Title
Effect of pressure or temperature pretreatment of isolated pea protein on properties of the enzymatic hydrolysates
Author
Dongfang Chao, Rong He, Stephanie Jung, Rotimi E. Aluko
Year
2013
Journal
Food Research International
Abstract
Commercial isolated pea protein dispersion (IPP, 1%, w/v) was pretreated with high pressure (200–600 MPa, 5 min at 24 °C) or heat (100 °C, 30 min) prior to hydrolysis using 1–4% (w/w) alcalase concentrations. Fluorescence spectroscopy showed that heat pretreated IPP had a 35% higher level of exposed hydrophobic groups (measured as fluorescence intensity, FI) than the untreated protein. In contrast, the 200 MPa pressure pretreatment produced a 15% increase in FI while 400 and 600 MPa pretreatments, respectively, caused 5 and 60% decreases in FI. Heat pretreatment of IPP enhanced hydrolysis into smaller peptide sizes when compared to peptides from the 24 °C pretreated protein. The 200 MPa pretreatment enhanced IPP hydrolysis into smaller peptides, especially at lower (1–2%) alcalase concentrations. Protein hydrolysates produced from heat-pretreated IPP were less active against angiotensin converting enzyme (ACE) when compared to those from the 24 °C pretreated protein. In general, heat or high pressure pretreatment of IPP favored production of ACE- and renin-inhibitory enhanced protein hydrolysates at a lower (1%) alcalase concentration.
Instrument
FP-6300
Keywords
Fluorescence, Protein structure, Chemical stability, Thermal stability, Biochemistry, Food science