Gelation and gel properties of soybean glycinin in a transglutaminase-catalyzed system

Gelation of glycinins as catalyzed by transglutaminase was investigated. The surface lysine and glutamine residues of glycinin increased with heating. In the gelation of native and heat-treated glycinins catalyzed by transglutaminase, the formation of epsilon-(gamma-glutamyl)lysyl cross-links was pr...

Full description

Saved in:
Bibliographic Details
Published in:Journal of agricultural and food chemistry 1994-01, Vol.42 (1), p.159-165
Main Authors: Kang, Il Jun, Matsumura, Yasuki, Ikura, Koji, Motoki, Masao, Sakamoto, Hiroko, Mori, Tomohiko
Format: Article
Language:English
Subjects:
ACTIVIDAD CATALITICA
ACTIVIDAD ENZIMATICA
ACTIVITE CATALYTIQUE
ACTIVITE ENZYMATIQUE
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Biological and medical sciences
COLLOIDE
COLOIDES
Food industries
Fundamental and applied biological sciences. Psychology
GELIFICACION
GELIFICATION
PROTEINAS
PROTEINE
REACCIONES QUIMICAS
REACTION CHIMIQUE
SOJA
TRAITEMENT THERMIQUE
TRANSFERASAS
TRANSFERASE
TRATAMIENTO TERMICO
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Gelation of glycinins as catalyzed by transglutaminase was investigated. The surface lysine and glutamine residues of glycinin increased with heating. In the gelation of native and heat-treated glycinins catalyzed by transglutaminase, the formation of epsilon-(gamma-glutamyl)lysyl cross-links was proportional to the amount of their surface lysine and glutamine residues. Both the acidic and basic subunits participated in the gelation of heat-treated glycinins, while most of the basic subunits did not in the case of native glycinin. Glycinin heated in the presence and absence of N-ethylmaleimide exhibited linear strands of aggregates and branched strands or small aggregates, respectively, and formed hard and elastic gels having a well cross-linked network or soft and viscous gel shaving a poor network structure, respectively. Modification of lysine or glutamine residues of glycinin affected viscoelastic properties of the corresponding gels. From these results, it was concluded that gel properties may be controlled not only by the amounts of cross-links formed and lysine and glutamine residues available for transglutaminase reaction but also by the nature of substrate protein
ISSN:0021-8561
1520-5118
DOI:10.1021/jf00037a028