Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins. Relationship with dough properties and bread-making quality

STEFFOLANI ME; RIBOTTA PD; PEREZ GT; LEON AE

JOURNAL OF CEREAL SCIENCE (PRINT)

ACADEMIC PRESS LTD-ELSEVIER SCIENCE LTD

Año: 2010 vol. 51 p. 366 - 373

0733-5210

Glucose oxidase (Gox), transglutaminase (TG), and pentosanase (Pn) were investigated for their effecton bread quality. The changes introduced in wheat protein by the action of these enzymes were analysedto explain dough behaviour. Gox treatment decreased free sulphydryl groups (SHf), increasedglutenin macropolymer contents, and modified the electrophoretic pattern of protein fractions. Goxmodified mainly albumin, globulin, and glutenin, forming large protein aggregates. These modificationsexplained the high strength of the dough and the low bread specific volume of samples with Gox. TGtreatment modified solubility in SDS of protein and decreased glutenin macropolymer content.However, it formed large protein aggregates. The new cross-linking bonds introduced by this enzymewere different to SeS bonds and, consequently, the dough was less extensible and showed highresistance. Pn treatment increased water soluble pentosan content. Moreover, in these samplesa tendency to increase SHf content was observed. In addition, Pn increased protein solubility in isopropanol,which indicates that the reduction of pentosans size decreases steric impediment of insolublepentosans, thus increasing interaction among protein and making their extraction easier. These changesat the microscopic level allowed explaining the formation of softer dough and the production of higherspecific volume in breads with Pn.