Please use this identifier to cite or link to this item:http://hdl.handle.net/20.500.12105/5232
Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein
Materials. 2016; 9(5):357
In this study, trypsin (Enzyme Comission 184.108.40.206) 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 degrees 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.
corn cob powder functionalized | trypsin | immobilization | reactor | whey protein hydrolysates | peptides | LACTIC-ACID PRODUCTION | GREEN COCONUT FIBER | CORN COBS | HYDROTHERMAL TREATMENT | ACTIVATED SUPPORTS | AMINO-ACIDS | HYDROLYSIS | PRETREATMENT | BIOMASS | STABILIZATION
Files in this item