Gelling Properties of Globin-Succinylated Globin Conjugates

• Published in: NIPPON SHOKUHIN KOGYO GAKKAISHI Vol. 40; no. 6; pp. 437 - 440
• Main Authors: MIYAGUCHI, Yuji, NAKAMURA, Toyoo, TAKABATAKE, Satoru, YONEKURA, Masami, TSUTSUMI, Masakazu
• Format: Journal Article
• Language: English
• Published: Japanese Society for Food Science and Technology 1993
• ISSN: 0029-0394
• DOI: 10.3136/nskkk1962.40.437

Two kinds of conjugate were made from globin (G) and succinylated globin (SG); the one (CMHT) was prepared by β-mercaptoethanol-hydrogen peroxide treatment of these proteins, the other (CUT) by urea treatment of them, and the gelling properties of these conjugates were investigated. In the case of CMHT, the pH range of gel formation became wider as the compounding ratio of G was high. For example, though the gel-forming pH was only 2.0 when the ratio of G and SG was 3:7, the gel was formed in the pH 2.0 to 3.5 region when G and SG were 9:1. On the other hand, CUT formed gel at limited pH when the ratio of G and SG were 7:3 or 9:1 respectively. The gel of the conjugates was transparent in strong acidic pH region. In addition, the transparence of the gel increased with increasing the compounding ratio of G. In the equal ratio of G and SG, CMHT formed the strongest gel at pH 2.0. However, the gel strength of CMHT gel showed the maximum value at pH 3.0 in 9:1 ratio of G and SG. Although strong gel was formed at pH 2.0 when G and SG was 3:7 ratio, the values of the gel strength of CUT gel were low as a whole.