Lipophilization of β‐lactoglobulin: Effect on Hydrophobicity, Conformation and Surface Functional Properties

Abstract

8-Lactoglobulin was chemically modified by attaching different levels of stearic acid, and the effect on hydrophobic@, emulsifying and foaming properties was investigated. Incorporation of the hydrophobic ligands led to increased hydrophobic interactions, resulting in a decreasing solubility with extent of incorporation. Surface hydrophobicity measurements showed that the two fluorescence probes 8 anilinonaphthalene-1-sulfonate (ANS) and cis-parinaric acid (CPA) used were not equivalent. Some improvement of emulsifying and foaming properties was observed at low and medium levels of incorporation which decreased as the extent of fatty acid attachment further increased. High solubility and ANS surface hydrophobicity were both needed for the best emulsifying properties.

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

“…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.…”

Efeito da hidrólise tríptica e do pH sobre as propriedades funcionais do plasma bovino

“…A determinação da hidrofobicidade superficial foi realizada segundo a técnica descrita por AKITA & NAKAI [1]. A proteína foi solubilizada em tampão (fosfato dissódico a 0,02mol/L e ácido cítrico a 0,01mol/L), na faixa de 3,0 a 8,0, em concentrações de 1, 5, 8, 10 e 20mg de proteína/100mL.…”

Chemical lipophilization of soy protein isolates and wheat gluten

“…A close look at the literature reveals many ways of binding hydrophobic groups or modifying protein hydrophobicity, for instance acylation by fatty acid and N-hydroxysuccinimide esters [4][5][6], acylation by acetic, succinic and citraconic anhydrides [7][8][9], acylation by fatty acid anhydrides [10,11], reductive alkylation [12], plastein reactions inserting hydrophobic amino acids [13] or alcohols [14]. Obviously, the nature and length of the chains of the hydrophobic groups bound to proteins are directly linked to the final structural and functional properties of so modified proteins.…”