• KSBB Journal
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• v.23 no.6
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• pp.509-512
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• 2008

The hydrolysis reaction of soybean oil was conducted experimentally by various source enzymes. The analytical result of hydrolysate of soybean oil showed that the compositions were linoleic acid, olic acid, palmitic acid, and stearic acid in order. The enzymes CR-E and CC-E from Candida rufosa and Candida cylindracea had two hold or more hydrolysis conversions than those of Lipase 16, Novozyme 871, and Lipolase-100L under the same conditions. Therefore CR-E and CC-E were selected for further experiments. These two enzymes had similar ranges of optimun conditions as follows: pH 3-6, $35-45^{\circ}C$, and water to soybean oil ratio of 3.3 or above. They finally got conversions 95% above.

• Bulletin of the Korean Chemical Society
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• v.34 no.9
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• pp.2741-2746
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• 2013

The immobilization of enzyme is one of the key issues both in the field of enzymatic research and industrialization. In this work, we reported a facile method to immobilize Candida Antarctica lipase B (CALB) in alginate carrier. In the presence of calcium cation, the enzyme-alginate suspension could be cross-linked to form beads with porous structure at room temperature, and the enzyme CALB was dispersed in the beads. Activity of the enzyme-alginate composite was verified by enzymatic hydrolysis reaction of p-nitrophenol butyrate in aqueous phase. The effects of reaction parameters such as temperature, pH, embedding and lyophilized time on the reactive behavior were discussed. Reuse cycle experiments for the hydrolysis of p-nitrophenol butyrate demonstrated that activity of the enzyme-alginate composite was maintained without marked deactivation up to 6 repeated cycles.

• Journal of Microbiology and Biotechnology
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• v.26 no.9
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• pp.1579-1585
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• 2016

Sugar esters are valuable compounds composed of various sugars and fatty acids that can be used as antibacterial agents and emulsifiers in toothpaste and canned foods. For example, fructose fatty acid esters suppress growth of Streptococcus mutans, a typical pathogenic bacterium causing dental caries. In this study, fructose laurate ester was chosen as a target material and was synthesized by a transesterification reaction using Candida antarctica lipase B. We performed a solvent screening experiment and found that a t-butanol/dimethyl sulfoxide mixture was the best solvent to dissolve fructose and methyl laurate. Fructose laurate was synthesized by transesterification of fructose (100 mM) with methyl laurate (30 mM) in t-butanol containing 20% dimethyl sulfoxide. The conversion yield was about 90%, which was calculated based on the quantity of methyl laurate using high-performance liquid chromatography. Fructose monolaurate (M_r 361) was detected in the reaction mixture by high-resolution mass spectrometry. The inhibitory effect of fructose laurate on growth of oral or food spoilage microorganisms, including S. mutans, Bacillus coagulans, and Geobacillus stearothermophilus, was evaluated.

• Journal of Aquaculture
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• v.18 no.4
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• pp.245-251
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• 2005

This study was investigated the condition of their maximum activity to assay the enzymes of rotifer, Brachionus rotundiformis의 $\alpha$-amylase, total alkaline Protease, trypsin and TG-lipase activities of rotifer were higher and more sensitive in phosphate-NaOH buffer than Tris-HCl buffer. $\alpha$-amylase, trypsin and TG-lipase activities were appeared the maximum at pH 8.0, and total alkaline protease activity showed the maximum activity at pH 7.0. $\alpha$-amylase activity showed the highest activity at $40^{\circ}C$, and total alkaline protease and trypsin activities were assayed the highest at $55{\~}60^{\circ}C$. However, TG-lipase activity was appeared the highest at $25{\~}30^{\circ}C$. The optimum substrate concentration of enzyme activity of a-amylase, total alkaline protease, rypsin and TG-lipase were $3.5\%$ starch, $\0.6%$ azo-casein, $87.5{\mu}M$ BApNA and 81.2 mM olive oil, respectively. The optimum reaction time of enzyme activity of $\alpha$-amylase, total alkaline protease, trypsin and TG-lipase were increased up to 40, 60, 30 and 25 min., respectively. The data obtained in this study could be used for the digestive enzyme research of rotifer, B. rotundiformis.

• Biotechnology and Bioprocess Engineering:BBE
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• v.7 no.2
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• pp.76-84
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• 2002

On-line conversion estimation of enzymatic esterification reactions in solvent-free media was investigated. In principle, conversion to ester can be determined from the amount of water produced by the reaction, because water is formed as a by-product in a stoichiometric manner. In this study, we estimated the water production rate only from some measurements of relative humidity and water balances without using any analytical methods. In order to test the performance of the on-line conversion estimation, the lipase-catalyzed esterification of n-capric acid and n-decal alcohol in solvent-free media was performed whilst controlling water activity at various values. The reaction conversions estimated on-line were similar to those determined by offline gas chromatographic analysis. However, when the water activity was controlled at higher values, discrepancies between the estimated conversion values and the measured values became significant. The deviation was found to be due to the inaccurate measurement of the water content in the reaction medium during the initial stages of the reaction. Using a digital filter, we were able to improve the accuracy of the on-line conversion estimation method considerably. Despite the simplicity of this method, the on-line estimated conversions were in good agreement with the off-line measured values.

• Food Science and Preservation
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• v.20 no.2
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• pp.242-249
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• 2013

Thermal processing of (+)-catechin was carried out at $121^{\circ}C$ for different reaction times (1, 2, 3, 6, and 12 h). The reacted products, compounds (1) and (2), were isolated and quantified via HPLC analysis. The antioxidant properties of processed (+)-catechin and its isolated compounds for different reaction time was measured via radical scavenging assays using DPPH and $ABTS^+$ radicals. Additionally, the anti-obesity efficacy of the thermal treated (+)-catechin was evaluated via porcine pancreatic lipase assay. The reacted (+)-catechin for 3 h had a slightly higher antioxidant capacity than that the parent (+)-catechin. Products 1 and 2, which were isolated from the reacted mixture during 3 h, showed an antioxidant capacity, and these two compounds may be responsible for the antioxidant capacity of processed (+)-catechin. Simple thermal treatment of (+)-catechin can be used to produce (+)-epicatechin (1) and protocatechuic acid (2) with enhanced antioxidant and anti-adipogenic effects.

• Microbiology and Biotechnology Letters
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• v.37 no.4
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• pp.365-370
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• 2009

For the production of diglyceride (DG) containing medium chain fatty acid, which could be utilized as a substrate to structured lipid production, monoglyceride (MG) and caprylic acid were reacted in the presence of lipase. The reaction system was well mixed homogeneously without using any organic solvent. Among the lipases investigated, Lipozyme RM IM and Novozym 435 were selected on the basis of equilibrium DG yields from the medium chain fatty acid and MG. And reaction conditions such as addition of molecular sieve, water content of immobilized lipase, reaction temperature, and mole ratio of MG/caprylic acid are optimized to increase DG production by using Lipozyme RM IM. DG content of reaction mixture showed 8% increase by adding molecular sieve to reaction mixture. Removal of water from the immobilized lipase could affect seriously equilibrium content of DG. More than 2.8%(w/w) removal of water from the support could make 44% of DG. Optimum temperature was found to $60^{\circ}C$. Temperature shift from $60^{\circ}C$ to $25^{\circ}C$ resulted in increase of free fatty acid (FFA) content. The equilibrium DG yield was not seriously affected by on MG/caprylic acid molar ratio. However, at the stoichiometric ratio of 1:1 the highest DG yield was obtained. Increasing MG/caprylic acid ratio from 0.3 to 1.8 decreased FFA content from 34% to 13%, while MG content increased from 27% to 50%.

• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.8
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• pp.1200-1205
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• 2003

Structured lipids (SL) were synthesized by transesterification of corn oil and conjugated linoleic acid (CLA) in the continuous type reactor using sn-1,3 specific Rhizomucor miehei lipase. The parameters of reaction were observed in terms of flow rate, temperature, and substrate molar ratios. The highest incorporation of CLA was obtained with 1 mL/min flow rate, 55$^{\circ}C$ and 1 : 3 (corn oil/CLA) molar ratio, showing 10.26 ㏖%. When different reaction temperatures and substrate ratios were studied, the highest incorporation was obtained at $65^{\circ}C$ (17.33 ㏖%) and 1 : 5 (corn oil/CLA) ratio (17.50 ㏖%), respectively. After pancreatic lipase analysis, most of all CLA were found at sn-1,3 position. The iodine values of obtained SLs ranged from 110 to 120. From the neutral lipid analysis by normal-phase HPLC, produced SLs composed of 99.35 ∼ 99.89% triacylglycerols, 0.11 ∼ 0.51% 1,2- and 1,3-diacylglycerols, and 0.06 ∼ 0.22% monoacylglycerols.

• Microbiology and Biotechnology Letters
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• v.15 no.2
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• pp.98-103
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• 1987

Two phase reaction system was used to hydrolyze the olive oil for fat splitting. Kinetics of lipases in two phase system were investigated by determining the hydrolysis rate of triglycerides at various olive oil concentrations in isooctane using the microbial lipases from Candida rugosa and Rhizopus arrhizus. The rate equation in lipid hydrolysis for various olive oil concentrations in two phase system was deviated from the Michaelis-Menten kinetics. The results suggested that the olive oil concentration in isooctane affects the interfacial area. The dependency of the interfacial area on olive oil concentration is greater at the lower olive oil concentration than at the higher substrate concentration. We modified the rate equation by considering the interfacial area between two phases depending on the olive oil concentration in solvent phase.

• BMB Reports
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• v.30 no.1
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• pp.7-12
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• 1997

The kinetics of the interesterification of triolein and stearic acid catalyzed by immobilized Rhizopus delemar lipase were studied in a batch operation. In order to clarify the mechanisms of this reaction, three models are discussed under various conditions in terms of the ratio of triolein and stearic acid. The rate constants involved in the proposed model were determined by combining the numerical Gauss-elemination method, and the trial-and-error method so as to fit the calculated results with the experimental data. The accuracy of the obtained rate constants was confirmed after they were substituted for simultaneous differential equations and the equations simulated using an adaptive step-size Runge-Kutta method. Finally, the model which agrees with the calculated results and the experimental data was selected.