Rapid and accurate quantification of trypsin activity using integrated infrared and ultraviolet spectroscopy with data fusion techniques
Proteases play a crucial role in industrial enzyme formulations, with activity fluctuations significantly impacting product quality and yield. Therefore, developing a method for precise and rapid detection of protease activity is paramount. This study aimed to develop a rapid and accurate method for...
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Veröffentlicht in: | International journal of biological macromolecules 2024-10, Vol.278 (Pt 3), p.135017, Article 135017 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Proteases play a crucial role in industrial enzyme formulations, with activity fluctuations significantly impacting product quality and yield. Therefore, developing a method for precise and rapid detection of protease activity is paramount. This study aimed to develop a rapid and accurate method for quantifying trypsin activity using integrated infrared (IR) and ultraviolet (UV) spectroscopy combined with data fusion techniques. The developed method evaluates the enzymatic activity of trypsin under varying conditions, including temperature, pH, and ionic strength. By comparing different data fusion methods, the study identifies the optimal model for accurate enzyme activity prediction. The results demonstrated significant improvements in predictive performance using the feature-level data fusion approach. Additionally, substituting the spectral data of the samples in the validation sets into the best prediction model resulted in a minimal residual difference between predicted and true values, further verifying the model's accuracy and reliability. This innovative approach offers a practical solution for the efficient and precise quantification of enzyme activity, with broad applications in industrial processes.
•A comprehensive and rapid method was developed to quantify enzyme activity.•A data fusion strategy for predicting enzyme activity was proposed.•The feature-level data fusion combined with PLS created the best predictive models.•The best prediction models achieved prediction accuracy of 0.9525–0.9744.•Validation of the optimal model confirmed the reliability and stability of trypsin activity prediction. |
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ISSN: | 0141-8130 1879-0003 1879-0003 |
DOI: | 10.1016/j.ijbiomac.2024.135017 |