A Comparison Study on Functional Properties of Mungbean Protein and Chemically Modified Mungbean Protein

분리 녹두 단백질과 이를 화학적으로 수식화한 단백질간의 식품학적 기능성 비교

  • Sohn, Kyung-Hee (Dept. of Food & Nutr., College of Home Economics, Yonsei Univ) ;
  • Min, Sung-Hee (Dept. of Food & Nutr., College of Home Economics, Yonsei Univ) ;
  • Park, Hyun-Kyung (Dept. of Food & Nutr., College of Home Economics, Yonsei Univ) ;
  • Park, Jin (Dept. of Food & Nutr., College of Home Economics, Yonsei Univ)
  • 손경희 (연세대학교 생활과학대학 식품영양학과) ;
  • 민성희 (연세대학교 생활과학대학 식품영양학과) ;
  • 박현경 (연세대학교 생활과학대학 식품영양학과) ;
  • 박진 (연세대학교 생활과학대학 식품영양학과)
  • Published : 1991.08.01

Abstract

This study was carried out in order to investigate the change of protein functionalities such as foaming and emulsifying properties by succinylation of protein isolates. Succinylated and unsuccinylated munghean protein isolates were tested for finding out the effects of pH, heat treatment and sodium chloride concentration on the solubility, emulsion capacity, emulsion stability, foaming capacity, and foam stability. The results are summarized as follows: 1. Succinylation enhanced the solubility of MPI except at pH 4.5. When heated, succinylation greatly increased the solubility of succinylated MPI above $60^{\circ}C$. With the addition of NaCl, succinylation increased the solubility of MPI at acidic condition. 2. Emulsion capacity of succinylated MPI showed the lowest value at pH 7 and higher values at acidic and alkaine condition. when succinylated MPI was heated, emulsion capacity showed the highest at $80^{\circ}C$. With NaCl was added, emulsion capacity of succinylated MPI lincreased at pH 7, 9 or 11 decreased at pH 3 except addition of 1.0M NaCl. 3. Emulsion stability of MPI and succinylated MPI showed the highest at pH 4.5. Succinylation enhanced the emulsion stability of MPI at acidic condition. 4. The foaming capacity of MPI was increased at pH 3, 7 or 9 by succinylation. 5. When heated, foam stability of MPI and succinylated MPI showed the highest at pH 4.5 and at pH 11, respectively. When heated, both proteins showed the highest stability at $100^{\circ}C$.

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