TY - JOUR
T1 - Hydrolyzed wheat gluten suppresses transglutaminase-mediated gelation but improves emulsification of pork myofibrillar protein
AU - Xiong, Youling L.
AU - Agyare, Kingsley K.
AU - Addo, Kwaku
PY - 2008/10
Y1 - 2008/10
N2 - The influence of 15-h chymotrypsin-hydrolyzed wheat gluten (GH) on microbial transglutaminase (MTGase)-mediated interaction, gelation and emulsification of pork myofibrillar protein isolate (MPI) was investigated at two ionic strengths (0 M and 0.6 M NaCl) and pH 6.5. MTGase treatments in 0 M NaCl solution decreased the size of myosin heavy chain through deamidation, but this was inhibited by GH or in 0.6 M NaCl where myosin polymerization dominated. Stabilization of MPI (thermal transitions) by the MTGase treatment was also diminished (P < 0.05) by the presence of GH at both ionic strengths. These GH-induced MPI physicochemical changes greatly weakened the ability of MTGase to promote MPI thermal gelation (gel storage modulus, P < 0.05), especially at 0.6 M NaCl, which was shown to result from reduced protein aggregation. However, GH improved (P < 0.05) emulsifying properties of MPI, regardless of MTGase treatment.
AB - The influence of 15-h chymotrypsin-hydrolyzed wheat gluten (GH) on microbial transglutaminase (MTGase)-mediated interaction, gelation and emulsification of pork myofibrillar protein isolate (MPI) was investigated at two ionic strengths (0 M and 0.6 M NaCl) and pH 6.5. MTGase treatments in 0 M NaCl solution decreased the size of myosin heavy chain through deamidation, but this was inhibited by GH or in 0.6 M NaCl where myosin polymerization dominated. Stabilization of MPI (thermal transitions) by the MTGase treatment was also diminished (P < 0.05) by the presence of GH at both ionic strengths. These GH-induced MPI physicochemical changes greatly weakened the ability of MTGase to promote MPI thermal gelation (gel storage modulus, P < 0.05), especially at 0.6 M NaCl, which was shown to result from reduced protein aggregation. However, GH improved (P < 0.05) emulsifying properties of MPI, regardless of MTGase treatment.
KW - Emulsification
KW - Gelation
KW - Hydrolyzed wheat gluten
KW - Microbial transglutaminase
KW - Myofibrillar protein
UR - http://www.scopus.com/inward/record.url?scp=49649095219&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=49649095219&partnerID=8YFLogxK
U2 - 10.1016/j.meatsci.2008.02.005
DO - 10.1016/j.meatsci.2008.02.005
M3 - Article
C2 - 22063363
AN - SCOPUS:49649095219
SN - 0309-1740
VL - 80
SP - 535
EP - 544
JO - Meat Science
JF - Meat Science
IS - 2
ER -