@article{gerber_heitmann_joyce_buchert_siika-aho_1999, title={Adsorption of hemicellulases onto bleached kraft fibers}, volume={67}, ISSN={["0168-1656"]}, DOI={10.1016/S0168-1656(98)00163-1}, abstractNote={The presence of a cellulose binding domain was the main factor which influenced the adsorption of two Trichoderma reesei mannanases and a Trichoderma longibrachiatum xylanase onto bleached kraft fibers. The mannanase containing the binding domain adsorbed to a much greater extent than the mannanase and xylanase without binding domains. Once-dried fibers exhibited lower hemicellulase adsorption than the never-dried fibers. The adsorption onto once-dried fibers was only 30–50% the amount adsorbed onto virgin fibers. Adjustment of the ionic strength and pH of treatment was used to modify the charge on the fibers. Ionic strength had opposite effects on mannanase and mannanase core adsorption. Mannanase adsorption increased at high ionic strengths, while the mannanase core adsorption decreased. An increase in pH and fiber charge significantly enhanced the adsorption of xylanase.}, number={1}, journal={JOURNAL OF BIOTECHNOLOGY}, author={Gerber, PJ and Heitmann, JA and Joyce, TW and Buchert, J and Siika-aho, M}, year={1999}, month={Jan}, pages={67–75} }
 @article{gerber_joyce_heitmann_siika-aho_buchert_1997, title={Adsorption of a Trichoderma reesei endoglucanase and cellobiohydrolase onto bleached Kraft fibres}, volume={4}, ISSN={["1572-882X"]}, DOI={10.1023/A:1018444008305}, number={4}, journal={CELLULOSE}, author={Gerber, PJ and Joyce, TW and Heitmann, JA and Siika-Aho, M and Buchert, J}, year={1997}, month={Dec}, pages={255–268} }
 @article{gerber_heitmann_joyce_1997, title={Purification and characterization of xylanases from Trichoderma}, volume={61}, ISSN={["1873-2976"]}, DOI={10.1016/S0960-8524(97)00052-7}, abstractNote={Xylanase preparations free of cellulase contamination are often required for applications in the pulp and paper industry. Xylanases from Trichoderma have been purified and characterized in an effort to better understand the behavior of the various components of the xylanolytic system in order to optimize their effect. However, purification and characterization of xylanases from Trichoderma species are still incomplete. This review organizes current techniques for xylanase purification and examines the properties of xylanases that have been previously characterized. Problems with assays, lyophilizing, gel permeation behavior, gel electrophoresis and developing are also noted. From this review, a strategy for the isolation of an endoxylanase from a commercial preparation of T. longibrachiatum is developed.}, number={2}, journal={BIORESOURCE TECHNOLOGY}, author={Gerber, PJ and Heitmann, JA and Joyce, TW}, year={1997}, month={Aug}, pages={127–140} }