Transglutaminase cross-linking of whey/myofibrillar proteins and the effect on protein gelation

Transglutaminse (TGase)-catalyzed interactions of whey (WPI)/myofibrillar (MPI) protein isolates were investigated under 5 conditions: (1) ionic strengths; (2) calcium/ethylenediaminetetra-acetic acid (EDTA); (3) enzyme:substrate ratio; (4) WPI:MPI ratio; and (5) preheating of WPI (80°C). TGase treatments of MPI in distilled water converted myosin heavy chain and actin into lower-molecular-weight polypeptides. The reaction, accelerated by the presence of WPI but diminished by NaCl, was completely reversed upon extended incubation. There was no visible WPI/MPI cross-linking; and the enzyme:substrate or WPI:MPI ratio, preheating, calcium, and EDTA did not influence the enzyme reaction. TGase treatment did not alter the melting pattern of WPI/MPI mixtures, but markedly enhanced their thermal gelling ability.