메뉴 건너뛰기




Volumn 59, Issue 10, 2011, Pages 5390-5395

Evaluation of the potential of fungal and plant laccases for active-packaging applications

Author keywords

Active packaging; Immobilization; Laccase; Myceliophthora thermophila; Rhus vernicifera; Trametes versicolor

Indexed keywords

ACTIVE PACKAGING; IMMOBILIZATION; LACCASE; MYCELIOPHTHORA THERMOPHILA; RHUS VERNICIFERA; TRAMETES VERSICOLOR;

EID: 79957958907     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf103811g     Document Type: Article
Times cited : (18)

References (19)
  • 1
    • 0030297516 scopus 로고    scopus 로고
    • Microbial and biochemical spoilage of foods: An overview
    • DOI 10.1016/0168-1605(96)01139-7
    • Huis in't Veld, J. H. J. Microbial and biochemical spoilage of foods: an overview. Int. J. Food Microbiol. 1996, 33, 1-18. (Pubitemid 26354172)
    • (1996) International Journal of Food Microbiology , vol.33 , Issue.1 , pp. 1-18
    • Huis In't Veld, J.H.J.1
  • 2
    • 0037471584 scopus 로고    scopus 로고
    • Lipid oxidation in herring fillets (Clupea harengus) during ice storage measured by a commercial hybrid gas-sensor array system
    • Haugen, J. E.; Undeland, I. Lipid oxidation in herring fillets (Clupea harengus) during ice storage measured by a commercial hybrid gas-sensor array system. J. Agric. Food Chem. 2003, 51, 752-759.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 752-759
    • Haugen, J.E.1    Undeland, I.2
  • 4
    • 47149106224 scopus 로고    scopus 로고
    • Enzyme immobilization in latex dispersion coatings for active food packaging
    • DOI 10.1002/pts.796
    • Nestorson, A.; Neoh, K. G.; Kang, E. T.; Jarnstrom, L.; Leufvén, A. Enzyme immobilization in latex dispersion coatings for active food packaging. Packag. Technol. Sci. 2008, 21, 193-205. (Pubitemid 351975882)
    • (2008) Packaging Technology and Science , vol.21 , Issue.4 , pp. 193-205
    • Nestorson, A.1    Neon, K.G.2    Kang, E.T.3    Jarnstrom, L.4    Leufven, A.5
  • 5
    • 44449174427 scopus 로고    scopus 로고
    • Diastereomer selectivity in the degradation of a lignin model compound of the arylglycerol β-aryl ether type by white-rot fungi
    • Bohlin, C; Lundquist, K.; Jonsson, L. J. Diastereomer selectivity in the degradation of a lignin model compound of the arylglycerol β-aryl ether type by white-rot fungi. Enzyme Microb. Technol. 2008, 43, 199-204.
    • (2008) Enzyme Microb. Technol. , vol.43 , pp. 199-204
    • Bohlin, C.1    Lundquist, K.2    Jonsson, L.J.3
  • 6
    • 0030838432 scopus 로고    scopus 로고
    • Characterization of the gene encoding an extracellular laccase of myceliophthora thermophila and analysis of the recombinant enzyme expressed in aspergillus oryzae
    • Berka, R. M.; Schneider, P.; Golightly, E J.; Brown, S. H.; Madden, M.; Brown, K. M.; Halkier, T.; Mondorf, K.; Xu, F. Characterization of the gene encoding an extracellular laccase of Myceliophthora thermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzae. Appl. Environ. Microbiol. 1997, 63, 3151-3157. (Pubitemid 27337808)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.8 , pp. 3151-3157
    • Berka, R.M.1    Schneider, P.2    Golightly, E.J.3    Brown, S.H.4    Madden, M.5    Brown, K.M.6    Halkier, T.7    Mondorf, K.8    Xu, F.9
  • 7
    • 0029370191 scopus 로고
    • Urushi (oriental lacquer) - A natural aesthetic durable and future-promising coating
    • Kumanotani, J. Urushi (oriental lacquer) - a natural aesthetic durable and future-promising coating. Prog. Org. Coat. 1995, 26, 163-195.
    • (1995) Prog. Org. Coat , vol.26 , pp. 163-195
    • Kumanotani, J.1
  • 8
    • 0027703684 scopus 로고
    • Immobilized enzymes - learning from past successes and failures
    • DOI 10.1016/0167-7799(93)90080-S
    • Katchalski-Katzir, E. Immobilized enzymes - learning from past successes and failures. Trends Biotechnol. 1993, 11, 471-478. (Pubitemid 23332969)
    • (1993) Trends in Biotechnology , vol.11 , Issue.11 , pp. 471-478
    • Katchalski-Katzir, E.1
  • 9
    • 0014935886 scopus 로고
    • Purification and properties of laccase and stellacyanin from Rhus vernicifera
    • Reinhammar, B. Purification and properties of laccase and stellacyanin from Rhus vernicifera. Biochim. Biophys. Acta 1970, 205, 35-47.
    • (1970) Biochim. Biophys. Acta , vol.205 , pp. 35-47
    • Reinhammar, B.1
  • 11
    • 33646871798 scopus 로고    scopus 로고
    • Oxidation capacity of laccases and peroxidases as reflected in experiments with methoxy-substituted benzyl alcohols
    • DOI 10.1385/ABAB:129:1:303
    • Hong, F.; Jonsson, L. J.; Lundquist, K.; Wei, Y. J. Oxidation capacity of laccases and peroxidases as reflected in experiments with methoxy-substituted benzyl alcohols. Appl. Biochem. Biotechnol. 2006, 129, 303-319. (Pubitemid 43787199)
    • (2006) Applied Biochemistry and Biotechnology , vol.129 , Issue.1-3 , pp. 303-319
    • Hong, F.1    Jonsson, L.J.2    Lundquist, K.3    Wei, Y.4
  • 12
    • 0015514062 scopus 로고
    • Oxidation-reduction potentials of electron acceptors in laccases and stellacyanin
    • Reinhammar, B. Oxidation-reduction potentials of electron acceptors in laccases and stellacyanin. Biochim. Biophys. Acta 1972, 275, 245-259.
    • (1972) Biochim. Biophys. Acta , vol.275 , pp. 245-259
    • Reinhammar, B.1
  • 13
    • 0030025889 scopus 로고    scopus 로고
    • A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability
    • DOI 10.1016/0167-4838(95)00210-3
    • Xu, F.; Shin, W. S.; Brown, S. H.; Wahleithner, J. A.; Sundaram, U. M.; Solomon, E. I. A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability. Biochim. Biophys. Acta-Protein Struct. Mol. Enzymol. 1996, 1292, 303-311. (Pubitemid 26071166)
    • (1996) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1292 , Issue.2 , pp. 303-311
    • Xu, F.1    Shin, W.2    Brown, S.H.3    Wahleithner, J.A.4    Sundaram, U.M.5    Solomon, E.I.6
  • 14
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • Feller, G.; Gerday, C. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 2003, 1, 200-208.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 17
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilization - Aqueous and non-aqueous environment
    • Iyer, P. V.; Ananthanarayan, L. Enzyme stability and stabilization - aqueous and non-aqueous environment. Process Biochem. 2008, 43, 1019-1032.
    • (2008) Process Biochem. , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 18
    • 15944415079 scopus 로고    scopus 로고
    • Octanol-water partition coefficient of glucose, sucrose, and trehalose
    • DOI 10.1016/j.carres.2004.12.038, PII S0008621505000960
    • Mazzobre, M. F.; Roman, M. V.; Mourelle, A. F.; Corti, H. R. Octanol-water partition coefficient of glucose, sucrose, and trehalose. Carbohydr. Res. 2005, 340, 1207-1211. (Pubitemid 40431800)
    • (2005) Carbohydrate Research , vol.340 , Issue.6 , pp. 1207-1211
    • Mazzobre, M.F.1    Roman, M.V.2    Mourelle, A.F.3    Corti, H.R.4
  • 19
    • 1642494890 scopus 로고    scopus 로고
    • Quantum-chemical modeling of the process of drug adsorption and the immobilization of phytocomponents in medicinal forms
    • DOI 10.1023/A:1026327826532
    • Pogrebnyak, A. V.; Stepanova, E. F. Quantum-chemical modeling of the process of drug adsorption and the immobilization of phytocomponents in medicinal forms. Pharm. Chem. J. 2003, 37, 374-378. (Pubitemid 38124441)
    • (2003) Pharmaceutical Chemistry Journal , vol.37 , Issue.7 , pp. 374-378
    • Pogrebnyak, A.V.1    Stepanova, E.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.