• KSBB Journal
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• v.19 no.5
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• pp.385-389
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• 2004

In this research, the chemo-enzymatic synthesis of sorbitan methacrylate was investigated to optimize reaction conditions. Firstly, sorbitan was manufactured by sorbitol cyclic reaction in the presence of p-toluenesulfonic acid (p-TSA) as catalyst material. Secondly, sorbitan methacrylate was synthesized by immobilized lipase Novozyme 435 with acyl donors in t-butanol. As a result of enzymatic synthesis of sorbitan methacrylate, the conversion yield reached about $65\%$ in the condition of initial sorbitan conc. 50 g/L, enzyme content $3\%$ (w/v) , molar ratio 1:3, reaction temperature 50^{circ}C and reaction time 42 hrs using methyl methacrylate as acyl donor. Comparing with acyl donors and reaction temperature, the conversion yield reached about 18, 65 and $80\%$ with methacrylic acid, methyl methacrylate and vinyl methacrylate as acyl donor, respectively. And optimum reaction temperature was 60, 50, and 50^{circ}C, respectively

• Journal of the Korean Applied Science and Technology
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• v.35 no.4
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• pp.1048-1056
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• 2018

Non-edible oil sources (i.e., Palm Acid Oil, waste animal fat) usually contain relatively high amount of free fatty acids (FFA) that make them inadequate for direct base catalyzed transesterification reaction. Enzymatic biodiesel synthesis can solve several problems posed by the alkaline-catalyzed transesterification, and has certain advantages over the chemical catalysis of transesterification, as it is less energy intensive, allows easy recovery of glycerol and the transesterification of glycerides with high free fatty acid contents. In this study, we synthesized biodiesel through enzymatic catalyzed process using high free fatty acid containing waste oil in biodiesel reactor (1 ton/day) and optimized the biodiesel production processes.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1978.10a
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• pp.206.4-206
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• 1978

By utilizillg whole cell enzyme of the Xantho-monas citri IFO 3835, cephalexin is synthesized directly from 7-amino-deacetoxy cephalosporanic acid (7-ADCA) and phenyl glycine methyl ester (PGM). To date, cephalexin has been manufactu-red by chemical process involving fairly large number of steps to protect the amino group of phenly glycine and carboxyl group of 7-ADCA. However, the enzymatic process involves only a single step with 85％ conversion in 90 minutes. The fermentation variables studied indicate that oxygen transfer is limiting step in the enzyme production. Optimum conditions for enzymatic reaction were 37 C, pH 6.0, and the optimum substrate molar ratio of PGM to 7-ADCA was 2. Other variables that are related to the biochemical properties of whole cell enzyme temperature stability, pH stability, kinetic constants, reusing effect, enzyme loading effect were also evaluated.

• KSBB Journal
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• v.18 no.3
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• pp.222-228
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• 2003

This study was performed to research a chemo-enzymatic synthesis of sorbitan acrylate. It w as firstly to determine the optimum conditions for D-sorbitol cyclic reaction in the presence of p-toluenesulfonic acid (p-TSA) as catalyst material. It was secondly to find the optimum conditions for sorbitan acrylate synthesis using immobilized lipase Novozym 435 in t-butanol from its materials. The maximum yield of 1,4-sorbitan synthesis were obtained approximately 90% (w/w) at 13$0^{\circ}C$ and 200 mmHg vacuum pressure with 1% (w/w) p-TSA after 150 min reactin time on our experimental system. The product from optimum condition was less color than those obtained at higher temperatures and minimized byproduct and unreacted D-sorbitol. Sorbitan acrylate was synthesized to around 63.5% conversion of 1,4-sorbitan. The experimental optimum condition was found at 5$0^{\circ}C$, atmospheric pressure, 3% (w/v) Novozym 435, 50 g/L 1,4-sorbitan of initial reactant concentration, and 1:3 molar ratio of 1,4-sorbitan to acrylic acid.

• KSBB Journal
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• v.21 no.2
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• pp.118-122
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• 2006

In this report, we describe that the use of GroEL/GroES-enriched S30 extract remarkably enhances the solubility and enzymatic activity of cell-free synthesized rPA, which requires the correct formation of 9 disulfide bonds for its biological activity. We found that the stable maintenance of redox potential is necessary, but not sufficient for the optimal expression of active rPA. In a control reaction without using additional molecular chaperones, most of the rPA molecules were aggregated almost instantly after their expression and thus failed to exhibit the enzymatic activity. However, by the use of GroEL/GroES-enriched extract, combined with IAM-treatment, approximately $30{\mu}g/ml$ of active rPA was expressed in the cell-free synthesis reaction. This result not only demonstrates the efficient production of complex proteins, but also shows the control and flexibility offered by the cell-free protein synthesis system.

• BMB Reports
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• v.37 no.3
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• pp.339-342
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• 2004

Germination is a process which characterized with nescient synthesis of genes. Among the genes synthesized during the germination of wheat embryos, germin genes, proteins and their enzymatic activity were defined. Germin is a water soluble homopentameric glycoprotein which is remarkable resistant to degradation by a broad range of proteases including pepsin. Germin proteins found to have strong oxalate oxidase activity which produces hydrogen peroxide by degrading oxalic acid. The current study, aimed to localize the germin genes, proteins and enzymatic activities in developing coleoptiles which is a rapidly growing protective tissue of leaf primordium and shoot apex. Non-radioactively abeled germin riboprobes were employed to localize germin mRNAs in situ. FITC (Fluorescein isothiocyanate) and alkaline phosphatase linked anti-germin antibodies were used to localize germin proteins under the fluorescence and light microscopy and finally germin enzymatic activity was localized by using appropriate enzyme assay. The results revealed that in coleoptiles germin genes, proteins and their enzymatic activity were predominantly associated with the cells of epidermis and vascular bundle sheath cells.

• Proceedings of the Korean Aquaculture Society Conference
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• 2006.05a
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• pp.81-82
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• 2006

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.311-311
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• 2005

• 한국당과학회:학술대회논문집
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• 2006.11a
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• pp.9-10
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• 2006

• 한국당과학회:학술대회논문집
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• 2006.11a
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• pp.51-51
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• 2006