galactosidases resulted in an 80% and 68% reduction in the raffinose oligo saccharides in the soymilk, respectively. In the repeated batch, a 73% reduction was obtained in the fourth cycle. A fluidized bed reactor was also designed to treat soymilk continuously and the performance of the immobilized ${\alpha}$-galactosidase tested at different flow rates, resulting in a 90% reduction of raffinose-family oligosaccharides in the soymilk at a flow rate 40 ml/h. Therefore, the present study demonstrated that immobilized ${\alpha}$-galactosidase in a continuous mode is efficient for reducing the oligosaccharides present in soymilk, which may be of considerable interest for industrial application.

• 한국미생물·생명공학회지
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• 제27권3호
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• pp.208-214
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• 1999

The condition for immobilization of the partially purified agarase from Bacillus cereus ASK202 and the properties of the immobilized enzyme have been investigated. Agarase was immobilized on various supports by entrapment method. The enzyme immobilized on Na-alginate bead showed the highest activity among those studied. The optimal reaction conditions of the immobilized agarase were obtained in 3%(w/v) Na-alginate for the matrix, bead diameter of 2.5mm, 1 unit of agarase solution and 1.0%(w/v) calcium chloride solution. The optimum pH and temperature of the immobilized agarase were pH and temperature of the immobilized agarase were pH 7.0 and 4$0^{\circ}C$, respectively. Km and Vmax values were 0.5mg/ml.min, respectively. The immobilized agarase conerted agar to agarobiose, and their total conversion ratio under the optimal condition was 89%.

• 한국식품저장유통학회지
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• 제5권2호
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• pp.186-190
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• 1998

In order to investigate the possible application of immobilized yeast cells in sparkling wine production instead of riddling puns by the traditional method, fermentation characteristics were tested during the sparkling wine fermentation in the bottle using immobilized yeast cells with alginate. The rates of sugar consumption and alcohol production were faster with free cells than those with immobilized cells during the fermentation. The higher concentration of yeast cells and the lower concentration of alginate in the cell immobilization resulted in the faster sugar consumption and alcohol production. It also resulted in the increase of yeast cell concentration released from immobilized beads during the fermentation. However, no differences were shown in the contents of alcohol, residual sugar and CO2 pressure after fermentation. In case concentration of yeast cells released from immobilized beads during bottle fermentation, the higher concentration of alginate had and the lower had.

• 한국식품영양과학회지
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• 제22권6호
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• pp.797-802
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• 1993

The properties of the alcohol-oxidase from yeasts assimilating of methanol(Hansenula polymorpha CBS 4732, Pichia pastoris CBS 2612 and Candida boidinii CBS 8106) as free(cellules, purified enzymes) and immobilized forms(immobilized cellules, immobilized enzymes) were investigated. Immobilization enhanced the activity and stability of alcohol-oxidase to a certain degree. The optimum temperature of the immobilized alcohol-oxidase was lower than those of the free forms. The pH / activi쇼 profiles of alcohol-oxidase did not change by immobilization, but changed by the microorganisms. When the immobilized cellules were stocked at 4$^{\circ}C$ in 10mM potassium phosphate buffer(pH 7.5 or 8.0), alcohol-oxidase was more stable than those were stocked in potassium phosphate buffer containing 0.65M sucrose. The immobilization modifies the conditions of oxidation on the various substrates. alcohol-oxidase in immobilized forms showed some with higher Km value for methanol than that in free ones.