1984
DOI: 10.1111/j.1399-3011.1984.tb02747.x
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Physicochemical properties of maltosyl and glucosaminyl derivatives of beta‐lactoglobulin

Abstract: 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 in… Show more

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Cited by 18 publications
(2 citation statements)
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“…This glycosylation method functionally alters food proteins, resulting in a marked resistance toward destroying the conformation and coagulation of ovalbumin, 2) changes in many physiochemical properties of -lactoglobulin, 3) solubilization of wheat gluten, 4) and the development of outstanding emulsifying properties in lysozymes.…”
mentioning
confidence: 99%
“…This glycosylation method functionally alters food proteins, resulting in a marked resistance toward destroying the conformation and coagulation of ovalbumin, 2) changes in many physiochemical properties of -lactoglobulin, 3) solubilization of wheat gluten, 4) and the development of outstanding emulsifying properties in lysozymes.…”
mentioning
confidence: 99%
“…reduced viscosity, ultraviolet difference spectra, intrinsic fluorescence, and circular dichroism, and functional, e.g. interfacial properties, solubility, foaming and emulsification, properties of the glycosylated derivatives of b-LG were conducted and will be reported in subsequent papers (14)(15)(16)(17).…”
mentioning
confidence: 99%