Effect of lactose on cross‐linking of milk proteins during heat treatments

Al-Saadi, Jasim M S; Easa, Azhar Mat; Deeth, Hilton C.

doi:10.1111/j.1471-0307.2012.00878.x

Cited by 53 publications

(39 citation statements)

References 28 publications

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“…For instance, Al-Saadi et al [46] compared the formation of non-enzymatic cross-links in milk protein samples during heat treatment at 95 • C in the presence or absence of lactose. They observed considerable polymerisation in both cases, but cross-linking was more pronounced in the presence of lactose, indicating a strong impact of the Maillaird reaction in addition to dehydroalanine-derived cross-links such as lysinoalanine.…”

Section: Literature Review Of Studies On Cross-linked Caseinmentioning

confidence: 99%

“…Alkaline treatment, especially in combination with heating, transforms particular amino acid residues into reactive intermediates, which form cross-links by reactions with other functional groups. Typical products are lysinoalanine, histidinoalanine and lanthionine, which can be determined by chromatographic techniques, e.g., [43][44][45][46][47][48]. Severe heat treatment may even induce the formation of isopeptide bonds between lysine and glutamine (N-ε-(γ-glutamyl)-lysine) or asparagine (N-ε-(β-aspartyl)-lysine), however, these reactions are competed by the Maillard reaction and therefore restricted in the presence of reducing carbohydrates [23,42,49,50].…”

Section: Non-enzymatic Cross-linkingmentioning

confidence: 99%

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Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

et al. 2018

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Abstract:Casein is the major protein fraction in milk, and its cross-linking has been a topic of scientific interest for many years. Enzymatic cross-linking has huge potential to modify relevant techno-functional properties of casein, whereas non-enzymatic cross-linking occurs naturally during the storage and processing of milk and dairy products. Two size separation techniques were applied for characterisation of these reactions: gel electrophoresis and size exclusion chromatography. This review summarises their separation principles and discusses the outcome of studies on cross-linked casein from the last~20 years. Both methods, however, show limitations concerning separation range and are applied mainly under denaturing and reducing conditions. In contrast, field flow fractionation has a broad separation range and can be easily applied under native conditions. Although this method has become a powerful tool in polymer and nanoparticle analysis and was used in few studies on casein micelles, it has not yet been applied to investigate cross-linked casein. Finally, the principles and requirements for absolute molar mass determination are reviewed, which will be of increased interest in the future since suitable calibration substances for casein polymers are scarce.

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Section: Literature Review Of Studies On Cross-linked Caseinmentioning

confidence: 99%

Section: Non-enzymatic Cross-linkingmentioning

confidence: 99%

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

et al. 2018

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“…Dworschak and others () and Al‐Saadi and others () made similar observations by adding D‐glucose in alkali‐treated proteins or lactose in heated milk protein. The Maillard reaction occurs when some carbohydrates react with ε‐NH 2 of some amino acids under certain conditions (Friedman ).…”

Section: Resultsmentioning

confidence: 53%

“…Various chemical additives, such as certain sulfhydryl compounds, glucose, malic acid, ascorbic acid, sodium sulfite, acylation reagents, and metal salts, have been used to reduce the formation of LAL in model systems or actual food samples during alkali or heat‐treatment processes (Friedman , , ; Dworschak and others ; Friedman and others ; Friedman and Gumbmann ; Chang and others ; Al‐Saadi and others ). They presented effective mitigation of LAL formation not only by inhibiting or reducing dehydroalanine intermediate formation, but also by diminishing lysine precursor for LAL formation, besides bringing about some other changes through protein chemical modifications (Friedman ).…”

Section: Introductionmentioning

confidence: 99%

Effects of Sulfhydryl Compounds, Carbohydrates, Organic Acids, and Sodium Sulfite on the Formation of Lysinoalanine in Preserved Egg

Luo

Zhao

et al. 2014

Journal of Food Science

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To identify inhibitors for lysinoalanine formation in preserved egg, sulfhydryl compounds (glutathione, L-cysteine), carbohydrates (sucrose, D-glucose, maltose), organic acids (L-ascorbic acid, citric acid, DL-malic acid, lactic acid), and sodium sulfite were individually added at different concentrations to a pickling solution to prepare preserved eggs. Lysinoalanine formation as an index of these 10 substances was determined. Results indicate that glutathione, D-glucose, maltose, L-ascorbic acid, citric acid, lactic acid, and sodium sulfite all effectively diminished lysinoalanine formation in preserved egg albumen and yolk. When 40 and 80 mmol/L of sodium sulfite, citric acid, L-ascorbic acid, and D-glucose were individually added into the pickling solution, the inhibition rates of lysinoalanine in the produced preserved egg albumen and yolk were higher. However, the attempt of minimizing lysinoalanine formation was combined with the premise of ensuring preserved eggs quality. Moreover, the addition of 40 and 80 mmol/L of sodium sulfite, 40 and 80 mmol/L of D-glucose, 40 mmol/L of citric acid, and 40 mmol/L of L-ascorbic acid was optimal to produce preserved eggs. The corresponding inhibition rates of lysinoalanine in the albumen were approximately 76.3% to 76.5%, 67.6% to 67.8%, 74.6%, and 74.6%, and the corresponding inhibition rates of lysinoalanine in the yolk were about 68.7% to 69.7%, 50.6% to 51.8%, 70.4%, and 57.8%. It was concluded that sodium sulfite, D-glucose, L-ascorbic, and citric acid at suitable concentrations can be used to control the formation of lysinoalanine during preserved egg processing.

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“…The patterns show thick bands at the entry of stacking gel corresponding to high molecular mass protein aggregates, which were not able to penetrate the gel. Aggregates probably correspond to denatured whey proteins associated with themselves and caseins via thiol-disulphide exchange 16,17 , non-covalent interactions 18 and/or covalent interactions 19 . Faint bands corresponding to native-like whey proteins namely α-la and β-lg further supported this suggestion.…”

Section: Resultsmentioning

confidence: 99%

Electrophoretic characterization of protein interactions suggesting limited feasibility of accelerated shelf-life testing of ultra-high temperature milk

Grewal

Chandrapala

Donkor

et al. 2017

Journal of Dairy Science

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Accelerated shelf life testing is applied to a variety of products to estimate keeping quality in a short period of time. The industry has not been successful to apply this approach to UHT milk due to a number of chemical and physical changes of milk proteins that take place during processing and storage. These changes were investigated applying accelerated shelf life principles on UHT milk samples containing 2 different fat levels using native-and SDSpolyacrylamide gel electrophoresis. UHT skim (SM) and whole milk (WM) samples were stored at 20, 30, 40 and 50 °C for 28 days. Irrespective of fat content, UHT treatment had a similar effect on electrophoretic patterns of milk proteins. At the start of testing, proteins were crosslinked mainly through disulphide and non-covalent interactions. However, storage at and above 30 °C enhanced protein crosslinking more via covalent interactions. Extent of aggregation appeared to be influenced by fat content as WM contained a greater amount in comparison to that in SM implying aggregation via melted and/or oxidised fat. Based on reduction in loss in absolute quantity of individual proteins, covalent crosslinking in WM was facilitated manly through deamidated residues and products of lipid oxidation, while Maillard and dehydroalanine products were the main contributors involved in protein changes in SM.Protein crosslinking appears to follow a different pathway at higher temperatures (≥ 40 °C) to that at lower temperatures, which may make it very difficult to extrapolate these changes to predict protein crosslinking at lower temperatures.

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Effect of lactose on cross‐linking of milk proteins during heat treatments

Cited by 53 publications

References 28 publications

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

Effects of Sulfhydryl Compounds, Carbohydrates, Organic Acids, and Sodium Sulfite on the Formation of Lysinoalanine in Preserved Egg

Electrophoretic characterization of protein interactions suggesting limited feasibility of accelerated shelf-life testing of ultra-high temperature milk

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