Physical and Molecular Properties of Egg-white Lipid Films

• Published in: Journal of food science Vol. 64; no. 5; pp. 860 - 864
• Main Authors: Handa, A., Gennadios, A., Hanna, M.A., Weller, C.L., Kuroda, N.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.09.1999; Institute of Food Technologists; Wiley Subscription Services, Inc
• Subjects: Applied sciences; Biological and medical sciences; Chemistry; Compounding ingredients; edible films; Egg and egg product industries; egg white; Exact sciences and technology; Food industries; Food science; Fundamental and applied biological sciences. Psychology; Lipids; oleic acid; Plasticizers; Polymer industry, paints, wood; protein films; Proteins; sulfhydryl groups; Technology of polymers; Ovalbumin; Alanine; Lipids; Egg white; Physical properties; Tensile strength; Ethylene oxide polymer; Extension; Steam permeability; Plasticizer; Edible film; Disulfide bond; Lysine; Oleic acid; Biopolymer; Egg product; Lysophospholipid; Animal protein; Unsaturated fatty acid; Rheological properties
• ISSN: 0022-1147; 1750-3841
• DOI: 10.1111/j.1365-2621.1999.tb15928.x

Polyethylene glycol‐plasticized films were cast from alkaline (pH 11.25), heated (45 °C for 20 min), aqueous egg white (EW) solutions, with or without (10% or 20% w/w of EW) milkfat (two fractions), oleic acid, or egg yolk lysophospho‐lipid (LPL). The lipids did not reduce (P > 0.05) film water vapor permeability. Oleic acid increased (P < 0.05) tensile strength and elongation, and surface sulfhydryl group (SH) concentrations in EW solutions. Oleic acid probably increased negative charges on EW proteins, unfolding protein chains, and exposing SH groups. LPL also slightly increased (P < 0.05) surface SH concentrations in non‐heated mixtures. Electrophoretic patterns suggested oleic acid interactions with ovalbumin, ovotransferrin, and lysozyme. No lysinoalanine was in film‐forming mixtures based on lysine measurements.