Some physico-chemical properties and structural changes of bovine β-casein upon glycation

Darewicz, Małgorzata; Dziuba, J.; Mioduszewska, H.

doi:10.1002/(sici)1521-3803(199808)42:03/04<213::aid-food213>3.0.co;2-i

Cited by 15 publications

(12 citation statements)

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“…In below-presented studies we used analytical approach described by Nessar and Furth [19], that have been employed viz optical spectroscopy. It was found via that method, that seven glucose molecules were bound to one molecule of b-casein [14]. More recently, mass spectrometry has been employed in this field.…”

Section: Characterization Of Glycosylated B-caseinmentioning

confidence: 82%

“…In our ealier studies we reported about the changes of bovine b-casein upon 15-day glycosylation with glucose [14]. We concluded that glycosylation of b-casein proceeded in stages.…”

mentioning

confidence: 99%

“…The present work was carried out to determine the effect of covalent binding of glucose molecules to b-casein on its emulsion properties in relation to molecular status of b-casein. Our intensions in this study was to increase the amphiphilic feature of b-casein via terminating the reaction of coupling glucose molecules after 24 h (time was calculated from our earlier results) [14].…”

mentioning

confidence: 99%

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The effect of glycosylation on emulsifying and structural properties of bovine β-casein

Darewicz¹,

Dziuba²

2001

Nahrung

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A number of attempts have been made to improve the functional properties of milk proteins by chemical modifications. One of such modifications is glycosylation which was carried out to determine the effect of covalent binding of glucose molecules to beta-casein (beta CN) on its emulsifying properties. It was found that up to six molecules of glucose were bound to one molecule of beta CN. Glycosylated beta CN produced smaller emulsion droplets than the intact beta CN. Increases in emulsion-forming and -stabilizing properties were observed. A prerequisite of proteins to form emulsions is their adsorption onto oil/water interface. Therefore the secondary structure of intact and glycosylated beta CN, both in solution and adsorbed onto a hydrophobic teflon/water interface also were studied by far-ultra violet circular dichroism (CD). It appeared, that after glycosylation the degree of helicity of intact beta CN decreased and the incorporation of glucose moieties most likely resulted in a type beta-turn formation after adsorption onto the interface.

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Section: Characterization Of Glycosylated B-caseinmentioning

confidence: 82%

“…In our ealier studies we reported about the changes of bovine b-casein upon 15-day glycosylation with glucose [14]. We concluded that glycosylation of b-casein proceeded in stages.…”

mentioning

confidence: 99%

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confidence: 99%

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The effect of glycosylation on emulsifying and structural properties of bovine β-casein

Darewicz¹,

Dziuba²

2001

Nahrung

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“…After these modifications, they concluded that glycation (1) shifted the pHi of casein toward more acidic pH values and (2) decreased the solubility at acid pH. In another publication, the same team (Darewicz et al 1999b) reported structural changes deduced by modification of absorption spectra in UV and a better heat stability of β-casein after its glycation. Corzo-Martinez et al (2010) worked on the characterization and improvement of rheological properties of glycated sodium caseinate with galactose, lactose, and dextran.…”

Section: Reaction With Sugarsmentioning

confidence: 97%

Modifications of structures and functions of caseins: a scientific and technological challenge

Broyard

Gaucheron

2015

Dairy Sci. & Technol.

250

133

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Casein molecules are used in food industry as ingredients. They can be used as isolated forms and under micellar form consisting in an association of different casein molecules and calcium phosphate. In this review, after a brief reminder of the main characteristics of casein molecules and casein micelles, the modifications of caseins induced by physical, chemical, and enzymatic actions are reported. The resulting new physicochemical properties (mineral and casein compositions, charge, hydrophobicity, aggregation state, and morphology) and techno-functionalities (heat stability, viscosity, gelation, emulsifying, and foaming properties) are described and discussed with a special attention paid to the results obtained in our laboratory since several decades.

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“…There are some reports in which the glycosylation enhances the thermal stability of food proteins [2,6,16,26,42], and the same functional improvement was also observed in fish Mf [7,19]. Figure 30.4 shows the thermal stability of carp Mf conjugated with alginate oligosaccharide (Mf-AO conjugate) under different NaCl concentrations and pH levels [34].…”

Section: Improvement Of the Thermal Stability And Emulsion-forming Abmentioning

confidence: 99%

A New Approach to the Functional Improvement of Fish Meat Proteins

Saeki

2010

Handbook of Seafood Quality, Safety and Health Applications

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Fish and shellfish are important protein sources and are widely used as raw material for preparation of processed seafood. Fish meat is highly nutritious, and its myofibrillar (Mf) protein has excellent functional properties, such as emulsion-and gel-forming abilities, and water-holding capabilities. Various technologies for dealing with fish meat, such as freezedrying, spray-drying, extrusion cooking, and high-hydrostatic-pressure processing, have been developed and applied to the seafood industry. However, fish Mf protein is thermally and chemically less stable than that of other vertebrates, and the food functionality is impaired easily as protein denaturation progresses. Therefore, the suppression of protein denaturation during the storage of materials and food processing is important to the manufacturing of high-quality processed seafood. Processing technologies, such as low-temperature storage to keep fish flesh close to freezing (partial freezing), mixing with edible cryoprotectants, and rapid neutralisation of meat by washing with alkaline solution, have been developed for decreasing protein denaturation during processing.Protein glycosylation is an effective method for improving the functional properties of proteins, and various techniques are available to prepare synthetic glycoproteins [3][4][5]8,18]. Recently, the focus has been placed on the neoglycoprotein-synthetic system using the Maillard reaction [14] as an effective method to improve the functional properties of food proteins. The protein glycosylation system is superior to other types of chemical modification for food proteins because it proceeds under mild and safe conditions without the use of chemicals. Food proteins, such as ovalbumin [14], ␤-lactoglobulin [9], phosvitin [26], lysozyme [36], and protamine [21], have been conjugated with various reducing sugars through the Maillard reaction to improve their functional properties such as thermal stability, emulsion-forming ability, antioxidant system to fish meat protein, and succeeded in improving its food functionality. This chapter reviews the enhancing effect of glycosylation through the Maillard reaction on food functionality of fish muscle protein and provides a discussion on the feasibility of using the protein glycosylation technology in the seafood industry. Handbook of Seafood Q uality, Safety and Health ApplicationsEdited by Cesarettin Alasalvar, Fereidoon Shahidi, Kazuo Miyashita and Udaya Wanasundara

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Some physico-chemical properties and structural changes of bovine β-casein upon glycation

Cited by 15 publications

References 0 publications

The effect of glycosylation on emulsifying and structural properties of bovine β-casein

The effect of glycosylation on emulsifying and structural properties of bovine β-casein

Modifications of structures and functions of caseins: a scientific and technological challenge

A New Approach to the Functional Improvement of Fish Meat Proteins

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