• KSBB Journal
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• 제23권6호
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• pp.509-512
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• 2008

원료물질인 대두유를 산가수분해하여 지방산의 함량을 분석한 결과 linoleic acid, oleic acid, palmitic acid, stearic acid의 함량순으로 분석되었다. 동일한 조건하에 대두유의 가수분해반응 전화율을 조사한 결과 Candida rugosa와 Candida cylindracea 에서 유래된 효소인 CR-E와 CC-E가 Lipase 16, Novozyme 871과 Lipolase-100 L보다 2배이상 높았다. 따라서 CR-E와 CC-E를 선정하여 반응조건에 대한 실험을 수행하였다. CR-E와 CC-E의 경우 비슷한 결과를 보여, pH $3{\sim}6$, $35-45^{\circ}C$, 물과 대두유의 중량비가 3.3 이상이었을 때가 최적인 반응조건이었으며 95% 이상의 높은 전화율을 나타내었다.

• 식품기술
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• 제7권2호
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• pp.64-73
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• 1994

Using 20 lipases from various microbial origins medium chain glycerides, namely, mono-, di-, and tri-carproyl glycerols from glycerol and acid were synthesized in isooctane. Enzyme reaction was performed at 0.35 M of capric acid, 0.025M of glycerol and the same mass of silica gel to remove water in 5ml of isooctane with 30mg of lyophilized lipase. Among 20 lipases, eleven lipases showed good synthetic activities, especially lipase from Pseudomonas aeruginosa (Lipase PS), Rhizomucor miehei origined lipase and Chromobacterium viscosum lipase (Lipase CV) showed good activities for production of tricaproylglycerol, while Lipase OF-360 (origined from Candida rugosa) and Lipase D (Rhizopus delemar) were good for production of dicaprolyglycerol. The lipases, especially Lipase PS, have high thermal stability at $ 60^{circ}C$, and optimum pH of lyophilization for dehydrating the lipase was pH 6.5.

• Journal of Microbiology and Biotechnology
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• 제7권2호
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• pp.151-156
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• 1997

Two commercially available lipases, Lipase OF (non-specific lipase from Candida rugosa) and Lipolase 100T (1, 3-specific lipase from Aspergillus niger), were immobilized on insoluble hydrophobic support HDPE (high density polyethylene) by the physical adsorption method. Hydrolysis performance was enhanced by mixing a non-specific Lipase OF and a 1, 3-specific Lipolase 100T at a 2 : 1 ratio. The results also showed that the immobilized lipase maintained its activity at broader temperature ($25~55^{\circ}C$) and pH (4-8) ranges than soluble lipases. In the presence of organic solvent (isooctane), the immobilized lipase retained most of its activity in upto 12 runs of hydrolysis experiment. However, without organic solvent in the reaction mixture, the immobilized lipase maintained most of its activity even after 20 runs of hydrolysis experiment.

• Biotechnology and Bioprocess Engineering:BBE
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• 제6권2호
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• pp.150-155
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• 2001

It has been observed that water, which is absolutely essential for enzyme activity, can induce the agglomeration of enzyme particles in organic media. Although enzyme agglomeration is significant in that it usually reduces enzyme activity and stability, little attention has been paid to the quantitative analysis of enzyme agglomeration behavior in nonaqueous biocatalytic systems. In this study, the effect of water and silica gel on enzyme agglomeration were investigated using Candida rugosa lipase and cyclohexane as a model enzyme and an organic medium. The extent of enzyme agglomeration was quantified by sieve analysis of freeze-dried agglomerates. Increasing the water content of the medium increased the size of the enzyme agglomerates, and it was found that water produced during the esterification reaction could also promote the agglomeration of enzyme particles suspended in organic media. On the other hand, the size of the enzyme agglomerates was remarkably reduced in the presence of silica gel at the same water content. We also show that this increase in the size of enzyme agglomerates results in lower reaction rates in organic solvents.

• 한국의류학회지
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• 제36권6호
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• pp.653-662
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• 2012

This study measured the effect of general pre-treatment on PLA fabrics to confirm the benefits of enzymatic processing on PLA fabrics in the textile industry as well as evaluated the hydrolytic activities of three lipases. The effects of lipase hydrolysis were analyzed through moisture regain, dyeing ability, tensile strength, and surface morphology. As a result, PLA fibers were easily damaged by a low concentration of sodium hydroxide and a low treatment temperature. The optimal treatment conditions of Lipase from Candida cylindracea were pH 8.0, $40^{\circ}C$, and 1,000 U. The optimal treatment conditions for Lipase from Candida rugosa were pH 7.2, $37^{\circ}C$, and 1,000 U. The optimal treatment conditions for Lipase from Porcine pancreas were pH 8.0, $37^{\circ}C$, and 2,000 U. The moisture regain and dyeing ability of PLA fabrics increased and the tensile strength of PLA fabrics decreased. The results of surface morphology revealed that there were some cracks due to hydrolysis on the surface of the fiber.

• Bulletin of the Korean Chemical Society
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• 제24권9호
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• pp.1269-1275
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• 2003

The quaternary carbon-containing alcohols (1-6) were resolved enantioselectively by various lipases such as PFL (Pseudomonas fluorescens lipase), LAK (Pseudomonas fluorescens lipase), CRL (Candida rugosa lipase) and PCL (Pseudomonas cepacia lipase). The enzymatic resolution of racemic alcohol $({\pm})-2$ gave the excellent enantioselectivity in favor of (S)-2d in 99% ee, while those of the racemic alcohols (1, 3, 4, 5 and 6) gave the resolved alcohols with moderate to good enantioselectivity. Also, their absolute configurations were determined by chemical transformation to the known compounds.

• KSBB Journal
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• 제14권6호
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• pp.696-701
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• 1999

본 연구에서는 lipase를 이용해서 ricinoleic acid를 대량생산하기 위해 피마자유의 완전가수분해 조건을 찾고자 하였다. 널리 알려진 lipase CR, lipase CC, lipase PP를 대상으로 피마자유의 가수분해의 가능성을 시험하고, 유기용매를 사용함으로써 가수분해도를 향상시킬 수 있음을 확인하였다. 일반적으로 lipase의 활성을 감소시키는 극성용매의 경우 피마자유의 가수분해에 있어서도 효소의 활성을 감소시켰고, 물과 섞이지 않는 hydrophobic solvent가 피마자유의 가수분해도를 크게 증가시키는 것을 확인하였다. 본 연구에서는 isopropyl ether의 효과가 가장 크며, 조건에 따라 가수분해도를 두 배 이상 증가시킨다는 것을 확인하였다. 그리고 유기용매를 사용함으로써 pH의 영향을 바꾸거나 감소시킬 수 있다는 사실도 확인하였다. 용매와 물의 부피비에 의해서 가수분해가 영향을 받는다는 사실과 특히 유기용매보다는 물의 양에 절대적으로 영향받는다는 사실을 발견하였다. 하지만, 물과 유기용매의 부피비와 함께 lipase와 피마자유의 무게비도 매우 중요하다는 것을 확인하였다. 30$^{\circ}C$에서 isopropyl ether를 사용할 경우 무게 비로 2 wt%일 때는 약 82%, 4 wt% 이상의 lipase CC나 lipase CR을 사용하면 피마자유가 완전히 가수분해되는 사실을 발견하였다.

• Journal of Microbiology and Biotechnology
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• 제8권2호
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• pp.165-170
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• 1998

Lipase-catalyzed esterification of n-butyl oleate was carried out in n-hexane as a model reaction. The optimal activity of Candida rugosa lipase was shown in a water activity ($a_w$) range of 0.52 to 0.65 at $30^{\circ}C$. The water produced from the esterification was removed by a tubular type pervaporation system. The rate of ester formed from the enzymatic esterification was allowed to be the same as the rate of water removal by maintaining an optimal $a_w$ of the reaction system using an on-off dewatering control device. The reaction rate and yield with a$a_w$ control were increased two folds higher than the respective values for the uncontrolled reaction.

• 한국미생물·생명공학회지
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• 제24권2호
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• pp.213-216
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• 1996

Optically active carboxylic acid, D-(-)-$\beta$-hydroxyisobutyric acid {(D)-(-)-HIBA} is a useful chiral starting material for the preparation of enantiomerically pure bioactive compounds which have a chiral methyl carbon center in the molecule such as captopril, $\alpha$-tocopherol, erythromycin A, muscone and so on. (S)-3-Acetoxy-2-methylpropanol can be used as the precursor of (D)-(-)-HIBA, that is, chemical oxidation of the hydroxyl group and subsequent hydrolysis of acyl group in (S)-3-acetoxy-2-methylpropanol affords D-(-)-$\beta$-hydroxyisobutyric acid. (S)-3-Acetoxy-2-methyl-propanol was prepared by lipase-catalyzed asymmetric hydrolysis. In the enzymatic hydrolysis system, lipase AY (Candida rugosa) provided the expected (S)-3-acetoxy-2-methylpropanol in 60% e.e. of the enantiomeric purity under the phosphate buffer and organic co-solvent system.

• 한국신재생에너지학회:학술대회논문집
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• 한국신재생에너지학회 2010년도 춘계학술대회 초록집
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• pp.251.1-251.1
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• 2010

바이오디젤은 동식물성 기름과 메탄올의 트랜스에스테르화 반응에 의해 생산되는 지방산메틸에스테르(FAME, fatty acid methyl esters)로서, 트랜스에스테르화 공정에는 KOH, NaOH, $NaOCH_3$등의 균질계 화학촉매를 이용한 방법, 무촉매 공정인 초임계 메탄올 이용 방법, 그리고 효소촉매를 이용한 방법이 있다. 초임계 공정은 에너지 소비와 장치비가 커서 경제성이 떨어지는 것으로 보고되며 화학촉매 공정은 반응 효율이 높다는 장점을 가지고 있지만, 반응 및 정제단계가 복잡하고 정제과정에 폐수를 발생시키는 문제점을 가지고 있다. 고정화 효소를 사용하는 효소 공정은 에너지 비용의 절감, 후 처리 공정의 단순화, 고 순도의 글리세롤을 얻을 수 있는 장점이 있지만, 반응 속도가 느리고 효소 가격이 비싸다는 단점이 있어 현재까지 상업화되지 못하고 있다. 반응속도가 높고 재사용이 가능한 효소 촉매 공정 개발을 위해 본 연구에서는 Candida rugosa, Rizhopus oryzae 2종을 실리카에 동시 고정화하였다. 고정화 Lipase의 제조는 실리카겔을 과산화수소를 이용하여 전처리를 하고 Acetone과 3-APTES의 혼합용액을 첨가한 후 실리카겔과 (silanization)을 진행 하였다. 그리고 glutaraldehyde를 첨가 하여 공유 결합을 형성 한 후에 증류수를 사용하여 실리카겔을 회수하여 lipase(Rizhopus oryzae, Candida rugosa 10% 용액)를 고정화 하였다. 고정화 효소의 효소 활성을 측정한 결과 3000-3500 Unit(${\mu}mol/g{\cdot}min$)으로 측정되었다. 제조된 고정화 효소를 이용하여 Canola Oil을 바이오디젤로 전환하는 실험을 진행하였으며 생성물로부터 고정화 효소를 분리한 후에 상층의 에스테르층을 취하여 수세한 뒤 원심분리하여 FAME 함량을 측정한 결과 83%의 바이오디젤을 얻을 수 있었다. 그리고 효소 촉매 트랜스에스테르화 반응의 Enzyme, Water, Methanol 투입량의 반응 변수들에 대하여 반응표면분석법(Response Surface Methodology)을 적용하여 최적 반응조건을 도출하는 연구를 수행하였다.