2012 journal article
Effects of Heating Rate and pH on Fracture and Water-Holding Properties of Globular Protein Gels as Explained by Micro-Phase Separation
JOURNAL OF FOOD SCIENCE, 77(2), E60–E67.
author keywords: egg white; heating rate; micro-phase separation; pH; whey protein isolate
MeSH headings : Egg Proteins / chemistry; Food Handling / methods; Gels / chemistry; Hydrogen-Ion Concentration; Milk Proteins / chemistry; Temperature; Water / chemistry; Whey Proteins
TL;DR:
Gel formation and physical properties of globular protein gels can be explained by micro-phase separation and heating rates that are too rapid require additional holding time at the end-point temperature to allow for full network development.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
6. Clean Water and Sanitation
(OpenAlex)
Source: Web Of Science
Added: August 6, 2018
Abstract: The effect of heating rate and pH on fracture properties and held water (HW) of globular protein gels was investigated. The study was divided into 2 experiments. In the 1st experiment, whey protein isolate (WPI) and egg white protein (EWP) gels were formed at pH 4.5 and 7.0 using heating rates ranging from 0.1 to 35 °C/min and holding times at 80 °C up to 240 min. The 2nd experiment used one heating condition (80 °C for 60 min) and probed in detail the pH range of 4.5 to 7.0 for EWP gels. Fracture properties of gels were measured by torsional deformation and HW was measured as the amount of fluid retained after a mild centrifugation. Single or micro‐phase separated conditions were determined by confocal laser scanning microscopy. The effect of heating rate on fracture properties and HW of globular protein gels can be explained by phase stability of the protein dispersion and total thermal input. Minimal difference in fracture properties and HW of EWP gels at pH 4.5 compared with pH 7.0 were observed while WPI gels were stronger and had higher HW at pH 7.0 as compared to 4.5. This was due to a mild degree of micro‐phase separation of EWP gels across the pH range whereas WPI gels only showed an extreme micro‐phase separation in a narrow pH range. In summary, gel formation and physical properties of globular protein gels can be explained by micro‐phase separation.Practical Application: The effect of heating conditions on hardness and water‐holding properties of protein gels is explained by the relative percentage of micro‐phase separated proteins. Heating rates that are too rapid require additional holding time at the end‐point temperature to allow for full network development. Increase in degree of micro‐phase separation decreases the ability for protein gels to hold water.