Pressure induced changes in the gelation of milk protein concentrates

Briscoe, B.J.; Luckham, P.F.; Staeritz, Karsten U.

doi:10.1016/s0921-0423(02)80137-x

Cited by 5 publications

(4 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The results suggest that increasing the non-micellar casein content by HP treatment of milk is a strategy that may be used to obtain high protein milk powders with enhanced solubility. Improved gelation of MPC has been reported by Briscoe et al (2002) after application of moderate pressures (up to 1000 bar).…”

Section: Modification Of Functional Properties By Processingmentioning

confidence: 92%

“…A further explanation indicated that the possible formation of casein-calcium-pectin complexes with the casein micelles or in the serum phase, along with casein-casein and pectin-pectin interactions (through calcium) and casein-pectin complexes formed during acidification, are responsible for the development of the acid-induced three-dimensional network. The work on understanding the formation of gels in MPC is still on-going with the predominant factor still not yet determined Briscoe et al (2002). also studied the gelation of aqueous MPC (13% w/w) and attributed the enhanced gelation upon pressurization (up to 1000 bar) on the disruption of hydrophobic groups and ionization of charged groups caused by an increase in electrostriction and to a smaller extent on the disruption of hydrogen bonds.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Functional Characteristics of Milk Protein Concentrates and Their Modification

Uluko

Lü

et al. 2015

Critical Reviews in Food Science and Nutrition

View full text Add to dashboard Cite

A major deterrent to the usage of milk protein concentrate (MPC), a high-protein milk product with increasing demand as a food and sports drink ingredient, has been its poor functional characteristics when compared with other milk protein products such as whey protein concentrate and sodium caseinates. This review discusses the recent research on functional properties of MPC, focusing on factors that may contribute to the poor functional characteristics before, during, and after production. Current research, methods employed, and new understanding on the causes of poor solubility of MPC at mild temperatures (about 20°C) has been presented, including loss of solubility during storage as these areas have received unprecedented attention over the past decade, and also affects other useful functional properties of MPC, such as emulsifying properties, gelation, and foaming. Processing methods, which include heat treatment, high-pressure application, microwave heating, ultrasound application, and enzyme and salts modification, have been used or have potential to modify or improve the functional properties of MPCs. Future research on the effects of these processing methods on the functional properties, including effects of enzyme hydrolysis on bitterness and bioactivity, has also been discussed.

show abstract

Section: Modification Of Functional Properties By Processingmentioning

confidence: 92%

mentioning

confidence: 99%

Functional Characteristics of Milk Protein Concentrates and Their Modification

Uluko

Lü

et al. 2015

Critical Reviews in Food Science and Nutrition

View full text Add to dashboard Cite

show abstract

“…The Haake High Pressure High Temperature (HPHT) Rheometer (Germany=UK), a purpose built viscometer based upon a Haake RV 100 viscometer [1][2][3][4][5] adopts the principle of a standard rotational viscometer and uses a special magnetic coupling to transmit the driving torque from the sample which is housed in a pressure chamber. Pressures of up to 1000 bar can be applied to the material under investigation and the instrument measures the material properties while pressure is applied.…”

Section: Experimental Methodsmentioning

confidence: 99%

Gelation of Milk Protein Concentrates Induced by Moderate Hydrostatic Pressures

Briscoe

Luckham

Staeritz³

2002

High Pressure Research

View full text Add to dashboard Cite

Gelation of aqueous milk protein concentrates made up of spray dried milk was monitored both at atmospheric pressure and at moderate pressures (up to 1000 bar) using rheological methods. A Paar Physica UDS 200 rheometer was used to measure the gelation time at atmospheric pressure as a function of the temperature for a protein concentration of 16% [w=w]. The temperature dependence of the gelation time is well approximated by the Ross-Murphy model, which was originally developed to describe the concentration dependence of the gelation time. Using a purpose built Haake High Pressure High Temperature Rheometer, the effects of moderate pressures upon the gelation of milk protein concentrates (13% [w=w] protein content) were investigated. It was found that the gelation time reduces significantly (by up to almost an order of magnitude), when pressures of up to 1000 bar were applied. These findings, combined with the work of others indicate that these pressures bring about two effects: (1) casein micelle dissociation and as a result facilitate reassociation of those smaller micelle fragments, and (2) denaturation of beta-lactoglobulin. However, the main contribution to enhanced gelation was attributed to the caseins. It is not clear if association of whey proteins with caseins occur at moderate pressures around 50 C. We have modelled the dependence of the rate of gelation on pressure by an Eyring reaction rate process type equation. The major contribution to enhanced gelation upon pressurisation was attributed to a disruption of hydrophobic groups and ionisation of charged groups caused by an increase in electrostrictionhowever, disruption of hydrogen bonds was suggested to contribute to a lesser but still important extent.

show abstract

“…The unbound fluid content decreased with increasing peanut protein concentration, and the gel strength was higher than that of a protein solution at a low concentration. However, at higher concentration, the gel strength decreased because of the disordered gel network structure [29]. Wheat gluten protein (WGP) is also an important source of protein in human food and contains approximately 15 amino acids [30].…”

Section: Regulation Of Internal Factors Protein Composition and Contentmentioning

confidence: 99%

Plant Protein Heat-Induced Gels: Formation Mechanisms and Regulatory Strategies

Ma,

Chen

2023

Coatings

View full text Add to dashboard Cite

With increasing awareness of human health, proteins from plant sources are being considered as alternatives to those from animal sources. The market for plant-based meat substitutes is expanding to satisfy the growing consumer demand. However, the functional properties of natural proteins frequently do not satisfy the needs of the modern food industry, which requires high-quality properties. Research on improving the functional properties of proteins is currently a popular topic. Based on the gel properties of proteins, this study focused on the formation mechanism of heat-induced protein gels, which will be helpful in expanding the market for plant protein gel products. Regulatory strategies for heat-induced gels were reviewed, including protein composition, pH, ionic strength, other food components, and processing techniques. The effects of other food components (such as polysaccharides, proteins, polyphenols, and liposomes) are discussed to provide insights into the properties of plant protein gels. Studies have shown that these factors can effectively improve the properties of plant protein gels. In addition, the development and application potential of emerging processing technologies that can contribute to safe and effective applications in actual food production are discussed. For the future, plant protein gels are playing an irreplaceable role in the new direction of future food.

show abstract

Pressure induced changes in the gelation of milk protein concentrates

Cited by 5 publications

References 13 publications

Functional Characteristics of Milk Protein Concentrates and Their Modification

Functional Characteristics of Milk Protein Concentrates and Their Modification

Gelation of Milk Protein Concentrates Induced by Moderate Hydrostatic Pressures

Plant Protein Heat-Induced Gels: Formation Mechanisms and Regulatory Strategies

Contact Info

Product

Resources

About