Browsing Food Chemistry & Technology by Subject "Gelation"
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Evaluation of a fluorescence and infrared backscatter sensor to monitor acid induced coagulation of skim milkA prototype sensor that employs both ultraviolet excited fluorescence and infrared light backscatter was evaluated as an in-line process analytical technology (PAT) tool to monitor acid induced coagulation kinetics of skim milk. Coagulation experiments were carried out at 32 °C using three concentrations of glucono-delta-lactone (GDL). Measurement of storage modulus (G′) of acidified skim milk gel was used as a reference rheological method to monitor the coagulation kinetics. Prediction models were developed to predict the times required for acidified skim milk coagulum to reach selected G′ values (0.5 Pa, 1 Pa, 5 Pa, 10 Pa and 15 Pa) using time parameters extracted from the ultraviolet excited fluorescence and infrared light backscatter profiles. A strong correlation was observed between the predicted times developed using time parameters extracted from the prototype sensor profiles and the measured G′ times extracted from the rheometer (R2 = 0.97, standard error of prediction = 2.8 min). This study concluded that the prototype fluorescence and infrared backscatter sensor investigated combined with the developed rheological prediction model can be used as a potential PAT tool for in-line monitoring of coagulation kinetics in the manufacture of acid induced milk gels. Industrial relevance: The prototype fluorescence and infrared backscatter sensor investigated in this study combined with the developed rheological prediction model can be employed to monitor and control coagulation kinetics in a wide range of dairy processing applications including fresh cheese varieties and yoghurt manufacture.
The influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelationThe effect of bovine serum albumin (BSA) on the heat-induced denaturation, aggregation and subsequent acid-induced gelation of β-lactoglobulin (β-lg) was investigated in this work. Changes in the denaturation kinetics of β-lg during heating at 78 °C were determined by monitoring the disappearance of the native protein by reverse-phase chromatography. Replacing β-lg with increasing amounts of BSA, while keeping the total protein concentration constant at 5% (w/w), significantly increased the denaturation rate of β-lg from 2.57±0.30×10−3(g L−1)(1−n)s−1 to 5.07±0.72×10−3(g L−1)(1−n)s−1 (β-lg: BSA ratio of 3:1 w/w). The reaction order for β-lg was 1.40±0.09. Partial replacement of β-lg with BSA (β-lg: BSA ratio of 3:1 w/w) significantly increased the reaction order to 1.67±0.13. Heat-induced aggregates between β-lg and BSA were studied by dynamic light scattering, two-dimensional electrophoresis and size exclusion chromatography. The partial replacement of β-lg with BSA significantly changed the gelling properties of the acid-induced gels. A rapid rate of acidification resulted in a significant decrease, while a slow acidification rate resulted in a significant increase in gel strength. Size exclusion chromatography demonstrated that intermolecular disulphide bond formation occurred during both heat-induced denaturation/aggregation and subsequent acid-induced gelation. Results clearly indicate that BSA contributed to the formation of these disulphide bonds.