In vitro digestibility and functional properties of chemically modified casein

Sen, Lourminia C.; Lee, Honson S.; Feeney, Robert E.; Whitaker, John R.

doi:10.1021/jf00104a032

Cited by 30 publications

(26 citation statements)

References 7 publications

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“…The digestibility of an Cisl-casein film with chymotrypsin was measured according to the method of Sen et al 6 -TGase, C(sl-casein film prepared without transglutaminase; +TGase, C(sl -casein film prepared with transglutaminase. The concentration of C(sl-casein was 5%.…”

Section: Digestibility Of the Filmmentioning

confidence: 99%

α_s1-Casein Film Prepared Using Transglutaminase

Motoki

Aso

Seguro

et al. 1987

Agricultural and Biological Chemistry

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Section: Digestibility Of the Filmmentioning

confidence: 99%

α_s1-Casein Film Prepared Using Transglutaminase

Motoki

Aso

Seguro

et al. 1987

Agricultural and Biological Chemistry

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“…Representative protein conjugates with synthetic polymers include the conjugates of proteins and polyethylene glycol (Inada et al, 1995;Veronese, 2001) and immobilized enzymes (Taylor, 1991;Liang et al, 2000). On the other hand, many studies to improve the functions of proteins by conjugation with various saccharides were also conducted: alkylation (Nieto & Palacian, 1983;Sen et al, 1981) esterification , amidation , deamidation (Matsudomi et al, 1985;Wu et al, 1976), lipophilization (Akita & Nakai, 1990a;1990b), covalent attachment of gluconic acid (Kitabatake et al, 1985), cross-linking with transglutaminase (Nio et al, 1985;Motoki et al, 1987) and so on. An overview of the studies on protein-saccharide conjugates shows that most of the studies have been carried out by attachment or elimination of low-molecular weight molecules.…”

Section: Introduction: What Is Neoglycoprotein ?mentioning

confidence: 99%

Functional Improvements in Food Proteins in Multiple Aspects by Conjugation with Saccharides: Case Studies of .BETA.-Lactoglobulin-Acidic Polysaccharides Conjugates.

Hattori

2002

FSTR

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Many studies on the conjugates of proteins and saccharides (neoglycoproteins) have been carried out over the past 20 years to improve the function of proteins. However, most have been carried out by attachment or elimination of low-molecular weight molecules for single purposes. The structure-function relationship of the conjugates has not been well understood, and little is known about the improvement of proteins by conjugation with polysaccharides. We sought to achieve functional improvements in food proteins in multiple aspects by conjugation with charged polysaccharides. We chose bovine ␤-lactoglobulin (␤-LG) as the target protein for improvement of the function and attached carboxymethyl dextrans (CMDs) of different molecular weight (10, 40, 70 and 162 kDa) covalently. After conjugation and purification, we explored the structure of the ␤-LG-CMD conjugates to prove that we could prepare conjugates while maintaining the native-like structure of protein molecule. By conjugation with CMDs, enhancement of thermal stability, improvement in the emulsifying properties and reduction of immunogenicity of ␤-LG could be achieved. Increases in the CMD content and net charge were viewed as the major factors in the improved emulsifying properties. Conjugation with high saccharide content using polysaccharides of higher molecular weight is believed to be effective in reduced immunogenicity of ␤-LG.

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“…Since the changes in viscosity of glycosylated derivatives of b-LG were small compared to the viscosity of denatured b-LG, the tertiary structures of glycosylated derivatives of b-LG were apparently only partially unfolded. The viscosity of other chemically modified proteins was also affected by modification (3, 24,25). The large increase in viscosity of succinylated arachin was attributed to increased electronegativity, dissociation of the oligomeric structure and alterations in the secondary conformations of the proteins (3).…”

Section: Viscosity Of Glycosylated Derivatives Of Beta-lactoglo Bulinmentioning

confidence: 99%

“…The ultraviolet difference spectra of several chemically modified proteins were affected by the extent of modification and type of group attached (1,3,24,25). The difference spectra of succinylated arachin indicated that some of the buried aromatic amino acids were exposed to water and that some of the tyrosyl residues were polarized (3).…”

Section: Ultraviolet Difference Spectra Of Glycosylated Derivatives Omentioning

confidence: 99%

“…The difference spectra of aspartylcasein indicated tyrosyl residues were exposed to more polar environments than in native casein (24). The difference spectra of alkylated derivatives of casein indicated that some tyrosyl and some tryptophyl residues were exposed to more polar environments (25). Thus, chemical modification of proteins can cause the environments of aromatic amino acid residues to become more polar and cause more of these residues to be exposed to ultraviolet radiation.…”

Section: Ultraviolet Difference Spectra Of Glycosylated Derivatives Omentioning

confidence: 99%

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Physicochemical properties of maltosyl and glucosaminyl derivatives of beta‐lactoglobulin

Waniska

Kinsella

1984

International Journal of Peptide and Protein Research

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Maltosyl and glucosaminyl derivatives of beta‐lactoglobulin (b‐LG) were analyzed for their physicochemical properties: reduced viscosity, ultraviolet difference spectra, intrinsic fluorescence, hydrophobicity and circular dichroism. The viscosity of these derivatives increased as the mass of the carbohydrates covalently linked to b‐LG increased. The ultraviolet difference spectra and the intrinsic fluorescence of these proteins revealed that the microenvironments of aromatic amino acid residues of b‐LG were increasingly exposed to the surface of the protein as the extent of modification increased; and the polarity of these residues also increased as modification increased. The hydrophobicities of M‐b‐LG derivatives decreased as the extent of modification increased while the hydrophobicities of G‐b‐LG derivatives were relatively unchanged. The circular dichroic analysis of these proteins indicated that the ordered secondary structures of the extensively modified derivatives of b‐LG were partially unfolded. Thus, the carbohydrates covalently linked to b‐LG altered many physiochemical properties. These physicochemical changes of b‐LG apparently resulted from an alteration of forces stabilizing the structure of the protein.

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In vitro digestibility and functional properties of chemically modified casein

Cited by 30 publications

References 7 publications

α_s1-Casein Film Prepared Using Transglutaminase

α_s1-Casein Film Prepared Using Transglutaminase

Functional Improvements in Food Proteins in Multiple Aspects by Conjugation with Saccharides: Case Studies of .BETA.-Lactoglobulin-Acidic Polysaccharides Conjugates.

Physicochemical properties of maltosyl and glucosaminyl derivatives of beta‐lactoglobulin

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In vitro digestibility and functional properties of chemically modified casein

Cited by 30 publications

References 7 publications

αs1-Casein Film Prepared Using Transglutaminase

αs1-Casein Film Prepared Using Transglutaminase

Functional Improvements in Food Proteins in Multiple Aspects by Conjugation with Saccharides: Case Studies of .BETA.-Lactoglobulin-Acidic Polysaccharides Conjugates.

Physicochemical properties of maltosyl and glucosaminyl derivatives of beta‐lactoglobulin

Contact Info

Product

Resources

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α_s1-Casein Film Prepared Using Transglutaminase

α_s1-Casein Film Prepared Using Transglutaminase