期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 55, 期 2, 页码 439-445出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf061002r
关键词
alpha-zein; protein emulsifying properties; protein deamidation; protein hydrolysis; surface hydrophobicity; circular dichroism; dynamic light scattering
Different deamidation conditions for the Z19 alpha-zein were studied in order to find the best conditions for the development of the emulsifying properties. Alkaline deamidation was chosen, and the effects on the peptide bond cleavage, secondary structure, emulsifying properties, and surface hydrophobicity were studied. The Z19 alpha-zein was deamidated by using 0.5 N NaOH containing 70% ethanol at 70 degrees C for 12 h. A deamidation degree (DD) of 60.6 +/- 0.5%, and a degree of hydrolysis (DH) of 5 +/- 0.5% were achieved. Analysis by far-UV circular dichroism showed that the denaturation was mainly promoted by the high temperature used during the incubation. The adequate balance between the DD and the DH results in an effective emulsifying property improvement for the Z19 alpha-zein. Thus, after the deamidation treatment, the surface hydrophobicity decreased from 9.5 x 10(4) +/- 6.8 x 10(3) to 46 x 10(4) +/- 2.1 x 10(3), and the emulsion stability increased from 18 +/- 0.7% to 80 +/- 4.7% since the oil globules stabilized by the modified protein were smaller (57.7 +/- 5.73 nm) and more resistant to coalescence than those present in the native protein emulsions (1488 +/- 3.92 nm).
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