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The effect of lupin protein isolation procedures on the emulsifying and water binding capacity of a meat‐protein system
Author(s) -
MANRIQUE J.,
THOMAS M. A.
Publication year - 1976
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.1976.tb00739.x
Subject(s) - water holding capacity , extraction (chemistry) , chromatography , isoelectric point , chemistry , protein isolate , protein purification , precipitation , protein precipitation , water extraction , isoelectric focusing , food science , biochemistry , enzyme , physics , meteorology
Summary A study on the emulsifying capacity and water binding capacity of lupin protein (isolates and concentrates) using various isolation procedures was carried out. These procedures included protein extraction in single or double step in alkaline or acid conditions by the use of a wet or dry milling technique. Different ion conditions were also used. For comparison, soya bean and lupin protein were extracted through a co‐precipitation procedure. Protein extraction by wet milling and then precipitation and drying at isoelectric pH promoted water binding capacity, while dry milling and alkaline extraction enhanced the emulsifying capacity. Protein co‐precipitation and ion environmental conditions are other factors influencing the emulsifying capacity and water binding capacity. The proper choice of these parameters will determine the optimum conditions for emulsifying and water binding capacity of a protein isolate or concentrate.