Thermostability of endo-1 , 4-β-xylanase II from Trichoderma reesei studied by electrospray ionization Fourier-transform ion cyclotron resonance MS , hydrogen / deuterium-exchange reactions and dynamic light scattering

@inproceedings{JanneThermostabilityOE,
  title={Thermostability of endo-1 , 4-β-xylanase II from Trichoderma reesei studied by electrospray ionization Fourier-transform ion cyclotron resonance MS , hydrogen / deuterium-exchange reactions and dynamic light scattering},
  author={J Janne and Juha Rouvinen and Matti S. A. Leisola and Ossi Turunen and Pirjo Vainiotalo}
}
Endo-1,4-β-xylanase II (XYNII) from Trichoderma reesei is a 21 kDa enzyme that catalyses the hydrolysis of xylan, the major plant hemicellulose. It has various applications in the paper, food and feed industries. Previous thermostability studies have revealed a significant decrease in enzymic activity of the protein at elevated temperatures in citrate buffer [Tenkanen, Puls and Poutanen (1992) Enzyme Microb. Technol. 14, 566–574]. Here, thermostability of XYNII was investigated using both… CONTINUE READING