Λεπτομέρειες βιβλιογραφικής εγγραφής
| Τίτλος: |
Kinetic characterization of Streptomyces griseus protease: A comparative study of linear and non-linear regression methods. |
| Συγγραφείς: |
Zarza-Gonzalez, Evelyn A.1 (AUTHOR), Gonzáles Benítez, Litzy Ayelem1 (AUTHOR), Cruz Maldonado, Juan Jesús1 (AUTHOR) juan.jcm@tec.mx |
| Πηγή: |
Biocatalysis & Biotransformation. Aug2026, Vol. 44 Issue 4, p299-314. 16p. |
| Θεματικοί όροι: |
*Enzyme kinetics, *Nonlinear regression, *Enzymology, *Curve fitting, *Monte Carlo method, *Streptomyces griseus |
| Περίληψη: |
Enzymes are biological catalysts that facilitate biochemical reactions and are widely applied in industrial processes. In this study we explored kinetic characterization of enzymes, focusing on the estimation of kinetic parameters such as the maximum reaction rate ( υ max ) and the Michaelis-Menten constant ( K m ) , using both linear regression (LR) and nonlinear regression (NLR) methods. Performance of these methods in terms of bias, precision, and accuracy was assessed through synthetic data obtained via Monte Carlo simulations under diverse experimental-like conditions, including data size, substrate concentration distribution and the presence of outliers. Results showed that LR, particularly the Lineweaver-Burk method, consistently yield biased and inaccurate estimates, in contrast NLR methods provide more precise and accurate estimates without the distortion inherent in LR. Moreover, logarithmic substrate distribution improved parameter estimation robustness for most methods, except for Lineweaver-Burk. Further assessment employing experimental data from a commercial protease of S. griseus validated these results and demonstrated that NLR methods provide more precise and accurate estimates than most LR techniques. Experimental assays determined K m of 0.50 ± 0.10 mg/mL and υ max of 0.93 ± 0.05 U/mL (35.8 ± 1.9 U/mg) with an optimal protease activity at 65 °C and pH 8.5. This research underscores the significance of employing appropriate kinetic estimation techniques and conditions to provide reliable kinetic parameters while establishing a basis for future research focused on optimizing enzyme-based processes. [ABSTRACT FROM AUTHOR] |
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