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- Volk, Veronika, et al. Show all 5 Authors
- Journal of the science of food and agriculture 2019 v.99 no.7 pp. 3443-3450
- aspergillopepsin; bitterness; emulsifying; emulsifying properties; enzymatic hydrolysis; enzyme inactivation; half life; heat inactivation; hydrolysates; hydrolysis; pH; protein denaturation; protein hydrolysates; taste; temperature; viscosity; whey protein isolate
- ... BACKGROUND: One possible way to modify the emulsifying properties of whey proteins is by enzymatic hydrolysis. However, most studies covering the influence of the hydrolysis on whey proteins used a heating step (>65 °C) to inactivate the enzyme. This leads to irreversible product changes, like protein denaturation and increased viscosity. Here, the objective was to investigate the single effect of ...
- Volk, Veronika, et al. Show all 6 Authors
- Journal of agricultural and food chemistry 2018 v.67 no.3 pp. 905-915
- Pseudomonas lundensis; UHT milk; amino acid sequences; circular dichroism spectroscopy; enzyme activity; heat tolerance; heat treatment; metalloproteinases; pH; sequence analysis; skim milk; temperature
- ... In the current study, the extracellular endopeptidases from Pseudomonas lundensis and Pseudomonas proteolytica were investigated. The amino acid sequence identity between both endopeptidases is 68%. Both endopeptidases were purified to homogeneity and partially characterized. They were classified as metallopeptidases with a maximum activity at pH 10.0 (P. lundensis) or 8.5 (P. proteolytica) at 35 ...