Guedes Paula V, de Freitas Rilton A, Franco Célia R C, Cândido Lys Mary B
Post-graduate Programme of Food Engineering, Chemical Engineering Department, Federal University of Paraná, P.O. Box 19011, Curitiba, PR, Brazil.
Chemistry Department, Federal University of Paraná, P.O. Box 19032, Curitiba, PR, Brazil.
J Dairy Res. 2022 Feb 28:1-8. doi: 10.1017/S0022029922000115.
Caseinomacropeptide (CMP) is derived from the chymosin cleavage of κ-casein during cheese production. This study developed gels from CMPs, which were isolated by different ultrafiltration systems, and whey protein isolate (WPI), and studied their rheological and ultrastructural characteristics. The 30% WPI gel showed high elastic modulus (G') values and stronger structure than the other samples with CMP. Another gel, with 50% protein, 30% WPI and 20% CMP sample isolated from the 30 kDa retentate, had a weaker structure and lower G' value. The third gel, with 30% WPI and 20% CMP sample from the 5 kDa retentate derived from the 30 kDa retentate, presented intermediate structural strength. Despite the increase in protein concentration from the addition of CMP, there was a decrease in the strength of the gel network. Different CMP isolation processes also contributed to differences in the microscopic analysis of gel structures with the same protein content.
