메뉴 건너뛰기




Volumn 105, Issue 10, 2003, Pages 608-613

Improvement of lipase stability in the presence of commercial triglycerides

Author keywords

Commercial triglycerides; Lipase; Low water systems; Stability; Triglyceride oxidation

Indexed keywords

4 HYDROXYNONENAL; ALBUMIN; ALDEHYDE; FUNCTIONAL GROUP; HYDROPEROXIDE; MALONALDEHYDE; NOVOZYME 435; OIL; POISON; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG; WATER;

EID: 0242266579     PISSN: 14387697     EISSN: None     Source Type: Journal    
DOI: 10.1002/ejlt.200300818     Document Type: Conference Paper
Times cited : (13)

References (24)
  • 1
    • 0039934889 scopus 로고
    • Biotechnology and the oleochemical industry
    • J. Casey, A. Macrae: Biotechnology and the oleochemical industry. INFORM 3 (1992) 203-207.
    • (1992) INFORM , vol.3 , pp. 203-207
    • Casey, J.1    Macrae, A.2
  • 2
    • 0031162606 scopus 로고    scopus 로고
    • Applications of lipase
    • N. N. Gandhi: Applications of lipase. J. Am. Oil Chem. Soc. 74 (1997) 621-633.
    • (1997) J. Am. Oil Chem. Soc. , vol.74 , pp. 621-633
    • Gandhi, N.N.1
  • 3
    • 0024655878 scopus 로고
    • Enzymatic catalysis in monophasic organic solvents
    • J. S. Dordick: Enzymatic catalysis in monophasic organic solvents. Enzyme Microb. Technol. 11 (1989) 194-211.
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 194-211
    • Dordick, J.S.1
  • 4
    • 0024278258 scopus 로고
    • Enzymatic catalysis in nonaqueous solvents
    • A. Zaks, A. M. Klibanov: Enzymatic catalysis in nonaqueous solvents. J. Biol. Chem. 263 (1988) 3194-3201.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2
  • 5
    • 0026517617 scopus 로고
    • Enzyme function in organic solvent
    • M. N. Gupta: Enzyme function in organic solvent. Eur. J. Biochem. 203 (1992) 25-32.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 25-32
    • Gupta, M.N.1
  • 6
    • 0024829242 scopus 로고
    • Tailored triglycerides and esters
    • A. R. Macrae: Tailored triglycerides and esters. Biochem. Soc. T. 17 (1989) 1146-1148.
    • (1989) Biochem. Soc. T. , vol.17 , pp. 1146-1148
    • Macrae, A.R.1
  • 7
    • 0027695471 scopus 로고
    • Enzymatic transesterification of rapeseed oil and lauric acids in a continuous reactor
    • P. Forssel, P. Parawori, P. Linko, K. Poutanen: Enzymatic transesterification of rapeseed oil and lauric acids in a continuous reactor. J. Am. Oil Chem. Soc. 70 (1993) 1105-1109.
    • (1993) J. Am. Oil Chem. Soc. , vol.70 , pp. 1105-1109
    • Forssel, P.1    Parawori, P.2    Linko, P.3    Poutanen, K.4
  • 8
    • 0028815168 scopus 로고
    • Continuous enantioselective transesterification in organic solvents. Use of suspended lipase preparations in a microfiltration membrane reactor
    • D. Indlekofer, M. Funke, W. Claasen, M. Reuss: Continuous enantioselective transesterification in organic solvents. Use of suspended lipase preparations in a microfiltration membrane reactor. Biotechnol. Progr. 11 (1995) 436-442.
    • (1995) Biotechnol. Progr. , vol.11 , pp. 436-442
    • Indlekofer, D.1    Funke, M.2    Claasen, W.3    Reuss, M.4
  • 9
    • 0028797444 scopus 로고
    • Development of a novel hollow-fibre membrane reactor for the interesterification of triglycerides and fatty acids using modified lipase
    • S. Basheer, K. Mogi, M. Naksima: Development of a novel hollow-fibre membrane reactor for the interesterification of triglycerides and fatty acids using modified lipase. Process Biochem. 30 (1995) 531-536.
    • (1995) Process Biochem. , vol.30 , pp. 531-536
    • Basheer, S.1    Mogi, K.2    Naksima, M.3
  • 10
    • 0031049670 scopus 로고    scopus 로고
    • Organic-phase enzymic esterification in a hollow- fiber membrane reactor with in situ gas-phase water activity control
    • Z. Ujang, N. Al-Sharbati, A. M. Vaidka: Organic-phase enzymic esterification in a hollow- fiber membrane reactor with in situ gas-phase water activity control. Biotechnol. Prog. 13 (1997) 39-42.
    • (1997) Biotechnol. Prog. , vol.13 , pp. 39-42
    • Ujang, Z.1    Al-Sharbati, N.2    Vaidka, A.M.3
  • 12
    • 0025323824 scopus 로고
    • Preparation and purification of soybean lipoxigenase-derived unsaturated hydroperoxy and hydroperoxyfatty acids and determination of molar absorbivities of hydroxy fatty acids
    • G. Graft, L. A. Anderson, L. W. Jaques: Preparation and purification of soybean lipoxigenase-derived unsaturated hydroperoxy and hydroperoxyfatty acids and determination of molar absorbivities of hydroxy fatty acids. Anal. Biochem. 188 (1990) 38-47.
    • (1990) Anal. Biochem. , vol.188 , pp. 38-47
    • Graft, G.1    Anderson, L.A.2    Jaques, L.W.3
  • 13
    • 0027257751 scopus 로고
    • A rapid screening test to determine the antioxidant potencies of natural and synthetic antioxidant
    • W. A. Pryor, J. A. Cornicelli, L. J. Devall, B. Tait, B. K. Trivedi, D. T. Vitiak, M. Wu: A rapid screening test to determine the antioxidant potencies of natural and synthetic antioxidant. J. Org. Biochem. 58 (1993) 3521-3532.
    • (1993) J. Org. Biochem. , vol.58 , pp. 3521-3532
    • Pryor, W.A.1    Cornicelli, J.A.2    Devall, L.J.3    Tait, B.4    Trivedi, B.K.5    Vitiak, D.T.6    Wu, M.7
  • 14
    • 0035819407 scopus 로고    scopus 로고
    • Development of small-size tubular-flow continuous reactors for the analysis of the operational stability of enzymes in low-water environments
    • D. Pirozzi, P. J. Halling: Development of small-size tubular-flow continuous reactors for the analysis of the operational stability of enzymes in low-water environments. Biotechnol. Bioeng. 72 (2001) 244-248.
    • (2001) Biotechnol. Bioeng. , vol.72 , pp. 244-248
    • Pirozzi, D.1    Halling, P.J.2
  • 17
    • 0021758483 scopus 로고
    • Cytotoxic aldehydes originating from the peroxidation of liver microsomial lipids. Identification of 4.5-dihydroxydecenal
    • A. Benedetti, M. Comporti, R. Fulceri, H. Esterbauer: Cytotoxic aldehydes originating from the peroxidation of liver microsomial lipids. Identification of 4.5-dihydroxydecenal. Biochim. Biophys. Acta. 792 (1984) 172-181.
    • (1984) Biochim. Biophys. Acta. , vol.792 , pp. 172-181
    • Benedetti, A.1    Comporti, M.2    Fulceri, R.3    Esterbauer, H.4
  • 18
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehydes and related aldehydes
    • H. Esterbauer, R. J. Schaur, H. Zollner: Chemistry and biochemistry of 4-hydroxynonenal, malonaldehydes and related aldehydes. Free Rad. Biol. Med. 11 (1991) 91-128.
    • (1991) Free Rad. Biol. Med. , vol.11 , pp. 91-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 19
    • 0027535124 scopus 로고
    • Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxynonenal. Selective modification of an active-site lysine
    • L. I. Szweda, K. Uchida, L. Tsai, E. R. Stadtman: Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxynonenal. Selective modification of an active-site lysine. J. Biol. Chem. 268 (1993) 3342-3347.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3342-3347
    • Szweda, L.I.1    Uchida, K.2    Tsai, L.3    Stadtman, E.R.4
  • 20
    • 0030181297 scopus 로고    scopus 로고
    • Determination of the sites of 4-hydroxy-2-nonenal adduction by electrospray tandem mass spectrometry
    • M. S. Bolgar, S. J. Gaskell: Determination of the sites of 4-hydroxy-2-nonenal adduction by electrospray tandem mass spectrometry. Anal. Chem. 68 (1996) 2325-2330.
    • (1996) Anal. Chem. , vol.68 , pp. 2325-2330
    • Bolgar, M.S.1    Gaskell, S.J.2
  • 21
    • 0029986692 scopus 로고    scopus 로고
    • Chemical characterization of a protein-4-hydroxy-2-nonenal cross-link:immunochemical detection in miochondria exposed to oxidative stress
    • J. A. Conn, L. Tsai, B. Friguet, L I. Szweda: Chemical characterization of a protein-4-hydroxy-2-nonenal cross-link:immunochemical detection in miochondria exposed to oxidative stress. Arch. Biochem. Biophys. 328 (1996) 158-164.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 158-164
    • Conn, J.A.1    Tsai, L.2    Friguet, B.3    Szweda, L.I.4
  • 22
    • 0031721684 scopus 로고    scopus 로고
    • Mass spectrometric analysis of 2′-deoxiribonucleoside and 2′-deoxiribonucleotide adducts with aldehydes derived from lipid peroxidation
    • D. R. Doerge, P. Yi, M. I. Churchwell, S. W. Preece, J. Langridge, P. P. Fu: Mass spectrometric analysis of 2′-deoxiribonucleoside and 2′-deoxiribonucleotide adducts with aldehydes derived from lipid peroxidation. Rapid Commun. Mass Spectrom. 12 (1998) 1665-1672.
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 1665-1672
    • Doerge, D.R.1    Yi, P.2    Churchwell, M.I.3    Preece, S.W.4    Langridge, J.5    Fu, P.P.6
  • 23
    • 0031772147 scopus 로고    scopus 로고
    • U-101033U (2.4-diaminopyrrolopyrimidine), a potent inhibitor of membrane lipid peroxidation as assessed by the production of 4-HNE, MDA, and 4-HNE-protein adducts
    • T. T. Rohn, L.K. Nelson, G. Waeg, M. T. Quinn: U-101033U (2.4-diaminopyrrolopyrimidine), a potent inhibitor of membrane lipid peroxidation as assessed by the production of 4-HNE, MDA, and 4-HNE-protein adducts. Biochem. Pharmacol. 56 (1998) 1371-1379.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 1371-1379
    • Rohn, T.T.1    Nelson, L.K.2    Waeg, G.3    Quinn, M.T.4
  • 24
    • 0035872342 scopus 로고    scopus 로고
    • Mechanism of action of Malodialdehyde and 4-Hydroxynonenal on Xanthine Oxidoreductase
    • G. Cighetti, L. Bortone, S. Sal, P. Allevi: Mechanism of action of Malodialdehyde and 4-Hydroxynonenal on Xanthine Oxidoreductase. Arch. Biochem. Biophys. 289(2) (2001) 195-200.
    • (2001) Arch. Biochem. Biophys. , vol.289 , Issue.2 , pp. 195-200
    • Cighetti, G.1    Bortone, L.2    Sal, S.3    Allevi, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.