Title of article
Protein extraction optimisation, characterisation, and functionalities of protein isolate from bitter melon (Momordica charantia) seed
Author/Authors
Horax، نويسنده , , Ronny and Hettiarachchy، نويسنده , , Navam and Kannan، نويسنده , , A. and Chen، نويسنده , , Pengyin Chen، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2011
Pages
6
From page
545
To page
550
Abstract
Bitter melon seeds are a rich source of protein. Optimum conditions for protein extraction from the seeds, determined using a response surface design, were at a pH 9.0 and 1.3 M NaCl. Soy protein isolate (SPI) was included for comparison. Surface hydrophobicity of bitter melon seed protein isolate (BMSPI) (690) was significantly higher than that of SPI (399). Electrophoretograms of BMSPI showed bands at 40 and 55 kDa, and at 22, 25, and 35 kDa in non-reducing and reducing buffers, respectively. BMSPI had most of the essential amino acids and hence could be considered as a high quality protein. BMSPI had a single denaturation temperature (113.1 °C) while SPI had two denaturation temperatures (78.0 and 94.8 °C). The proteins exhibited U-shaped curves with solubilities ranging from 62.0% to 67.5% for BMSPI and 86.7% to 90.1% for SPI at pH ⩾ 7.0. BMSPI had lower emulsifying activity (0.36 vs. 0.73), foaming capacity (39.6 vs. 61.0 ml), and foaming stability (21.5 vs. 25.5 min) than had SPI.
Keywords
Bitter melon seed , functionality , Protein , characterisation
Journal title
Food Chemistry
Serial Year
2011
Journal title
Food Chemistry
Record number
1963076
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