期刊
FOODS
卷 11, 期 4, 页码 -出版社
MDPI
DOI: 10.3390/foods11040516
关键词
degree of hydrolysis; milk protein concentrate; molecular mass distribution; sodium caseinate; turbidity; viscosity; whey protein
资金
- Doctoral School on the Agro-Food System of the UniversitaCattolica del Sacro Cuore (PhD grantship from Fondazione di Piacenza e Vigevano)
This study investigated the physicochemical properties of hydrolysates generated from different protein sources using two enzymes. The degree of hydrolysis increased with incubation time, and the hydrolysis with Debitrase HYW20 (TM) resulted in higher levels of small peptides compared to Prolyve (TM). The effect of hydrolysis on physicochemical properties varied depending on the substrate and the heat inactivation step had an impact on the physical properties of the hydrolysates.
This study determined the physicochemical properties (apparent viscosity (eta(app)), turbidity (A(550nm)), particle size and molecular mass distribution) of hydrolysates generated from whey protein concentrate (WPC), milk protein concentrate (MPC) and sodium caseinate (NaCN), following incubation with Debitrase HYW20 (TM) and Prolyve (TM) at 50 degrees C, pH 7.0 for 1 and 4 h, before and after heat inactivation (80 degrees C for 10 min). The degree of hydrolysis (DH) increased with incubation time, giving values of 6.56%, 8.17% and 9.48%, following 1 h hydrolysis of WPC, MPC and NaCN with Debitrase HYW20 (TM), and 12.04%, 15.74% and 17.78%, respectively, following 4 h incubation. These DHs were significantly higher compared to those obtained following 4 h incubation with Prolyve (TM). Hydrolysis with Debitrase HYW20 (TM) gave >40% of peptides with molecular masses < 1 kDa for all substrates, which was higher than the value obtained following hydrolysis with Prolyve (TM). The effect of hydrolysis on the physicochemical properties was substrate dependent, since eta(app) decreased in WPC and NaCN hydrolysates, particle size decreased for all the substrates, with aggregate formation for MPC, and turbidity decreased in WPC and MPC hydrolysates, while it increased in NaCN hydrolysates. The physical properties of the hydrolysates were influenced by the enzyme thermal inactivation step in a DH-dependent manner, with no significant effect on turbidity and viscosity for hydrolysates at higher DHs.
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