ENZYME-INDUCED COAGULATION OF CASEIN MICELLES - A NUMBER OF DIFFERENT KINETIC-MODELS

被引:16
|
作者
HYSLOP, DB
机构
[1] Department of Food Science, University of Wisconsin, Madison, WI
关键词
D O I
10.1017/S0022029900027874
中图分类号
S8 [畜牧、 动物医学、狩猎、蚕、蜂];
学科分类号
0905 ;
摘要
Several mathematical models are presented in an attempt to describe the kinetics of the enzyme-induced coagulation of casein micelles. In each model the primary phase of the clotting reaction is assumed to follow first order kinetics. The only differences amongst the various models centre on the definition of the flocculation rate constant, which is defined in seven different ways. The rate constants are defined and discussed in terms of activation energy and functionality theory. The first model is such that the number of functional sites is two. The second is such that the number is much larger. The third and fourth are such that there is an exponential energy barrier, one which has a magnitude proportional to the extent of proteolysis caused by the clotting enzyme. These two definitions differ only in the pre-exponent. In one case the pre-exponent is a constant, whereas in the other it is dependent on the size of clotting particles. The fifth and sixth definitions are also energy barrier rate constants, but the energy barrier changes in an arbitrary fashion with respect to time during proteolysis. The seventh definition assumes a large number of functional sites, but such that the number increases with extent of proteolysis. In the Payens nomenclature (Payens, 1989), all models could be considered to be 'source' models, and all are derived using the Drake moment equation (Drake, 1972). Only the first model has a truly constant flocculation rate parameter, and only this model has a relatively simple analytical solution. All other models yield analytical solutions only by way of infinite series expansions. Thus, all models are presented in terms of power series expansions, and only through the first five time-dependent coefficients. This confines all models to the early stages of coagulation. In all cases the first three coefficients are virtually the same. The first two coefficients involve only proteolysis, and the third includes initial flocculation information. Time-dependent changes in the flocculation rate constant begin to take effect in the fourth, coefficient. When the fourth coefficients of the third and seventh models are compared, a simple relationship is suggested between free energy barrier removal and functional site generation, but only assuming that the number of functionalities is large.
引用
收藏
页码:517 / 533
页数:17
相关论文
共 50 条
  • [31] Application of casein-combined enzyme-induced carbonate precipitation to mitigate shallow failure in cut slope
    Phanvongsa, Nilundone
    Nakayenga, Joyce
    Hata, Toshiro
    BULLETIN OF ENGINEERING GEOLOGY AND THE ENVIRONMENT, 2023, 82 (12)
  • [32] Heat-induced coagulation of goat milk: modification of the environment of the casein micelles by membrane processes
    Bouhallab, S
    Leconte, N
    Le Graet, Y
    Garem, A
    LAIT, 2002, 82 (06): : 673 - 681
  • [33] COMPARISON OF ION CURRENT NOISE PREDICTED FROM DIFFERENT KINETIC-MODELS OF SODIUM CHANNEL
    CLAY, JR
    BIOPHYSICAL JOURNAL, 1977, 17 (02) : A12 - A12
  • [34] RHEOLOGICAL STUDY ON THE RENNET-INDUCED GELATION OF CASEIN MICELLES WITH DIFFERENT SIZES
    NIKI, R
    KOHYAMA, K
    SANO, Y
    NISHINARI, K
    POLYMER GELS AND NETWORKS, 1994, 2 (02) : 105 - 118
  • [35] Heat-induced gelation of casein micelles in aqueous suspensions at different pH
    Thomar, Peggy
    Nicolai, Taco
    COLLOIDS AND SURFACES B-BIOINTERFACES, 2016, 146 : 801 - 807
  • [36] A SINGLE-PARAMETER FAMILY OF ADJUSTMENTS FOR FITTING ENZYME KINETIC-MODELS TO PROGRESS-CURVE DATA
    DUGGLEBY, RG
    NASH, JC
    BIOCHEMICAL JOURNAL, 1989, 257 (01) : 57 - 64
  • [37] Effects of enzyme-induced carbonate precipitation (EICP) with different urease sources on the zinc remediation
    Chen, Yanbo
    Wang, Qingyang
    Bian, Yi
    Zhan, Liangtong
    Gao, Yufeng
    Guo, Haowen
    Wang, Yuze
    Gao, Yunqi
    JOURNAL OF HAZARDOUS MATERIALS, 2024, 480
  • [38] EFFECT OF MICROENVIRONMENTAL CHANGES ON KINETIC PARAMETERS OF STEADY-STATE ENZYME-INDUCED BACTERIAL BIOLUMINESCENT REACTION
    Sukovataya, I. E.
    Tyulkova, N. A.
    Kaykova, E. V.
    BIOLUMINESCENCE AND CHEMILUMINESCENCE: CHEMISTRY, BIOLOGY AND APPLICATIONS, 2007, : 27 - +
  • [39] MULTICOMPARTMENT KINETIC-MODELS FOR INJURY, RESUSCITATION, INDUCED LAG AND GROWTH IN BACTERIAL-CELL POPULATIONS
    HILLS, BP
    MACKEY, BM
    FOOD MICROBIOLOGY, 1995, 12 (04) : 333 - 346
  • [40] Proteolysis of Micellar β-Casein by Trypsin: Secondary Structure Characterization and Kinetic Modeling at Different Enzyme Concentrations
    Vorob'ev, Mikhail M.
    Acikgoez, Burcin Dersu
    Guler, Gunnur
    Golovanov, Andrey V.
    Sinitsyna, Olga V.
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2023, 24 (04)