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Volumn 58, Issue 5, 2010, Pages 3147-3152

Kinetic modeling of the thermal inactivation of bacteriocin-like inhibitory substance P34

Author keywords

Bacteriocin like inhibitory substance p34; Kinetic modeling; Thermal inactivation; Thermodynamic activation parameters

Indexed keywords

BACTERIOCIN;

EID: 77949363101     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf903626w     Document Type: Article
Times cited : (26)

References (49)
  • 1
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter, P. D.; Hill, C. Ross, R. P. Bacteriocins: Developing innate immunity for food. Nat. Rev. Microbiol. 2005, 3, 777-788.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 2
    • 0001389338 scopus 로고
    • Bacteriocins and food application
    • Eckner, K. Bacteriocins and food application. Dairy Food Environ. Sanit. 1992, 12, 204-209.
    • (1992) Dairy Food Environ. Sanit , vol.12 , pp. 204-209
    • Eckner, K.1
  • 4
    • 0036589165 scopus 로고    scopus 로고
    • Potential of bacteriocin-producing lactic acid bacteria for improvements in food safety and quality
    • O'Sullivan, L.; Ross, R. P.; Hill, C. Potential of bacteriocin-producing lactic acid bacteria for improvements in food safety and quality. Biochimie 2002, 84, 593-604.
    • (2002) Biochimie , vol.84 , pp. 593-604
    • O'Sullivan, L.1    Ross, R.P.2    Hill, C.3
  • 6
    • 1842587029 scopus 로고    scopus 로고
    • Bacteriocin-like substance production by Bacillus licheniformis strain P40
    • Cladera-Olivera, F.; Caron, G. R.; Brandelli, A. Bacteriocin-like substance production by Bacillus licheniformis strain P40. Lett. Appl. Microbiol. 2004, 38, 251-256.
    • (2004) Lett. Appl. Microbiol , vol.38 , pp. 251-256
    • Cladera-Olivera, F.1    Caron, G.R.2    Brandelli, A.3
  • 7
    • 24144459102 scopus 로고    scopus 로고
    • Purification and partial chemical characterization of the antimicrobial peptide cerein 8A
    • Bizani, D.; Dominguez, A. P. M.; Brandelli, A. Purification and partial chemical characterization of the antimicrobial peptide cerein 8A. Lett. Appl. Microbiol. 2005, 41, 269-273.
    • (2005) Lett. Appl. Microbiol , vol.41 , pp. 269-273
    • Bizani, D.1    Dominguez, A.P.M.2    Brandelli, A.3
  • 9
    • 34548689914 scopus 로고    scopus 로고
    • Characterization of a broad range antibacterial substance from a new Bacillus species isolated from Amazon basin
    • Motta, A. S.; Cannavan, F. S.; Tsai, S. M.; Brandelli, A. Characterization of a broad range antibacterial substance from a new Bacillus species isolated from Amazon basin. Arch. Microbiol. 2007, 188, 367-375.
    • (2007) Arch. Microbiol , vol.188 , pp. 367-375
    • Motta, A.S.1    Cannavan, F.S.2    Tsai, S.M.3    Brandelli, A.4
  • 10
    • 33646697752 scopus 로고    scopus 로고
    • Bacteriocins: Biological tools for bio-preservation and shelf-life extension
    • Deegan, L. H.; Cotter, P. D.; Hilla, C.; Ross, P. Bacteriocins: Biological tools for bio-preservation and shelf-life extension. Int. Dairy J. 2006, 16, 1058-1071.
    • (2006) Int. Dairy J , vol.16 , pp. 1058-1071
    • Deegan, L.H.1    Cotter, P.D.2    Hilla, C.3    Ross, P.4
  • 11
    • 0032544106 scopus 로고    scopus 로고
    • Effect of nisin on heath injury and inactivation of Salmonella enteritidis PT4
    • Boziaris, I. S.; Humpheson, L.; Adams, M. R. Effect of nisin on heath injury and inactivation of Salmonella enteritidis PT4. Int. J. Food Microbiol. 1998, 43, 7-13.
    • (1998) Int. J. Food Microbiol , vol.43 , pp. 7-13
    • Boziaris, I.S.1    Humpheson, L.2    Adams, M.R.3
  • 12
    • 49449115641 scopus 로고    scopus 로고
    • Combined effects of heat, nisin and acidification on the inactivation of Clostridium sporogenes spores in carrot-alginate particles: From kinetics to process validation
    • Naim, F.; Zareifard, M. R.; Zhu, S.; Huizing, R. H.; Grabowski, S.; Marcotte, M. Combined effects of heat, nisin and acidification on the inactivation of Clostridium sporogenes spores in carrot-alginate particles: From kinetics to process validation. Food Microbiol. 2008, 25, 936-941.
    • (2008) Food Microbiol , vol.25 , pp. 936-941
    • Naim, F.1    Zareifard, M.R.2    Zhu, S.3    Huizing, R.H.4    Grabowski, S.5    Marcotte, M.6
  • 13
    • 33847374664 scopus 로고    scopus 로고
    • Thermal processing and quality: Principles and overview
    • Awuah, G. B.; Ramaswamy, H. S.; Economides, A. Thermal processing and quality: Principles and overview. Chem. Eng. Process 2007, 46, 584-602.
    • (2007) Chem. Eng. Process , vol.46 , pp. 584-602
    • Awuah, G.B.1    Ramaswamy, H.S.2    Economides, A.3
  • 14
    • 0038540587 scopus 로고    scopus 로고
    • Comparative shelf life study and vitamin C loss kinetics in pateurised and high pressure processed reconstituted orange juice
    • Polydera, A. C.; Stoforos, N. G.; Taoukis, P. S. Comparative shelf life study and vitamin C loss kinetics in pateurised and high pressure processed reconstituted orange juice. J. Food Eng. 2003, 60, 21-29.
    • (2003) J. Food Eng , vol.60 , pp. 21-29
    • Polydera, A.C.1    Stoforos, N.G.2    Taoukis, P.S.3
  • 15
    • 38849117092 scopus 로고    scopus 로고
    • Kinetic modeling of food quality: A critical review
    • Van Boekel, M. A. J. S. Kinetic modeling of food quality: A critical review. Compr. Rev. Food Sci. Food Saf. 2008, 7, 144-158.
    • (2008) Compr. Rev. Food Sci. Food Saf , vol.7 , pp. 144-158
    • Van Boekel, M.A.J.S.1
  • 16
    • 1942440028 scopus 로고    scopus 로고
    • Ascorbic acid degradation kinetics in mushrooms in a high-temperature short-time process controlled by a thermoresistometer
    • Blasco, R.; Esteve, M. J.; Frígola, A.; Rodrigo, M. Ascorbic acid degradation kinetics in mushrooms in a high-temperature short-time process controlled by a thermoresistometer. Lebensm.-Wiss. Technol. 2004, 37, 171-175.
    • (2004) Lebensm.-Wiss. Technol , vol.37 , pp. 171-175
    • Blasco, R.1    Esteve, M.J.2    Frígola, A.3    Rodrigo, M.4
  • 17
    • 34648828896 scopus 로고    scopus 로고
    • Thermal inactivation kinetics of peroxidase in mint leaves
    • Shalini, G. R.; Shivhare, U. S.; Basu, S. Thermal inactivation kinetics of peroxidase in mint leaves. J. Food Eng. 2008, 55, 147-153.
    • (2008) J. Food Eng , vol.55 , pp. 147-153
    • Shalini, G.R.1    Shivhare, U.S.2    Basu, S.3
  • 18
    • 56349159059 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A
    • Lappe, R.; Cladera-Olivera, F.; Dominguez, A. P. M.; Brandelli, A. Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A. J. Food Eng. 2009, 91, 223-227.
    • (2009) J. Food Eng , vol.91 , pp. 223-227
    • Lappe, R.1    Cladera-Olivera, F.2    Dominguez, A.P.M.3    Brandelli, A.4
  • 19
    • 0036198888 scopus 로고    scopus 로고
    • Characterization of an antibacterial peptide produced by Brevibacterium linens
    • Motta, A. S.; Brandelli, A. Characterization of an antibacterial peptide produced by Brevibacterium linens. J. Appl. Microbiol. 2002, 92, 63-71.
    • (2002) J. Appl. Microbiol , vol.92 , pp. 63-71
    • Motta, A.S.1    Brandelli, A.2
  • 21
    • 0032820274 scopus 로고    scopus 로고
    • Kinetic study of the irreversible thermal and pressure inactivation of myrosinase from broccoli (Brassica oleracea L. Cv. Italica)
    • Ludikhuyze, L.; Ooms, V.; Weemaes, C.; Hendrickx, M. Kinetic study of the irreversible thermal and pressure inactivation of myrosinase from broccoli (Brassica oleracea L. Cv. Italica). J. Agric. Food Chem. 1999, 47, 1794-1800.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 1794-1800
    • Ludikhuyze, L.1    Ooms, V.2    Weemaes, C.3    Hendrickx, M.4
  • 22
    • 0031762786 scopus 로고    scopus 로고
    • Kinetic models for thermal inactivation of multiple pectinesterases in citrus juices
    • Chen, C. S.; Wu, M. C. Kinetic models for thermal inactivation of multiple pectinesterases in citrus juices. J. Food Sci. 1998, 63, 747-750.
    • (1998) J. Food Sci , vol.63 , pp. 747-750
    • Chen, C.S.1    Wu, M.C.2
  • 23
    • 0032487740 scopus 로고    scopus 로고
    • Kinetics of combined pressure-temperature inactivation of avocado polyphenol oxidase
    • Weemaes, C. A.; Ludikhuyze, L. R.; van den Broeck, I.; Hendrickx, M. Kinetics of combined pressure-temperature inactivation of avocado polyphenol oxidase. Biotechnol. Bioeng. 1998, 60, 292-300.
    • (1998) Biotechnol. Bioeng , vol.60 , pp. 292-300
    • Weemaes, C.A.1    Ludikhuyze, L.R.2    van den Broeck, I.3    Hendrickx, M.4
  • 24
    • 0030745740 scopus 로고    scopus 로고
    • Fractional conversion for determining texture degradation kinetics of vegetables
    • Rizvi, A. F.; Tong, C. H. Fractional conversion for determining texture degradation kinetics of vegetables. J. Food Sci. 1997, 62, 1-7.
    • (1997) J. Food Sci , vol.62 , pp. 1-7
    • Rizvi, A.F.1    Tong, C.H.2
  • 25
    • 84987266075 scopus 로고
    • A statistical distribution of wide applicability
    • Weibull, W. A statistical distribution of wide applicability. J. Appl. Mech. 1951, 18, 293-297.
    • (1951) J. Appl. Mech , vol.18 , pp. 293-297
    • Weibull, W.1
  • 26
    • 0034151467 scopus 로고    scopus 로고
    • Modeling microbial survival during exposure to a lethal agent with varying intensity
    • Peleg, M.; Penchina, C. M. Modeling microbial survival during exposure to a lethal agent with varying intensity. Crit. Rev. Food Sci. 2000, 40, 159-172.
    • (2000) Crit. Rev. Food Sci , vol.40 , pp. 159-172
    • Peleg, M.1    Penchina, C.M.2
  • 27
    • 1042267844 scopus 로고    scopus 로고
    • A model of non-isothermal degradation of nutrients, pigments and enzymes
    • Corradini, M. G.; Peleg, M. A model of non-isothermal degradation of nutrients, pigments and enzymes. J. Agric. Food Chem. 2004, 84, 217-226.
    • (2004) J. Agric. Food Chem , vol.84 , pp. 217-226
    • Corradini, M.G.1    Peleg, M.2
  • 28
    • 70349119250 scopus 로고
    • Regression and time series model selection in small samples
    • Hurvich, C. M.; Tsai, C. L. Regression and time series model selection in small samples. Biometrika 1989, 76, 297-307.
    • (1989) Biometrika , vol.76 , pp. 297-307
    • Hurvich, C.M.1    Tsai, C.L.2
  • 29
    • 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
    • Schokker, E. P.; Van Boekel, M. A. J. S. Kinetic modeling of enzyme inactivation: Kinetics of heat inactivation at 90-110 °C of extracellular proteinase from Pseudomonas fluorescens 22F. J. Agric. Food Chem. 1997, 45, 4740-4747.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 4740-4747
    • Schokker, E.P.1    Van Boekel, M.A.J.S.2
  • 30
    • 0033026871 scopus 로고    scopus 로고
    • Modeling of the inactivation kinetics of the trypsin inhibitors in soy flour
    • Van den Hout, R.; Meerdink, G.; van't Riet, K. Modeling of the inactivation kinetics of the trypsin inhibitors in soy flour. J. Sci. Food Agric. 1999, 79, 63-70.
    • (1999) J. Sci. Food Agric , vol.79 , pp. 63-70
    • Van den Hout, R.1    Meerdink, G.2    van't Riet, K.3
  • 31
    • 33947371280 scopus 로고    scopus 로고
    • Purification and partial characterization of an antibacterial peptide produced by a novel Bacillus sp. strain isolated from Amazon basin
    • Motta, A. S.; Lorenzini, D.; Brandelli, A. Purification and partial characterization of an antibacterial peptide produced by a novel Bacillus sp. strain isolated from Amazon basin. Curr. Microbiol. 2007, 54, 282-286.
    • (2007) Curr. Microbiol , vol.54 , pp. 282-286
    • Motta, A.S.1    Lorenzini, D.2    Brandelli, A.3
  • 32
    • 27744457653 scopus 로고    scopus 로고
    • Purification and characterization of two novel antimicrobial peptides subpeptin JM4-A and subpeptin JM4-B produced by Bacillus subtilis JM4
    • Wu, S.; Jia, S.; Sun, D.; Chen, M.; Chen, X.; Zhong, J.; Huan, L. Purification and characterization of two novel antimicrobial peptides subpeptin JM4-A and subpeptin JM4-B produced by Bacillus subtilis JM4. Curr. Microbiol. 2005, 51, 292-296.
    • (2005) Curr. Microbiol , vol.51 , pp. 292-296
    • Wu, S.1    Jia, S.2    Sun, D.3    Chen, M.4    Chen, X.5    Zhong, J.6    Huan, L.7
  • 33
    • 0032112460 scopus 로고    scopus 로고
    • Reinterpretation of microbial survival curves
    • Peleg, M.; Cole, M. B. Reinterpretation of microbial survival curves. Crit. Rev. Food Sci. 1998, 38, 353-380.
    • (1998) Crit. Rev. Food Sci , vol.38 , pp. 353-380
    • Peleg, M.1    Cole, M.B.2
  • 34
    • 0037170799 scopus 로고    scopus 로고
    • On the use of the Weibull model to describe thermal inactivation of microbial vegetative cells
    • van Boekel, M. A. J. S. On the use of the Weibull model to describe thermal inactivation of microbial vegetative cells. Int. J. Food Microbiol. 2002, 74, 139-159.
    • (2002) Int. J. Food Microbiol , vol.74 , pp. 139-159
    • van Boekel, M.A.J.S.1
  • 35
    • 0141813615 scopus 로고    scopus 로고
    • Modeling the survival of two soilborne pathogens under dry structural solarization
    • Shlevin, E.; Saguy, S.; Mahrer, Y.; Katan, J. Modeling the survival of two soilborne pathogens under dry structural solarization. Phytopathology 2003, 93, 1247-1253.
    • (2003) Phytopathology , vol.93 , pp. 1247-1253
    • Shlevin, E.1    Saguy, S.2    Mahrer, Y.3    Katan, J.4
  • 36
    • 35748960500 scopus 로고    scopus 로고
    • A Weibullian model for microbial injury and mortality
    • Corradini, M. G.; Peleg, M. A Weibullian model for microbial injury and mortality. Int. J. Food Microbiol. 2007, 119, 319-328.
    • (2007) Int. J. Food Microbiol , vol.119 , pp. 319-328
    • Corradini, M.G.1    Peleg, M.2
  • 38
    • 0042866215 scopus 로고    scopus 로고
    • Studies on pH and thermal inactivation of pectolytic enzymes from Aspergillus niger
    • Naidu, G. S. N.; Panda, T. Studies on pH and thermal inactivation of pectolytic enzymes from Aspergillus niger. Biochem. Eng. J. 2003, 16, 57-67.
    • (2003) Biochem. Eng. J , vol.16 , pp. 57-67
    • Naidu, G.S.N.1    Panda, T.2
  • 39
    • 3042825076 scopus 로고    scopus 로고
    • Kinetic properties and thermal behavior of polygalacturonase used in fruit juice clarification
    • Ortega, N.; de Diego, S.; Perez-Mateos, M.; Busto, M. D. Kinetic properties and thermal behavior of polygalacturonase used in fruit juice clarification. Food Chem. 2004, 88, 209-217.
    • (2004) Food Chem , vol.88 , pp. 209-217
    • Ortega, N.1    de Diego, S.2    Perez-Mateos, M.3    Busto, M.D.4
  • 40
    • 0032940179 scopus 로고    scopus 로고
    • Kinetic study on thermal denaturation of hen involving precipitation egg-white lysozyme
    • Nohara, D.; Mizutani, A.; Sakai, T. Kinetic study on thermal denaturation of hen involving precipitation egg-white lysozyme. J. Biosci. Bioeng. 1999, 87, 199-205.
    • (1999) J. Biosci. Bioeng , vol.87 , pp. 199-205
    • Nohara, D.1    Mizutani, A.2    Sakai, T.3
  • 41
    • 84988119548 scopus 로고
    • Review: Enzyme inactivation during heat processing of food-stuffs
    • Adams, J. B. Review: Enzyme inactivation during heat processing of food-stuffs. Int. J. Food Sci. Technol. 1991, 26, 1-20.
    • (1991) Int. J. Food Sci. Technol , vol.26 , pp. 1-20
    • Adams, J.B.1
  • 42
    • 0032536139 scopus 로고    scopus 로고
    • Glycosylation and thermodynamic versus kinetic stability of horseradish peroxidase
    • Tams, J. W.; Welinder, K. G. Glycosylation and thermodynamic versus kinetic stability of horseradish peroxidase. FEBS Lett. 1998, 421, 234-236.
    • (1998) FEBS Lett , vol.421 , pp. 234-236
    • Tams, J.W.1    Welinder, K.G.2
  • 43
    • 17144409025 scopus 로고    scopus 로고
    • Heat inactivation and reactivation of broccoli peroxidase
    • Thongsook, T.; Barrett, D. M. Heat inactivation and reactivation of broccoli peroxidase. J. Agric. Food Chem. 2005, 53, 3215-3222.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 3215-3222
    • Thongsook, T.1    Barrett, D.M.2
  • 44
    • 84981851649 scopus 로고
    • Kinetics and energetics of thermal inactivation and the regeneration rates of a peroxidase system
    • Joffe, F. M.; Ball, C. O. Kinetics and energetics of thermal inactivation and the regeneration rates of a peroxidase system. J. Food Sci. 1962, 27, 587-592.
    • (1962) J. Food Sci , vol.27 , pp. 587-592
    • Joffe, F.M.1    Ball, C.O.2
  • 45
    • 43649106338 scopus 로고    scopus 로고
    • Kinetic study of the thermal inactivation of Cholinesterase enzymes immobilized in solid matrices
    • Bromberg, A.; Marx, S.; Frishman, G. Kinetic study of the thermal inactivation of Cholinesterase enzymes immobilized in solid matrices. Biochim. Biophys. Acta 2008, 1784, 961-966.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 961-966
    • Bromberg, A.1    Marx, S.2    Frishman, G.3
  • 46
    • 0003125897 scopus 로고
    • Experimental procedures for determining destruction kinetics of food components
    • Lenz, M. K.; Lund, D. B. Experimental procedures for determining destruction kinetics of food components. Food Technol. 1980, 34, 51-55.
    • (1980) Food Technol , vol.34 , pp. 51-55
    • Lenz, M.K.1    Lund, D.B.2
  • 47
    • 0029823108 scopus 로고    scopus 로고
    • Statistical aspects of kinetic modeling for food science problems
    • Van Boekel, M. A. J. S. Statistical aspects of kinetic modeling for food science problems. J. Food Sci. 1996, 61, 477-485.
    • (1996) J. Food Sci , vol.61 , pp. 477-485
    • Van Boekel, M.A.J.S.1
  • 49
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy, W.; Takase, M.; Wakabayashi, H.; Kawase, K.; Tomita, M. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J. Appl. Bacteriol. 1992, 73, 472-479.
    • (1992) J. Appl. Bacteriol , vol.73 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, M.5


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