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Developmental changes in storage proteins and peptidyl prolyl cis–trans isomerase activity in grains of different wheat cultivars

Dutta, Tanima, Kaur, Harsimran, Singh, Sandeep, Mishra, Akanksha, Tripathi, Jayant K., Singh, Narpinder, Pareek, Ashwani, Singh, Prabhjeet
Food chemistry 2011 v.128 no.2 pp. 450-457
cultivars, flowering, glutenins, dough, protein subunits, molecular weight, storage modulus, gliadin, gluten, polyacrylamide gel electrophoresis, principal component analysis, wheat, isomerases, wheat protein, enzyme activity, protein deposition, storage proteins, variability
In the present study, storage proteins from five different wheat cultivars were extracted, fractionated and evaluated for their accumulation at different stages of development. SDS–PAGE analysis revealed that the accumulation of high molecular weight glutenin subunits was cultivar and stage dependent. However, low molecular weight glutenin subunits’ accumulation was not altered significantly after 16days post anthesis in any of the cultivars. The rheological parameters (storage- and loss-modulus) of dough and gluten showed close association with either gliadins or glutenins. Peptidyl prolyl cis–trans isomerase (PPIase) activity, measured at different stages of grains development, showed variability with both the developmental stage and cultivar, and appeared to be primarily due to cyclophilins. Principal component analysis revealed the association of PPIase activity with either gliadin or total proteins, suggesting their significant role in the deposition of storage proteins in wheat.