Assistant Professor of Chemistry
Penn State Mont Alto
Although the nature provides us with abundant plant materials, utilizating them effectively has been lagging behind due to the rigid crystalline structure of cellulose in such biomass. Cellobiohydrolase I (CBH-I) cellulase can bound to cellulose microfibril and hydrolyze cellulose chain into cellobiose. This process can be used in the pretreatment of fermentation, which eventually produces ethanol as a petroleum substituent. However, such an enzymatic hydrolysis has not been commercialized because of its low turnover rate. The cellulase catalytic mechanism, which is necessary for protein engineering to acchieve an improved enzyme performance, remains elusive today. We are investigating on the behavior of CBH-I from T. reesei by computer modelling. This research will lead to a direct understanding towards the functions of different domains of this protein and can provide a visual guide for site mutagenesis experiments.