Endoxylanase and endoxylanase inhibition activities in the grain of winter rye cultivars

作者：Vidmantiene Daiva^*; Juodeikiene Grazina

来源：Zemdirbyste-Agriculture, 2010, 97(1): 3-10.

• rye
• extractable protein
• endoxylanase
• inhibition activity
• growing conditions

The study was designed to investigate the effect of variety, cultivation site and crop year on the endoxylanase activity in the winter rye varieties 'Joniai', 'Matador', 'Recrue, 'Fernando' and 'Picasso', and the newly developed hybrids LIA 426, LIA 391 and L1A 463. Partial purified soluble rye proteins were tested for their inhibition activity against commercial glycoside hydrolase (GH) family 11 endoxylanases of Trichoderma reesei and Thermomyces lanuginosus. The apparent endoxylanase activity values in the different rye samples varied between 0.31 and 1.42 U g(-1) grain. The endoxylanase activity levels largely depended on the variety and weather conditions before harvest. The inhibition activities in the different rye samples against T lanuginosus and T reesei enzymes varied between 19.0 and 33.4, and 11.4 and 24.8 IU 100 mg(-1) of dry wholemeal, respectively, and were linearly related. The endoxylanase inhibition activity was mainly dependent on genetic background and was less affected by the growing conditions and precipitation levels. The newly developed rye hybrids seem to have nearly related endoxylanase inhibition activity irrespective of the environmental conditions and genetics. The T. lanuginosus enzyme was found to be much more inhibited by the rye inhibitors. The rye protein fractions with inhibition activity contain the components with the molecular masses of about 10-11, 14 and 29-31 kDa. The differences in functionality of commercial enzymes and in screening these enzymes for the application to the rye-based processes can be explained according to the obtained results.

• 出版日期2010