메뉴 건너뛰기




Volumn 28, Issue 2, 2012, Pages 372-381

Comparison of several mathematical models for describing the joint effect of temperature and ph on glucanex activity

Author keywords

Curdlan; Enzymatic activity; Glucanex; Laminarin; Mathematical modeling; PH and temperature effects

Indexed keywords

CURDLAN; ENZYMATIC ACTIVITIES; GLUCANEX; LAMINARINS; MATHEMATICAL MODELING;

EID: 84859642762     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.733     Document Type: Article
Times cited : (23)

References (48)
  • 1
    • 0027396605 scopus 로고
    • Characterization of microbial biomasses and amylolytic preparations obtained from mussel processing waste treatment
    • Murado MA, Siso MIG, Gonzalez MP, Montemayor MI, Pastrana L, Pintado J. Characterization of microbial biomasses and amylolytic preparations obtained from mussel processing waste treatment. Bioresour Technol. 1993; 43: 117-125.
    • (1993) Bioresour Technol. , vol.43 , pp. 117-125
    • Murado, M.A.1    Siso, M.I.G.2    Gonzalez, M.P.3    Montemayor, M.I.4    Pastrana, L.5    Pintado, J.6
  • 2
    • 0030630823 scopus 로고    scopus 로고
    • Enzymatic transformation of sinapine using polyphenol oxidase from Trametes versicolor. Effect of pH and temperature and model development
    • Lacki K, Duvnjak Z. Enzymatic transformation of sinapine using polyphenol oxidase from Trametes versicolor. Effect of pH and temperature and model development. Chem Eng J. 1997; 65: 27-36.
    • (1997) Chem Eng J. , vol.65 , pp. 27-36
    • Lacki, K.1    Duvnjak, Z.2
  • 3
    • 0035809040 scopus 로고    scopus 로고
    • Modeling the effect of temperature and pH on activity of enzymes: the case of phytases
    • Tijskens LMM, Greiner R, Biekman ESA, Konietzny U. Modeling the effect of temperature and pH on activity of enzymes: the case of phytases. Biotechnol Bioeng. 2001; 72: 323-330.
    • (2001) Biotechnol Bioeng. , vol.72 , pp. 323-330
    • Tijskens, L.M.M.1    Greiner, R.2    Biekman, E.S.A.3    Konietzny, U.4
  • 5
    • 0017360586 scopus 로고
    • Reaction kinetics of poikilotherm development
    • Sharpe PJH and DeMichele DW. Reaction kinetics of poikilotherm development. J Theor Biol. 1977; 64: 649-670.
    • (1977) J Theor Biol. , vol.64 , pp. 649-670
    • Sharpe, P.J.H.1    DeMichele, D.W.2
  • 6
    • 0019508156 scopus 로고
    • Non-linear regression of biological temperature-dependent rate models based on absolute reaction-rate theory
    • Schoolfield RM, Sharpe PJH, Magnuson CE. Non-linear regression of biological temperature-dependent rate models based on absolute reaction-rate theory. J Theor Biol. 1981; 88: 719-731.
    • (1981) J Theor Biol. , vol.88 , pp. 719-731
    • Schoolfield, R.M.1    Sharpe, P.J.H.2    Magnuson, C.E.3
  • 7
    • 0020534991 scopus 로고
    • Model for bacterial culture growth rate throughout the entire biokinetic temperature range
    • Ratkowsky DA, Lowry RK, McMeekin TA, Stokes AN, Chandler RE. Model for bacterial culture growth rate throughout the entire biokinetic temperature range. J Bacteriol. 1983; 154: 1222-1226.
    • (1983) J Bacteriol. , vol.154 , pp. 1222-1226
    • Ratkowsky, D.A.1    Lowry, R.K.2    McMeekin, T.A.3    Stokes, A.N.4    Chandler, R.E.5
  • 8
    • 0020041977 scopus 로고
    • Relationship between temperature and growth rate of bacterial cultures
    • Ratkowsky DA, Olley J, McMeekin TA, Ball A. Relationship between temperature and growth rate of bacterial cultures. J Bacteriol. 1982; 149: 1-5.
    • (1982) J Bacteriol. , vol.149 , pp. 1-5
    • Ratkowsky, D.A.1    Olley, J.2    McMeekin, T.A.3    Ball, A.4
  • 9
    • 0026832995 scopus 로고
    • Parameters influencing hydrolysis kinetics of lipase in a hydrophilic membrane bioreactor
    • Pronk W, Boswinkel G, van't Riet K. Parameters influencing hydrolysis kinetics of lipase in a hydrophilic membrane bioreactor. Enzyme Microb Technol. 1992; 14: 214-220.
    • (1992) Enzyme Microb Technol. , vol.14 , pp. 214-220
    • Pronk, W.1    Boswinkel, G.2    van't Riet, K.3
  • 11
    • 64649105892 scopus 로고    scopus 로고
    • Mathematical modeling of growth of Salmonella in raw ground beef under isothermal conditions from 10 to 45°C
    • Juneja VK, Melendres MV, Huang L, Subbiah J, Thippareddi H. Mathematical modeling of growth of Salmonella in raw ground beef under isothermal conditions from 10 to 45°C. Int J Food Microbiol. 2009; 131: 106-111.
    • (2009) Int J Food Microbiol. , vol.131 , pp. 106-111
    • Juneja, V.K.1    Melendres, M.V.2    Huang, L.3    Subbiah, J.4    Thippareddi, H.5
  • 14
    • 0344234323 scopus 로고    scopus 로고
    • Kinetic models of activity for β-galactosidases: influence of pH, ionic concentration and temperature
    • Jurado E, Camacho F, Luzón G, Vicaria JM. Kinetic models of activity for β-galactosidases: influence of pH, ionic concentration and temperature. Enzyme Microb Technol. 2004; 34: 33-40.
    • (2004) Enzyme Microb Technol. , vol.34 , pp. 33-40
    • Jurado, E.1    Camacho, F.2    Luzón, G.3    Vicaria, J.M.4
  • 15
    • 73249120582 scopus 로고    scopus 로고
    • Carrot (Daucus carota L.) peroxidase inactivation, phenolic content and physical changes kinetics due to blanching
    • Gonçalves EM, Pinheiro J, Abreu M, Brandão TRS, Silva CLM. Carrot (Daucus carota L.) peroxidase inactivation, phenolic content and physical changes kinetics due to blanching. J Food Eng. 2010; 97: 574-581.
    • (2010) J Food Eng. , vol.97 , pp. 574-581
    • Gonçalves, E.M.1    Pinheiro, J.2    Abreu, M.3    Brandão, T.R.S.4    Silva, C.L.M.5
  • 16
    • 71849086788 scopus 로고    scopus 로고
    • Optimization of inulin hydrolysis by inulinase accounting for enzyme time- and temperature-dependent deactivation
    • Ricca E, Calabrò V, Curcio S, Iorio G. Optimization of inulin hydrolysis by inulinase accounting for enzyme time- and temperature-dependent deactivation. Biochem Eng J. 2009; 48: 81-86.
    • (2009) Biochem Eng J. , vol.48 , pp. 81-86
    • Ricca, E.1    Calabrò, V.2    Curcio, S.3    Iorio, G.4
  • 17
    • 35548956418 scopus 로고    scopus 로고
    • Kinetic characterisation and thermal inactivation study of partially purified red pepper (Capsicum annuum L.) peroxidase
    • Serrano-Martínez A, Fortea MI, del Amor FM, Núñez-Delicado E. Kinetic characterisation and thermal inactivation study of partially purified red pepper (Capsicum annuum L.) peroxidase. Food Chem. 2008; 107: 193-199.
    • (2008) Food Chem. , vol.107 , pp. 193-199
    • Serrano-Martínez, A.1    Fortea, M.I.2    del Amor, F.M.3    Núñez-Delicado, E.4
  • 18
    • 9944250922 scopus 로고    scopus 로고
    • Activities, stabilities, and reaction kinetics of three free and chitosan-clay composite immobilized enzymes
    • Chang MY, Juang RS. Activities, stabilities, and reaction kinetics of three free and chitosan-clay composite immobilized enzymes. Enzyme Microb Technol. 2005; 36: 75-82.
    • (2005) Enzyme Microb Technol. , vol.36 , pp. 75-82
    • Chang, M.Y.1    Juang, R.S.2
  • 19
    • 0037298581 scopus 로고    scopus 로고
    • Safety evaluation of a glucanase preparation intended for use in food inluding a subchronic study in rats and mutagenicity studies
    • Elvig SG, Pedersen PB. Safety evaluation of a glucanase preparation intended for use in food inluding a subchronic study in rats and mutagenicity studies. Regul Toxicol Pharm. 2003; 37: 11-19.
    • (2003) Regul Toxicol Pharm. , vol.37 , pp. 11-19
    • Elvig, S.G.1    Pedersen, P.B.2
  • 20
    • 33646771372 scopus 로고    scopus 로고
    • Production of soluble β-glucan from the cell wall of Saccharomyces cerevisiae
    • Kim KS, Yun HS. Production of soluble β-glucan from the cell wall of Saccharomyces cerevisiae. Enzyme Microb Technol. 2006; 39: 496-500.
    • (2006) Enzyme Microb Technol. , vol.39 , pp. 496-500
    • Kim, K.S.1    Yun, H.S.2
  • 21
    • 35548947556 scopus 로고    scopus 로고
    • Protein haze formation in white wines: effect of Saccharomyces cerevisiae cell wall components prepared with different procedures
    • Lomolino G, Curioni A. Protein haze formation in white wines: effect of Saccharomyces cerevisiae cell wall components prepared with different procedures. J Agric Food Chem. 2007; 55: 8737-8744.
    • (2007) J Agric Food Chem. , vol.55 , pp. 8737-8744
    • Lomolino, G.1    Curioni, A.2
  • 22
    • 74249118903 scopus 로고    scopus 로고
    • Martínez M, Vallés S, Manzanares P. β-Glucanases as a tool for the control of wine spoilage yeasts
    • Enrique M, Ibáñez A, Marcos JF, Yuste M, Martínez M, Vallés S, Manzanares P. β-Glucanases as a tool for the control of wine spoilage yeasts. J Food Sci. 2010; 75: 1253-1269.
    • (2010) J Food Sci. , vol.75 , pp. 1253-1269
    • Enrique, M.1    Ibáñez, A.2    Marcos, J.F.3    Yuste, M.4
  • 24
    • 78651031122 scopus 로고
    • Enzymes of starch degradation and synthesis
    • Bernfeld P. Enzymes of starch degradation and synthesis. Adv Enzymol. 1951; 12: 379-427.
    • (1951) Adv Enzymol. , vol.12 , pp. 379-427
    • Bernfeld, P.1
  • 25
    • 38249030137 scopus 로고
    • Statistical model selection criteria
    • Yi G, Judge G. Statistical model selection criteria. Econ Lett. 1988; 28: 47-51.
    • (1988) Econ Lett. , vol.28 , pp. 47-51
    • Yi, G.1    Judge, G.2
  • 26
    • 0036012998 scopus 로고    scopus 로고
    • Regression model selection: a residual likelihood approach
    • Shi P, Tsai C. Regression model selection: a residual likelihood approach. J R Stat Soc. 2002; 64: 237-252.
    • (2002) J R Stat Soc. , vol.64 , pp. 237-252
    • Shi, P.1    Tsai, C.2
  • 27
    • 0000120766 scopus 로고
    • Estimating the dimension of a model
    • Schwarz G. Estimating the dimension of a model. Annal Stat. 1978; 6: 461-464.
    • (1978) Annal Stat. , vol.6 , pp. 461-464
    • Schwarz, G.1
  • 28
    • 1642464789 scopus 로고    scopus 로고
    • Model comparison methods
    • In: Ludwig B, Michael LJ, editor. New York: Academic Press
    • Myung JI, Pitt MA. Model comparison methods. In: Ludwig B, Michael LJ, editor. Methods in Enzymology. New York: Academic Press; 2004: 351-366.
    • (2004) Methods in Enzymology. , pp. 351-366
    • Myung, J.I.1    Pitt, M.A.2
  • 29
    • 0000131403 scopus 로고    scopus 로고
    • Cross-validation methods
    • Browne MW. Cross-validation methods. J Math Psychol. 2000; 44: 108-132.
    • (2000) J Math Psychol. , vol.44 , pp. 108-132
    • Browne, M.W.1
  • 30
    • 0011529125 scopus 로고
    • Cross-validation and information criteria in causal modeling
    • Homburg C. Cross-validation and information criteria in causal modeling. J Market Res. 1991; 28: 137-144.
    • (1991) J Market Res. , vol.28 , pp. 137-144
    • Homburg, C.1
  • 31
    • 34547852206 scopus 로고    scopus 로고
    • Wilcox CV: an R package for fast variable selection in cross-validation
    • Boulesteix A. Wilcox CV: an R package for fast variable selection in cross-validation. Bioinformatics. 2007; 23: 1702-1704.
    • (2007) Bioinformatics. , vol.23 , pp. 1702-1704
    • Boulesteix, A.1
  • 32
    • 0031000325 scopus 로고    scopus 로고
    • pH and thermal stability studies of chitinase from Trichoderma harzianum: a thermodynamic consideration
    • Kapat A, Panda T. pH and thermal stability studies of chitinase from Trichoderma harzianum: a thermodynamic consideration. Bioprocess Eng. 1997; 16: 269-272.
    • (1997) Bioprocess Eng. , vol.16 , pp. 269-272
    • Kapat, A.1    Panda, T.2
  • 33
    • 9144229563 scopus 로고    scopus 로고
    • Stability and kinetics of β-1,3-glucanse from Trichoderma harzianum
    • Rana DS, Thèodore K, Naidu GSN, Panda T. Stability and kinetics of β-1, 3-glucanse from Trichoderma harzianum. Proc Biochem. 2003; 39: 149-155.
    • (2003) Proc Biochem. , vol.39 , pp. 149-155
    • Rana, D.S.1    Thèodore, K.2    Naidu, G.S.N.3    Panda, T.4
  • 36
    • 0016606406 scopus 로고
    • Solid substrate fermentor for ochratoxin A production
    • Lindenfelser LA, Ciegler A. Solid substrate fermentor for ochratoxin A production. Appl Microbiol. 1975; 29: 323-327.
    • (1975) Appl Microbiol. , vol.29 , pp. 323-327
    • Lindenfelser, L.A.1    Ciegler, A.2
  • 37
    • 0003164193 scopus 로고
    • Rate of degradation of nucleotides in cool-stored carp muscle
    • Ohta F, Hirabara T. Rate of degradation of nucleotides in cool-stored carp muscle. Memo Fac Fish Kagoshima Univ. 1977; 26: 97-102.
    • (1977) Memo Fac Fish Kagoshima Univ. , vol.26 , pp. 97-102
    • Ohta, F.1    Hirabara, T.2
  • 38
    • 0028982324 scopus 로고
    • Convenient model to describe the combined effects of temperature and pH on microbial growth
    • Rosso L, Lobry JR, Bajard S, Flandrois JP. Convenient model to describe the combined effects of temperature and pH on microbial growth. Appl Environ Microbiol. 1995; 61: 610-616.
    • (1995) Appl Environ Microbiol. , vol.61 , pp. 610-616
    • Rosso, L.1    Lobry, J.R.2    Bajard, S.3    Flandrois, J.P.4
  • 39
    • 0037009176 scopus 로고    scopus 로고
    • Dose-response relationships: an overview, a generative model and its application to the verification of descriptive models
    • Murado MA, González MP, Vázquez JA. Dose-response relationships: an overview, a generative model and its application to the verification of descriptive models. Enzyme Microb Technol. 2002; 31: 439-455.
    • (2002) Enzyme Microb Technol. , vol.31 , pp. 439-455
    • Murado, M.A.1    González, M.P.2    Vázquez, J.A.3
  • 40
    • 43049109137 scopus 로고    scopus 로고
    • Proposal for a simple and sensitive haemolytic assay for palytoxin: toxicological dynamics, kinetics, ouabain inhibition and thermal stability
    • Riobó P, Paz B, Franco JM, Vázquez JA, Murado MA. Proposal for a simple and sensitive haemolytic assay for palytoxin: toxicological dynamics, kinetics, ouabain inhibition and thermal stability. Harmful Algae. 2008; 7: 415-429.
    • (2008) Harmful Algae. , vol.7 , pp. 415-429
    • Riobó, P.1    Paz, B.2    Franco, J.M.3    Vázquez, J.A.4    Murado, M.A.5
  • 41
    • 76449083570 scopus 로고    scopus 로고
    • Mathematical model for the characterization and objective comparison of antioxidant activities
    • Murado MA, Vázquez JA. Mathematical model for the characterization and objective comparison of antioxidant activities. J Agric Food Chem. 2010; 58: 1622-1629.
    • (2010) J Agric Food Chem. , vol.58 , pp. 1622-1629
    • Murado, M.A.1    Vázquez, J.A.2
  • 42
    • 0036568634 scopus 로고    scopus 로고
    • Modelling temperature and pH dependence of lipase and peroxidase activity in Turkish hazelnuts
    • Seyhan F, Tijskens LMM, Evranuz O. Modelling temperature and pH dependence of lipase and peroxidase activity in Turkish hazelnuts. J Food Eng. 2002; 52: 387-395.
    • (2002) J Food Eng. , vol.52 , pp. 387-395
    • Seyhan, F.1    Tijskens, L.M.M.2    Evranuz, O.3
  • 43
    • 0041982330 scopus 로고    scopus 로고
    • Model selection tests for nonlinear dynamic models
    • Rivers D, Vuong Q. Model selection tests for nonlinear dynamic models. Econometrics J. 2002; 5: 1-39.
    • (2002) Econometrics J. , vol.5 , pp. 1-39
    • Rivers, D.1    Vuong, Q.2
  • 44
    • 0000177088 scopus 로고    scopus 로고
    • Key concepts in model selection: performance and generalizability
    • Forster MR. Key concepts in model selection: performance and generalizability. J Math. Psychol. 2000; 44: 205-231.
    • (2000) J Math. Psychol. , vol.44 , pp. 205-231
    • Forster, M.R.1
  • 45
    • 0001507671 scopus 로고
    • Model selection criteria: an investigation of relative accuracy, posterior probabilities, and combinations of criteria
    • Rust RT, Simester D, Brodie RJ, Nilikant V. Model selection criteria: an investigation of relative accuracy, posterior probabilities, and combinations of criteria. Manage. Sci. 1995; 41: 322-333.
    • (1995) Manage. Sci. , vol.41 , pp. 322-333
    • Rust, R.T.1    Simester, D.2    Brodie, R.J.3    Nilikant, V.4
  • 47
    • 0033969581 scopus 로고    scopus 로고
    • Characterization of a 29-kDa β-1,3-glucanase from Trichoderma harzianum
    • Noronha EF, Ulhoa CJ. Characterization of a 29-kDa β-1, 3-glucanase from Trichoderma harzianum. FEMS Microbiol Lett. 2000; 183: 119-123.
    • (2000) FEMS Microbiol Lett. , vol.183 , pp. 119-123
    • Noronha, E.F.1    Ulhoa, C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.