A comparative study of heat and high pressure induced gels of whey and egg albumen proteins and their binary mixtures

Ngarize, Sekai; Adams, A.R.; Howell, Nazlin K.

doi:10.1016/j.foodhyd.2004.12.008

Cited by 68 publications

(38 citation statements)

References 48 publications

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“…They consist primarily of β‐Lg, α‐La, BSA, immunoglobulins (Ig), LF, lactoperoxidase, glycomacropeptides, and proteose‐peptone (Almeida et al., ; Etzel, ). They have excellent amino acid composition and high digestibility and bioavailability of essential amino acids, especially branched‐chain amino acids (BCAA, leucine, isoleucine, and valine), in addition to having good technological properties such as solubility (Pelegrine & Gasparetto, ), emulsification (Girard, Turgeon, & Paquin, ), gelatinization (Ngarize, Adams, & Howell, ), and water retention capacity (Vidigal et al., ). In addition, they have antimicrobial and antioxidant functions (Balcão et al., ).…”

Section: Whey Proteinsmentioning

confidence: 99%

Interpolymeric Complexes Formed Between Whey Proteins and Biopolymers: Delivery Systems of Bioactive Ingredients

Santos

Costa

Garcia‐Rojas

2018

Comp Rev Food Sci Food Safe

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Whey proteins are obtained from dairy industry waste. Studies involving the analysis of the bioactive compounds in whey show health benefits, as it is an excellent source of indispensable amino acids. Milk whey contains principally β-lactoglobulin, α-lactoglobulin, bovine serum albumin, and lactoferrin, proteins with innumerable functional and technological properties. One application of these proteins in food is the formation of interpolymer complexes, along with other proteins or anionic polysaccharides. The formation of complexes occurs mainly through electrostatic interactions between a negatively charged biopolymer and a positively charged biopolymer. This formation is influenced by factors such as pH, ionic strength, and biopolymer ratio. Because they do not use high temperatures and chemical reagents and have additional nutritional and functional value, these complexes have been used as encapsulating agents for bioactive ingredients. Recent studies on their training and applications are addressed in this review to boost new research and applications in the food industry, thus increasing opportunities for utilizing whey proteins.

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Section: Whey Proteinsmentioning

confidence: 99%

Interpolymeric Complexes Formed Between Whey Proteins and Biopolymers: Delivery Systems of Bioactive Ingredients

Santos

Costa

Garcia‐Rojas

2018

Comp Rev Food Sci Food Safe

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“…The published studies can be grouped into casein-rich materials (Famelart et al, 1998;Fertsch et al, 2003;Hinrichs, 2007;Keim et al, 2006;Kumeno et al, 1993) and whey-proteinrich materials (Famelart et al, 1998;Fertsch et al, 2003;Kanno et al, 1998;Lee et al, 2006;Ngarize et al, 2005;Patel et al, 2005;Van Camp and Huyghebaert, 1995). A lower number of studies are available for the mixed systems, comprising of dairy and non-dairy matrices (Dickinson and James, 2000;Dumay et al, 1999;Hemar et al, 2010;Michel et al, 2001;Rademacher et al, 2003;Walkenström and Hermansson, 1997b;Zasypkin et al, 1996).…”

Section: High Pressure Processing For Texturing Foodsmentioning

confidence: 99%

“…This was because WPI-gel had a honey-comb type microstructure whereas WPC-gel had coral-like microstructure (Kanno et al, 1998). Ngarize et al (2005) prepared WPI gels (15% w/w, native pH) through HPP (400-800 MPa, at temperatures between 20 and 30°C, for 20 min). The gel hardness increased with increasing pressure.…”

Section: Pressure-induced Gels From Whey Protein Isolate or Concentratementioning

confidence: 99%

Structuring dairy systems through high pressure processing

Devi

Buckow

Hémar

et al. 2013

Journal of Food Engineering

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“…Recently, Raman spectroscopic studies have also been conducted to examine the structural changes that occur in meat proteins upon addition of cold-set binding agents to meat systems (Herrero, Cambero, Ordóñez, de la Hoz, & Carmona, 2008a). This technique has also been used to study the structure of various non-meat proteins such as egg albumen, whey and plasma proteins during the formation of heat-induced gels (AlizadehPasdar, Nakai, & Li-Chan, 2002;Ikeda, 2003;Ngarize, Adams, & Howell, 2005;Dávila, Páres, & Howell, 2006;Dávila, Páres, & Howell, 2007). And again it has been also used to study structural properties of soy proteins (Yu, Ma, Yuen, & Phillips, 2004;Moon & LiChan, 2007).…”

Section: Introductionmentioning

confidence: 99%

Raman spectroscopic determination of structural changes in meat batters upon soy protein addition and heat treatment

Herrero

Carmona

Cofrades

et al. 2008

Food Research International

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a b s t r a c tThis article reports an assessment of the potential of Raman spectroscopy for determination of structural changes in meat batter with and without soy protein isolate (SPI) upon heating. It also reports proximate composition, water binding and texture analyses. Various meat batters were made up for this purpose: a control meat batter and meat batters with 3% and 6% SPI with and without thermal treatment (70°C/ 30 min). Results showed an increase (P < 0.05) in penetration force, hardness and chewiness upon heating. In heated samples, increases (P < 0.05) in hardness and chewiness were observed as a result of SPI addition. Just in heated meat batter with added SPI, Raman spectroscopy analysis revealed decrease (P < 0.05) in a-helix accompanied by an increase (P < 0.05) in b-sheet structures after heating. Significant correlations were found between these secondary structural changes in meat proteins and water binding and textural properties of the meat batters.

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A comparative study of heat and high pressure induced gels of whey and egg albumen proteins and their binary mixtures

Cited by 68 publications

References 48 publications

Interpolymeric Complexes Formed Between Whey Proteins and Biopolymers: Delivery Systems of Bioactive Ingredients

Interpolymeric Complexes Formed Between Whey Proteins and Biopolymers: Delivery Systems of Bioactive Ingredients

Structuring dairy systems through high pressure processing

Raman spectroscopic determination of structural changes in meat batters upon soy protein addition and heat treatment

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