Functional properties of whey proteins microparticulated at low pH

Dissanayake, Muditha; Liyanaarachchi, Winston; Vasiljevic, Todor

doi:10.3168/jds.2011-4823

Cited by 83 publications

(50 citation statements)

References 30 publications

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“…This observation was in line with 187 the observations of an earlier study that showed enhanced heat stability of WP at low pH 188 (Dissanayake et al, 2012). The relatively low ∆H values of WP dispersion heated at pH 6 189 further indicated destruction of hydrophobic bonds, resulting in denaturation of WPs 190 (Damodaran, 2008) are clearly visible only in lane 3 ( Fig.…”

Section: Thermal Analysis Of Whey Protein Dispersions 181 182supporting

confidence: 79%

“…Therefore, the inclusion of WPs into food systems is dependent on processing 48 conditions applied and their influence on protein structure that, due to the heat sensitivity of 49 WPs, may even result in complete denaturation and thus limit their application. Recently a 50 novel approach to stabilization of WPs through microparticulation was proposed 51 (Dissanayake & Vasiljevic, 2009;Dissanayake, Liyanaarachchi, & Vasiljevic, 2012) to 52 alleviate this problem. 53…”

Section: Introduction 36 37mentioning

confidence: 99%

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Influence of heat and pH on structure and conformation of whey proteins

Dissanayake

Ramchandran

Piyadasa

et al. 2013

International Dairy Journal

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Please cite this article as: Dissanayake, M., Ramchandran, L., Piyadasa, C., Vasiljevic, T., Influence of heat and pH on structure and conformation of whey proteins, International Dairy Journal (2012), doi: 10.1016/j.idairyj.2012.08.014. This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. The aim of this study was to understand the fundamental interactions responsible for 24 aggregation of whey proteins (WPs) at pH 6 and 3 during heating at 140 ºC for 30 s in the 25 presence of different acidulants. The conformational changes in the various heat-treated WP 26 dispersions were studied using chemical bond blockers and analysed using differential 27 scanning calorimeter thermograms, polyacrylamide gel electrophoresis and turbidity 28 measurements. Overall, the results indicated that WPs were denatured mainly by disruption 29 of hydrophobic interactions, and that the extent of WP denaturation at pH 3 was affected by 30 the type of acidulant used. The type of acidulant affected the extent of formation of additional 31 high or medium molecular weight aggregates during heating at pH 3, while the types of 32 interactions involved in the formation of such aggregates were affected by the pH at heating. 33Introduction 36 37Whey proteins (WPs) have distinctive nutritional and functional properties that make 38 them unique food ingredients. Different attractive and repulsive molecular forces, involved in 39 the stability of unique three-dimensional structure of proteins (Damodaran, 2008), affect their 40 functionality. These include intrinsic van der Waals and steric forces, as well as electrostatic, 41 hydrogen bonding and hydrophobic interactions that arise from the influence of the 42 surrounding environment. The physico-chemical properties that govern the overall 43 functionality of WPs are a result of intrinsic factors native to the proteins, mainly their 44 structure and conformation, as well as extrinsic factors, such as environmental conditions 45 including pH and temperature. Any processing condition that influences the intrinsic or 46 extrinsic factors will affect protein conformation and thereby influence the functionality of 47WPs. Therefore, the inclusion of WPs into food systems is dependent on processing 48 conditions applied and their influence on protein structure that, due to the heat sensitivity of 49 WPs, may even result in complete denaturation and thus limit their application. Recently a 50 novel approach to stabilization of WPs through microparticulation was proposed 51 (Dissanayake & Vasiljevic, 2009;Dissanayake, Liyanaarachchi, & Vasiljevic, 2012) to 52 alleviate this problem. 53Heating, a commo...

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Section: Thermal Analysis Of Whey Protein Dispersions 181 182supporting

confidence: 79%

Section: Introduction 36 37mentioning

confidence: 99%

Influence of heat and pH on structure and conformation of whey proteins

Dissanayake

Ramchandran

Piyadasa

et al. 2013

International Dairy Journal

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show abstract

“…Since whey proteins are relatively low molecular weight and soluble at its isoelectric point [13], a thermal treatment is necessary to precipitate them [14]. During this process, β-Lg (the major component of whey proteins) undergoes a structural change-exposes the S-S groups, which play a central role in the formation of covalent "bridges" with other proteins.…”

Section: Yield and Water Retention Of Protein Aggregatesmentioning

confidence: 99%

Optimization of Proteins Recovery Process from Cheese Whey

Cuellas¹,

Rosa²,

Jorge³

2015

JAST-B

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Abstract:The process to obtain a protein-containing ingredient from the remaining whey of Argentinean "Cuatriolo" cheese production was studied. In order to optimize the protein recovery, physical and chemical treatments were investigated. Two protocols with different sequences of application of heating step and acid addition were assayed in the presence and absence of fat and CaCl 2 . The results were evaluated by the yield, water retention and particle size. The results showed that the highest yield of the process (76.6%) and an increase in water retention (39.8 w/w) were achieved when the acid was added after boiled and incubated for 30 min at 90 °C. In these working conditions, the presence of calcium shows a lower yield of recovery (72.8 %) and this behaviour correlates with a smaller particle size. Additionally, the presence of fat reduces the particle size and decreases the performance of the process (69.4%). Thus, the yield of protein recovery is related to the particle size of the aggregates, i.e., the recovery of proteins increases when increase the particle size. The simultaneous presence of fat and CaCl 2 increases the amount of water retained in the aggregated protein (47.62 w/w). In conclusion, the process of aggregation in whey protein should take into account both the design of suitable protocol and the presence of fat and additives.

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“…This method has been employed for years and used to produce low-moisture food products such as snacks and breakfast cereals. Another approach termed microparticulation has been used commercially to create whey protein-rich products with enhanced solubility at high temperatures (Dissanayake 2011 Milk is defined as the secretion of the mammary glands of mammals with the primary function to satisfy nutritional requirements of neonates. Milk of some animals, especially cows, buffaloes, goats, and sheep, is used for human consumption, either as such or in the form of a range of dairy products.…”

Section: Referencesmentioning

confidence: 99%

Wet Chemistry Method for Ceramic Membrane Preparation

Cui¹

2016

Encyclopedia of Membranes

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In the context of ▶ diafiltration, wash water is simply another term for diluent. This is the water used to replace impure solvent while retaining the desired product. A typical example might be the washing of a cell suspension prior to cell disruption to release an intracellular product.The typical way of doing this would be to subject the cell suspension to batch crossflow microfiltration while adding wash water at a rate that exactly balances the filtrate (▶ permeate) flow rate. Thus, the cells are retained, but the impure liquid in which the cells are suspended is gradually displaced by wash water.

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Functional properties of whey proteins microparticulated at low pH

Cited by 83 publications

References 30 publications

Influence of heat and pH on structure and conformation of whey proteins

Influence of heat and pH on structure and conformation of whey proteins

Optimization of Proteins Recovery Process from Cheese Whey

Wet Chemistry Method for Ceramic Membrane Preparation

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