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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제21권 제11호
- 발행연도
- 2011.1
- 수록면
- 1,159 - 1,165 (7page)
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Biodiesel is methyl and ethyl esters of long-chain fatty acids produced from vegetable oils or animal fats. Lipase enzymes have occasionally been used for the production of this biofuel. Recently, biodiesel production using immobilized lipase has received increased attention.
Through enhanced stability and reusability, immobilized lipase can contribute to the reduction of the costs inherent to biodiesel production. In this study, methanol-tolerant lipase M37 from Photobacterium lipolyticum was immobilized using the cross-linked enzyme aggregate (CLEA) method.
Lipase M37 has a high lysine content (9.7%) in its protein sequence. Most lysine residues are located evenly over the surface of the protein, except for the lid structure region,which makes the CLEA preparation yield quite high (~93%). CLEA M37 evidences an optimal temperature of 30oC, and an optimal pH of 9-10. It was stable up to 50oC and in a pH range of 4.0-11.0. Both soluble M37 and CLEA M37 were stable in the presence of high concentrations of methanol, ethanol, 1-propanol, and n-butanol. That is, their activities were maintained at solvent concentrations above 10% (v/v). CLEA M37 could produce biodiesel from olive oil and alcohols such as methanol and ethanol. Additionally, CLEA M37 generated biodiesel via both 2-step methanol feeding procedures.
Considering its physical stability and reusability, CLEA M37 may potentially be used as a catalyst in organic synthesis, including the biodiesel production reaction.
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참고문헌 (21)
참고문헌 신청
Chena, J.-W / 2003 / Regeneration of immobilized Candida antarctica lipase for transesterification / J. Biosci. Bioeng 95 : 466 ~ 469
Cunha, A. G / 2008 / Immobilization of Yarrowia lipolytica lipase - a comparison of stability of physical adsorption and covalent attachment techniques / Appl. Biochem. Biote
Jaeger, K. E / 1999 / Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases / Annu. Rev. Microbiol 53 : 315 ~
Jaeger, K. E / 2002 / Lipases for biotechnology / Curr. Opin. Biotechnol 13 : 390 ~ 397
Jung, S.-K. / 2008 / Structural basis for the cold adaptation of psychrophilic M37 lipase from Photobacterium lipolyticum / PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 71
Cunha, A. G / 2008 / Immobilization of Yarrowia lipolytica lipase - a comparison of stability of physical adsorption and covalent attachment techniques / Appl. Biochem. Biote
Jaeger, K. E / 1999 / Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases / Annu. Rev. Microbiol 53 : 315 ~
Jaeger, K. E / 2002 / Lipases for biotechnology / Curr. Opin. Biotechnol 13 : 390 ~ 397
Jung, S.-K. / 2008 / Structural basis for the cold adaptation of psychrophilic M37 lipase from Photobacterium lipolyticum / PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 71
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