Kinetic Model For Enzymatic Hydrolysis Of Decapterus Maruadsi Protein

Recently, the researchs of enzymatic hydrolysis Decapterus Maruadsi protein are the optimization of process conditions and the choice of enzyme, which was more than the law of enzymatic hydrolysis the process. The study of the dynamics in the enzymatic hydrolysis process is not only to deepen the understanding of enzymatic hydrolysis process, but also to obtain the goal of hydrolysis products of the hydrolysis conditions and effectively guide the production practice. The traditional methods modeled by the conventional Michaelis-Menten equation with constant kinetic parameters Michaelis constant is difficult to truly characterize the entire reaction course. In this paper, alkaline protease-Decapterus Maruadsi protein hydrolyzate system was characterized by the three methods of the macro-dynamic model,3D graphics, and the lumped kinetic model.Macro-dynamics characterization of alkaline protease-Decapterus Maruadsi protein hydrolyzate system was based on the reaction mechanism of the Michaelis-Menten equation, added influencing factors of the enzyme inactivation, substrate inhibition and product inhibition. Then the reaction ratestudy was substituted by the degree of hydrolysis, in order to establish the degree of hydrolysis kinetic model. The results of the degree of hydrolysis kinetic showed that the conditions of pH8.5, temperature47.5℃, the enzymatic system substrate inhibition and product inhibition could be ignored. Meanwhile, in order to improve efficiency and reduce the workload, estimating the model parameters was optimized by the D-optimal design method. The D-optimal design can be well applied to the estimation of the degree of hydrolysis of the enzymatic system dynamic model parameters. The macro enzymatic hydrolysis process was better characterized by the degree of hydrolysis of model, DH=5.781n [(-0.107+55.584[Eo]/[So])×t+1], the average relative error of6.67%, with certain guidance meaning and theoretical basis for optimizing process conditions.3D graphic characterization of alkaline protease-Decapterus Maruadsi protein hydrolyzate system was with a more clear purpose by introducing the molecular weight and the mass percentage of peptide segments. The molecular weight distribution of peptide fragments in the hydrolysates under different degree of hydrolysis was determined by size exclusion chromatography, the results was showed:the component of molecular weight greater than10kDa was constantly reduction. The variation other of virtual components were not obvious. In order to more systematic and intuitive characterization of the enzymatic system as a function of the degree of hydrolysis and molecular weight, weight percent based on the peptide fragments, the3D surface map had been drawn. Virtual component of more than lOkDa continued to decline, the following5kDa gradually increased, while5～10kDa firstly increased and then decreased. Which can be inferred that the main reaction course of the enzymatic system high molecular weight protein was gradually degraded into small molecular weight.3D surface fitted function to characterize the enzymatic system of mathematical expressions:m=10.4194+1.1209DH-0.0329(DH)2-0.0006(DH)3+0.0999(DH)2-Mw+23.7492Mw-16.4377(Mw)2+11.6233(Mw)3-0.8423DH·(Mw)2-2.2178DH·Mw, the average relative error12.75%. The reaction mechanism of the enzymatic system was characterized by the3D model,via the relationship the mass percentage, molecular weight and the degree of hydrolysis.Lumped kinetic characterization of alkaline protease-Decapterus Maruadsi protein hydrolyzate system was based on the solubility characteristics of Decapterus Maruadsi protein and the dynamic characteristics of the components to be designated as the four lumped. Then lumped components were measured Michaelis constant, product inhibition constants and substrate inhibition constant, with the Marquardt method to estimate the kinetic parameters of lumped kinetic reaction network. The lumped kinetic model was showed: components and kinetic reaction mechanism were described by the lumped kinetic model, which provided theoretical support to obtain peptide fragments.