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Volumn 131, Issue 4, 2012, Pages 1240-1247

Thermal and high hydrostatic pressure inactivation of myrosinase from green cabbage: A kinetic study

Author keywords

Brassica; Modelling; Myrosinase; Processing; Stability

Indexed keywords

BENEFICIAL EFFECTS; BRASSICA; BRASSICA SPECIES; COMBINED EFFECT; FIRST ORDER KINETICS; GLUCOSINOLATES; HIGH HYDROSTATIC PRESSURE; HIGH PRESSURE PROCESSING; HUMAN HEALTH; INACTIVATION KINETICS; KINETIC STUDY; MODELLING; MYROSINASE; TEMPERATURE RANGE; THERMAL INACTIVATION;

EID: 81855221954     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2011.09.111     Document Type: Article
Times cited : (57)

References (36)
  • 1
    • 0000295679 scopus 로고    scopus 로고
    • The myrosinase-glucosinolate system, its organisation and biochemistry
    • A.M. Bones, and J.T. Rossiter The myrosinase-glucosinolate system, its organisation and biochemistry Physiologia Plantarum 97 1 1996 194 208 (Pubitemid 126616896)
    • (1996) Physiologia Plantarum , vol.97 , Issue.1 , pp. 194-208
    • Bones, A.M.1    Rossiter, J.T.2
  • 2
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantification of micrograms quantities of protein utilizing principle of protein-dye binding
    • M.M. Bradford Rapid and sensitive method for quantification of micrograms quantities of protein utilizing principle of protein-dye binding Analytical Biochemistry 72 1-2 1976 248 254
    • (1976) Analytical Biochemistry , vol.72 , Issue.12 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0034671719 scopus 로고    scopus 로고
    • High resolution x-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base
    • DOI 10.1074/jbc.M006796200
    • W.P. Burmeister, S. Cottaz, P. Rollin, A. Vasella, and B. Henrissat High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base Journal of Biological Chemistry 275 50 2000 39385 39393 (Pubitemid 32058962)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 39385-39393
    • Burmeister, W.P.1    Cottaz, S.2    Rollin, P.3    Vasella, A.4    Henrissat, B.5
  • 4
    • 0031591140 scopus 로고    scopus 로고
    • Unifying the derivations for the Akaike and corrected Akaike information criteria
    • PII S0167715296001289
    • J.E. Cavanaugh Unifying the derivations for the Akaike and corrected Akaike information criteria Statistics and Probability Letters 33 2 1997 201 208 (Pubitemid 127162500)
    • (1997) Statistics and Probability Letters , vol.33 , Issue.2 , pp. 201-208
    • Cavanaugh, J.E.1
  • 5
    • 0031762786 scopus 로고    scopus 로고
    • Kinetic models for thermal inactivation of multiple pectinesterases in citrus juices
    • C.S. Chen, and M.C. Wu Kinetic models for thermal inactivation of multiple pectinesterases in citrus juices Journal of Food Science 63 5 1998 747 750 (Pubitemid 28494954)
    • (1998) Journal of Food Science , vol.63 , Issue.5 , pp. 747-750
    • Chen, C.S.1    Wu, M.C.2
  • 6
    • 0035559743 scopus 로고    scopus 로고
    • Erratum: Disposition of glucosinolates and sulforaphane in humans after ingestion of steamed and fresh broccoli (Nutrition and Cancer (2001) 38:2 (177))
    • C.C. Conaway, S.M. Getahun, L.L. Liebes, D.J. Pusateri, D.K.W. Topham, and M. Botero-Omary Disposition of glucosinolates and sulforaphane in humans after ingestion of steamed and fresh broccoli (Vol. 38, p. 177) Nutrition and Cancer-An International Journal 41 1-2 2001 196 (Pubitemid 34666241)
    • (2001) Nutrition and Cancer , vol.41 , Issue.1-2 , pp. 196
    • Conaway, C.C.1    Getahun, S.M.2    Liebes, L.L.3    Pusateri, D.J.4    Topham, D.K.W.5    Botero-Omary, M.6    Chung, F.-L.7
  • 7
    • 0035238964 scopus 로고    scopus 로고
    • Pungency levels of white radish (Raphanus sativus L.) grown in different seasons in Australia
    • R.C. Coogan, R.B.H. Wills, and V.Q. Nguyen Pungency levels of white radish (Raphanus sativus L.) grown in different seasons in Australia Food Chemistry 72 1 2001 1 3
    • (2001) Food Chemistry , vol.72 , Issue.1 , pp. 1-3
    • Coogan, R.C.1    Wills, R.B.H.2    Nguyen, V.Q.3
  • 8
    • 0043206318 scopus 로고    scopus 로고
    • Cancer modulation by glucosinolates: A review
    • S. Das, A.K. Tyagi, and H. Kaur Cancer modulation by glucosinolates: A review Current Science 79 12 2000 1665 1671
    • (2000) Current Science , vol.79 , Issue.12 , pp. 1665-1671
    • Das, S.1    Tyagi, A.K.2    Kaur, H.3
  • 10
    • 0030220832 scopus 로고    scopus 로고
    • Characteristics of a multicomponent first-order model for thermal inactivation of microorganisms and enzymes
    • DOI 10.1016/0168-1605(96)01004-5
    • H. Fujikawa, and T. Itoh Characteristics of a multicomponent first-order model for thermal inactivation of microorganisms and enzymes International Journal of Food Microbiology 31 1-3 1996 263 271 (Pubitemid 26297224)
    • (1996) International Journal of Food Microbiology , vol.31 , Issue.1-3 , pp. 263-271
    • Fujikawa, H.1    Itoh, T.2
  • 11
    • 0345398628 scopus 로고
    • A coupled enzymatic procedure for the determination of myrosinase activity
    • I.L. Gatfield, and T. Sand A coupled enzymatic procedure for the determination of myrosinase activity Lebensmittel-Wissenschaft and Technologie 16 2 1983 73 75
    • (1983) Lebensmittel-Wissenschaft and Technologie , vol.16 , Issue.2 , pp. 73-75
    • Gatfield, I.L.1    Sand, T.2
  • 12
    • 33745218882 scopus 로고    scopus 로고
    • Biology and biochemistry of glucosinolates
    • DOI 10.1146/annurev.arplant.57.032905.105228
    • B.A. Halkier, and J. Gershenzon Biology and biochemistry of glucosinolates Annual Review of Plant Biology 57 2006 303 333 (Pubitemid 44061027)
    • (2006) Annual Review of Plant Biology , vol.57 , pp. 303-333
    • Halkier, B.A.1    Gershenzon, J.2
  • 14
    • 0001622603 scopus 로고
    • Myrosinase is localized to the interior of myrosin grains and is not associated to the surrounding tonoplast membrane
    • A.S. Hoglund, M. Lenman, and L. Rask Myrosinase is localized to the interior of myrosin grains and is not associated to the surrounding tonoplast membrane Plant Science 85 2 1992 165 170
    • (1992) Plant Science , vol.85 , Issue.2 , pp. 165-170
    • Hoglund, A.S.1    Lenman, M.2    Rask, L.3
  • 15
    • 77955578408 scopus 로고    scopus 로고
    • Kinetic study of high pressure microbial and enzyme inactivation and selection of pasteurisation conditions for Valencia Orange Juice
    • G.I. Katsaros, M. Tsevdou, T. Panagiotou, and P.S. Taoukis Kinetic study of high pressure microbial and enzyme inactivation and selection of pasteurisation conditions for Valencia Orange Juice International Journal of Food Science and Technology 45 6 2010 1119 1129
    • (2010) International Journal of Food Science and Technology , vol.45 , Issue.6 , pp. 1119-1129
    • Katsaros, G.I.1    Tsevdou, M.2    Panagiotou, T.3    Taoukis, P.S.4
  • 17
    • 0032820274 scopus 로고    scopus 로고
    • Kinetic study of the irreversible thermal and pressure inactivation of myrosinase from broccoli (Brassica oleracea L. Cv. Italica)
    • DOI 10.1021/jf980964y
    • L. Ludikhuyze, V. Ooms, C. Weemaes, and M. Hendrickx Kinetic study of the irreversible thermal and pressure inactivation of myrosinase from broccoli (Brassica oleracea L-Cv. Italica) Journal of Agricultural and Food Chemistry 47 5 1999 1794 1800 (Pubitemid 29438719)
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.5 , pp. 1794-1800
    • Ludikhuyze, L.1    Ooms, V.2    Weemaes, C.3    Hendrickx, M.4
  • 18
    • 2942614968 scopus 로고    scopus 로고
    • Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli
    • DOI 10.1016/j.phytochem.2004.04.013, PII S0031942204001657
    • N.V. Matusheski, J.A. Juvik, and E.H. Jeffery Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli Phytochemistry 65 9 2004 1273 1281 (Pubitemid 38746674)
    • (2004) Phytochemistry , vol.65 , Issue.9 , pp. 1273-1281
    • Matusheski, N.V.1    Juvik, J.A.2    Jeffery, E.H.3
  • 19
    • 10144249599 scopus 로고    scopus 로고
    • Application of high hydrostatic pressure for increasing activity and stability of enzymes
    • DOI 10.1002/(SICI)1097-0290(19961020)52:2<320::AID-BIT12>3.0.CO;2-N
    • V.V. Mozhaev, R. Lange, E.V. Kudryashova, and C. Balny Application of high hydrostatic pressure for increasing activity and stability of enzymes Biotechnology and Bioengineering 52 2 1996 320 331 (Pubitemid 26317931)
    • (1996) Biotechnology and Bioengineering , vol.52 , Issue.2 , pp. 320-331
    • Mozhaev, V.V.1    Lange, R.2    Kudryashova, E.V.3    Balny, C.4
  • 20
    • 33846190151 scopus 로고    scopus 로고
    • High pressure-temperature effects on enzymatic activity: Naringin bioconversion
    • DOI 10.1016/j.foodchem.2006.05.033, PII S0308814606004262
    • H.J.V. Real, A.J. Alfaia, A.R.T. Calado, and M.H.L. Ribeiro High pressure-temperature effects on enzymatic activity: Naringin bioconversion Food Chemistry 102 3 2007 565 570 (Pubitemid 46108258)
    • (2007) Food Chemistry , vol.102 , Issue.3 , pp. 565-570
    • Vila Real, H.J.1    Alfaia, A.J.2    Calado, A.R.T.3    Ribeiro, M.H.L.4
  • 21
    • 0030745740 scopus 로고    scopus 로고
    • Fractional conversion for determining texture degradation kinetics of vegetables
    • A.F. Rizvi, and C.H. Tong A critical review - Fractional conversion for determining texture degradation kinetics of vegetables Journal of Food Science 62 1 1997 1 7 (Pubitemid 27295282)
    • (1997) Journal of Food Science , vol.62 , Issue.1 , pp. 1-7
    • Rizvi, A.F.1    Tong, C.H.2
  • 22
    • 4644282134 scopus 로고
    • Kinetic Study of the irreversible thermal deactivation of palmito (Acanthophoenix rubra) polyphenol oxidase and effect of pH
    • C.M. Robert, F.R. Cadet, C.C. Rouch, M. Pabion, and F. Richard-Forget Kinetic Study of the irreversible thermal deactivation of palmito (Acanthophoenix rubra) polyphenol oxidase and effect of pH Journal of Agricultural and Food Chemistry 43 5 1995 1143 1150
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , Issue.5 , pp. 1143-1150
    • Robert, C.M.1    Cadet, F.R.2    Rouch, C.C.3    Pabion, M.4    Richard-Forget, F.5
  • 24
    • 0000376495 scopus 로고    scopus 로고
    • Kinetic Modeling of Enzyme Inactivation: Kinetics of Heat Inactivation at 90-110 C of Extracellular Proteinase from Pseudomonas fluorescens 22F
    • E.P. Schokker, and M. van Boekel Kinetic modeling of enzyme inactivation: Kinetics of heat inactivation at 90-110 degrees C of extracellular proteinase from Pseudomonas fluorescens 22F Journal of Agricultural and Food Chemistry 45 12 1997 4740 4747 (Pubitemid 127485836)
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , Issue.12 , pp. 4740-4747
    • Schokker, E.P.1    Van Boekel, M.A.J.S.2
  • 26
    • 29244484265 scopus 로고    scopus 로고
    • Temperature and pressure stability of mustard seed (Sinapis alba L.) myrosinase
    • DOI 10.1016/j.foodchem.2005.03.046, PII S0308814605003341
    • D. Van Eylen, Indrawati, M. Hendrickx, and A. Van Loey Temperature and pressure stability of mustard seed (Sinapis alba L.) myrosinase Food Chemistry 97 2 2006 263 271 (Pubitemid 41828314)
    • (2006) Food Chemistry , vol.97 , Issue.2 , pp. 263-271
    • Van Eylen, D.1    Indrawati2    Hendrickx, M.3    Van Loey, A.4
  • 27
    • 34147097587 scopus 로고    scopus 로고
    • Kinetics of the stability of broccoli (Brassica oleracea Cv. Italica) myrosinase and isothiocyanates in broccoli juice during pressure/temperature treatments
    • DOI 10.1021/jf062630b
    • D. Van Eylen, I. Oey, M. Hendrickx, and A. Van Loey Kinetics of the stability of broccoli (Brassica oleracea cv. Italica) myrosinase and isothiocyanates in broccoli juice during pressure/temperature treatments Journal of Agricultural and Food Chemistry 55 6 2007 2163 2170 (Pubitemid 46556200)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.6 , pp. 2163-2170
    • Van Eylen, D.1    Oey, I.2    Hendrickx, M.3    Van Loey, A.4
  • 28
    • 38049113164 scopus 로고    scopus 로고
    • Behavior of mustard seed (Sinapis alba L.) myrosinase during temperature/pressure treatments: A case study on enzyme activity and stability
    • D. Van Eylen, I. Oey, M. Hendrickx, and A. Van Loey Behavior of mustard seed (Sinapis alba L.) myrosinase during temperature/pressure treatments: A case study on enzyme activity and stability European Food Research and Technology 226 3 2008 545 553
    • (2008) European Food Research and Technology , vol.226 , Issue.3 , pp. 545-553
    • Van Eylen, D.1    Oey, I.2    Hendrickx, M.3    Van Loey, A.4
  • 30
    • 9344240449 scopus 로고    scopus 로고
    • Glucosinolates and myrosinase activity in red cabbage (Brassica oleracea L. var. Capitata f. rubra DC.) after various microwave treatments
    • R. Verkerk, and M. Dekker Glucosinolates and myrosinase activity in red cabbage (Brassica oleracea L. var. Capitata f. rubra DC.) after various microwave treatments Journal of Agricultural and Food Chemistry 52 24 2004 7318 7323
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.24 , pp. 7318-7323
    • Verkerk, R.1    Dekker, M.2
  • 31
    • 0031835127 scopus 로고    scopus 로고
    • Induction of rat pancreatic glutathione S-transferase and quinone reductase activities by a mixture of glucosinolate breakdown derivatives found in brussels sprouts
    • M.A. Wallig, S. Kingston, R. Staack, and E.H. Jeffery Induction of rat pancreatic glutathione S-transferase and quinone reductase activities by a mixture of glucosinolate breakdown derivatives found in brussels sprouts Food and Chemical Toxicology 36 5 1998 265 373
    • (1998) Food and Chemical Toxicology , vol.36 , Issue.5 , pp. 265-373
    • Wallig, M.A.1    Kingston, S.2    Staack, R.3    Jeffery, E.H.4
  • 32
    • 34548224651 scopus 로고    scopus 로고
    • High pressure inactivation of lipoxygenase in soy milk and crude soybean extract
    • DOI 10.1016/j.foodchem.2007.06.056, PII S030881460700622X
    • R. Wang, X. Zhou, and Z.X. Chen High pressure inactivation of lipoxygenase in soy milk and crude soybean extract Food Chemistry 106 2 2008 603 611 (Pubitemid 47332873)
    • (2008) Food Chemistry , vol.106 , Issue.2 , pp. 603-611
    • Wang, R.1    Zhou, X.2    Chen, Z.3
  • 33
    • 0032487740 scopus 로고    scopus 로고
    • Kinetics of combined pressure-temperature inactivation of avocado polyphenoloxidase
    • DOI 10.1002/(SICI)1097-0290(19981105)60:3<292::AID-BIT4>3.0.CO;2-C
    • C.A. Weemaes, L.R. Ludikhuyze, I. Van den Broeck, and M.E. Hendrickx Kinetics of combined pressure-temperature inactivation of avocado polyphenoloxidase Biotechnology and Bioengineering 60 3 1998 292 300 (Pubitemid 28446889)
    • (1998) Biotechnology and Bioengineering , vol.60 , Issue.3 , pp. 292-300
    • Weemaes, C.A.1    Ludikhuyze, L.R.2    Van Den Broeck, I.3    Hendrickx, M.E.4
  • 34
    • 0021227229 scopus 로고
    • Determination of myrosinase (thioglucoside glucohydrolase) activity by a spectrophotometric coupled enzyme assay
    • A.P. Wilkinson, M.J.C. Rhodes, and G.R. Fenwick Determination of myrosinase (thioglucoside glucohydrolase) activity by a spectrophotometric coupled enzyme assay Analytical Biochemistry 139 2 1984 284 291 (Pubitemid 14079982)
    • (1984) Analytical Biochemistry , vol.139 , Issue.2 , pp. 284-291
    • Wilkinson, A.P.1    Rhodes, M.J.C.2    Fenwick, G.R.3
  • 35
    • 0036615409 scopus 로고    scopus 로고
    • Glucosinolate research in the Arabidopsis era
    • DOI 10.1016/S1360-1385(02)02273-2, PII S1360138502022732
    • U. Wittstock, and B.A. Halkier Glucosinolate research in the Arabidopsis era Trends in Plant Science 7 6 2002 263 270 (Pubitemid 36726529)
    • (2002) Trends in Plant Science , vol.7 , Issue.6 , pp. 263-270
    • Wittstock, U.1    Halkier, B.A.2
  • 36
    • 0001674517 scopus 로고
    • Myrosinase activity and total glucosinolates content of cruciferous vegetables, and some properties of cabbage myrosinase in Taiwan
    • G.C. Yen, and Q.K. Wei Myrosinase activity and total glucosinolates content of cruciferous vegetables, and some properties of cabbage myrosinase in Taiwan Journal of the Science of Food and Agriculture 61 4 1993 471 475
    • (1993) Journal of the Science of Food and Agriculture , vol.61 , Issue.4 , pp. 471-475
    • Yen, G.C.1    Wei, Q.K.2


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