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1.
Crit Rev Food Sci Nutr ; 56(7): 1108-25, 2016 May 18.
Article in English | MEDLINE | ID: mdl-24824044

ABSTRACT

The products formed by glycosylation of food proteins with carbohydrates via the Maillard reaction, also known as conjugates, are agents capable of changing and improving techno-functional characteristics of proteins. The Maillard reaction uses the covalent bond between a group of a reducing carbohydrates and an amino group of a protein. This reaction does not require additional chemicals as it occurs naturally under controlled conditions of temperature, time, pH, and moisture. Moreover, there is growing interest in modifying proteins for industrial food applications. This review analyses the current state of art of the Maillard reaction on food protein functionalities. It also discusses the influence of the Maillard reaction on the conditions and formulation of reagents that improve desirable techno-functional characteristics of food protein.


Subject(s)
Dietary Proteins/chemistry , Food , Maillard Reaction , Polysaccharides/chemistry , Chemical Phenomena , Dietary Carbohydrates , Glycosylation , Hot Temperature
2.
Carbohydr Polym ; 119: 210-8, 2015 Mar 30.
Article in English | MEDLINE | ID: mdl-25563962

ABSTRACT

Protein-polysaccharide conjugates often display improved techno-functional properties when compared to their individual involved biomolecules. α-Lactalbumin:acacia gum (α-la:AG) conjugates were prepared via Maillard reaction by the dry-heating method. Conjugate formation was confirmed using results of absorbance, o-phthalaldehyde test, sodium dodecyl sulfate-polyacrilamide gel electrophoresis (SDS-PAGE) and size exclusion chromatography. Techno-functional properties (emulsifying characteristics, solubility, and thermal stability) were evaluated for α-la, α-la/AG mixtures and α-la:AG conjugates. Conjugate thermal stability was improved compared to pure α-la treated at the same conditions of conjugate formation. Response surface methodology was used to establish models to predict solubility and emulsifying activity as functions of the salt concentration, pH and reaction time. α-la:AG conjugate solubility is affected in a complex manner by the three factors analyzed. Emulsifying activity index (EAI) of α-la is significantly affected by pH, while the α-la:AG EAI is affected by the three analyzed factors. Both solubility and EAI are maximized with pH 8.0, NaCl concentration of 0.3 mol L(-1) and two days of Maillard reaction.


Subject(s)
Emulsions/chemistry , Gum Arabic/chemistry , Lactalbumin/chemistry , Temperature , Chromatography, Gel , Electrophoresis, Polyacrylamide Gel , Hydrogen-Ion Concentration , Maillard Reaction , Protein Stability , Salts/chemistry , Solubility , Time Factors
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