In this study, trypsin (Enzyme Comission 3.4.21.4) was immobilized in a low cost, lignocellulosic support (corn cob powder—CCP) with the goal of obtaining peptides with bioactive potential from cheese whey. The pretreated support was activated with glyoxyl groups, glutaraldehyde and IDA-glyoxyl. The immobilization yields of the derivatives were higher than 83%, and the retention of catalytic activity was higher than 74%. The trypsin-glyoxyl-CCP derivative was thermally stable at 65 °C, a value that was 1090-fold higher than that obtained with the free enzyme. The trypsin-IDA-glyoxyl-CCP and trypsin-glutaraldehyde-CCP derivatives had thermal stabilities that were 883- and five-fold higher, respectively, then those obtained with the free enzyme. In the batch experiments, trypsin-IDA-glyoxyl-CCP retained 91% of its activity and had a degree of hydrolysis of 12.49%, while the values for trypsin-glyoxyl-CCP were 87% and 15.46%, respectively. The stabilized derivative trypsin-glyoxyl-CCP was also tested in an upflow packed-bed reactor. The hydrodynamic characterization of this reactor was a plug flow pattern, and the kinetics of this system provided a relative activity of 3.04 ± 0.01 U·g⁻¹ and an average degree of hydrolysis of 23%, which were suitable for the production of potentially bioactive peptides.

The authors would like to add the following sentence to the “Acknowledgments” section of their article [1]:

This study aimed to develop and characterize a bioreactor for the continuous production of bioactive peptides from whey proteins. For this purpose, a packed bed reactor (PBR) containing Alcalase immobilized on the glyoxyl‐corn‐cob‐powder support (AGCCP–PBR) was used to hydrolyze whey proteins at 50°C and pH 9.0. The hydrodynamic behavior of the reactor was characterized using phenol red as a tracer, revealing moderate axial dispersion with minimal preferential flow paths. The AGCCP–PBR proved highly effective for the bioconversion process, achieving a high degree of hydrolysis (63.9%) and high operational stability (kd = 0.032 h ⁻¹ ; half‐life = 246 h). The process yielded predominantly low‐molecular‐weight peptides (< 2600 m/z) with high ABTS radical scavenging activity (65.27% reduction). These results demonstrate the considerable potential of the system for applications in the food, pharmaceutical, and chemical industries, where antioxidant compounds play a key role in oxidation control and product stability. Furthermore, the AGCCP–PBR represents an efficient and sustainable strategy for converting by‐products from the dairy industry into functional ingredients, thereby adding value to cheese whey and contributing to waste valorization.

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