Enzymatic hydrolysis of protein: Mechanism and kinetic model Export

@article{citeulike:6058704, abstract = {The bioreaction mechanism and kinetic behavior of protein enzymatic hydrolysis for preparing active peptides were investigated to model and characterize the enzymatic hydrolysis curves. Taking into account single-substrate hydrolysis, enzyme inactivation and substrate or product inhibition, the reaction mechanism could be deduced from a series of experimental results carried out in a stirred tank reactor at different substrate concentrations, enzyme concentrations and temperatures based on M-M equation. An exponential equation dh/dt = aexp(-bh) was also established, where parameters a and b have different expressions according to different reaction mechanisms, and different values for different reaction systems. For BSA-trypsin model system, the regressive results agree with the experimental data, i.e. the average relative error was only 4.73\%, and the reaction constants were determined as K m = 0.0748 g/L, K s = 7.961 g/L, k d = 9.358/min, k 2 = 38.439/min, E a = 64.826 kJ/mol, E d = 80.031 kJ/mol in accordance with the proposed kinetic mode. The whole set of exponential kinetic equations can be used to model the bioreaction process of protein enzymatic hydrolysis, to calculate the thermodynamic and kinetic constants, and to optimize the operating parameters for bioreactor design.}, author = {Qi, Wei and He, Zhimin}, citeulike-article-id = {6058704}, citeulike-linkout-0 = {http://dx.doi.org/10.1007/s11458-006-0026-9}, citeulike-linkout-1 = {http://www.springerlink.com/content/441119195516572m}, day = {1}, doi = {10.1007/s11458-006-0026-9}, journal = {Frontiers of Chemistry in China}, keywords = {bsa, enzymatic\_hydrolysis, model}, month = {September}, number = {3}, pages = {308--314}, posted-at = {2009-11-03 09:34:10}, priority = {2}, title = {Enzymatic hydrolysis of protein: Mechanism and kinetic model}, url = {http://dx.doi.org/10.1007/s11458-006-0026-9}, volume = {1}, year = {2006} }

TY - JOUR ID - citeulike:6058704 L3 - citeulike-article-id:6058704 N2 - The bioreaction mechanism and kinetic behavior of protein enzymatic hydrolysis for preparing active peptides were investigated to model and characterize the enzymatic hydrolysis curves. Taking into account single-substrate hydrolysis, enzyme inactivation and substrate or product inhibition, the reaction mechanism could be deduced from a series of experimental results carried out in a stirred tank reactor at different substrate concentrations, enzyme concentrations and temperatures based on M-M equation. An exponential equation dh/dt = aexp(-bh) was also established, where parameters a and b have different expressions according to different reaction mechanisms, and different values for different reaction systems. For BSA-trypsin model system, the regressive results agree with the experimental data, i.e. the average relative error was only 4.73%, and the reaction constants were determined as K m = 0.0748 g/L, K s = 7.961 g/L, k d = 9.358/min, k 2 = 38.439/min, E a = 64.826 kJ/mol, E d = 80.031 kJ/mol in accordance with the proposed kinetic mode. The whole set of exponential kinetic equations can be used to model the bioreaction process of protein enzymatic hydrolysis, to calculate the thermodynamic and kinetic constants, and to optimize the operating parameters for bioreactor design. IS - 3 JF - Frontiers of Chemistry in China EP - 314 TI - Enzymatic hydrolysis of protein: Mechanism and kinetic model VL - 1 SP - 308 KW - bsa KW - enzymatic_hydrolysis KW - model AU - Qi, Wei AU - He, Zhimin PY - 2006/09/01/ UR - http://dx.doi.org/10.1007/s11458-006-0026-9 ER -