What question did this study set out to answer?

To evaluate the rate and extent of protein polymer formation in aseptically packed ultra-high-temperature (UHT) milk stored across various temperatures over time.

February 1, 1975Journal of Dairy Research

Properties of aseptically packed ultra-high-temperature milk: III. Formation of polymerized protein during storage at various temperatures

View Full Paper

Ask AI

Bookmark

Authors

AAA. T. Andrews

Discussion

Member takes

Overview

Laboratory study demonstrates temperature-dependent protein polymerization in stored UHT milk, indicating Maillard reactions drive substantial structural alterations over time.

Key Points

To evaluate the rate and extent of protein polymer formation in aseptically packed ultra-high-temperature (UHT) milk stored across various temperatures over time.
Stored UHT-treated milk across four temperatures (4°C, 20°C, 30°C, and 37°C) for up to 6 months and tracked protein polymers using gel filtration chromatography.
Assessed disulphide bonding, the individual contributions of casein fractions using electrophoresis, and proteolytic activity via trichloroacetic acid-soluble fragments.
After 6 months of storage, covalently bound polymers constituted 50% of milk proteins at 37°C, 40% at 30°C, 26% at 20°C, and 21% at 4°C, driven mainly by Maillard-type reactions.
Polymerization preferentially involved αs1-casein over β-casein and altered electrophoretic mobility, while disulphide-bonded polymers diminished gradually as cross-linking continued.
Trichloroacetic acid-soluble fragments showed minimal increases across storage, confirming proteolysis was negligible.

Cite This Study

A. T. Andrews (1975) studied this question.

synapsesocial.com/papers/6a898efbea82e62cf6fd4883 https://doi.org/10.1017/s0022029900015120

View Full Paper

Ask AI

Bookmark

February 1, 1975Journal of Dairy Research

Properties of aseptically packed ultra-high-temperature milk: III. Formation of polymerized protein during storage at various temperatures

View Full Paper

Ask AI

Bookmark

Authors

AAA. T. Andrews

Discussion

Member takes

Overview

Laboratory study demonstrates temperature-dependent protein polymerization in stored UHT milk, indicating Maillard reactions drive substantial structural alterations over time.

Key Points

To evaluate the rate and extent of protein polymer formation in aseptically packed ultra-high-temperature (UHT) milk stored across various temperatures over time.
Stored UHT-treated milk across four temperatures (4°C, 20°C, 30°C, and 37°C) for up to 6 months and tracked protein polymers using gel filtration chromatography.
Assessed disulphide bonding, the individual contributions of casein fractions using electrophoresis, and proteolytic activity via trichloroacetic acid-soluble fragments.
After 6 months of storage, covalently bound polymers constituted 50% of milk proteins at 37°C, 40% at 30°C, 26% at 20°C, and 21% at 4°C, driven mainly by Maillard-type reactions.
Polymerization preferentially involved αs1-casein over β-casein and altered electrophoretic mobility, while disulphide-bonded polymers diminished gradually as cross-linking continued.
Trichloroacetic acid-soluble fragments showed minimal increases across storage, confirming proteolysis was negligible.

Cite This Study

A. T. Andrews (1975) studied this question.

synapsesocial.com/papers/6a898efbea82e62cf6fd4883 https://doi.org/10.1017/s0022029900015120

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark