Sabanci University, Biological Sciences and Bioengineering, Istanbul, Turkey.
Biotechnol Prog. 2011 Sep-Oct;27(5):1257-63. doi: 10.1002/btpr.663. Epub 2011 Jul 19.
Trichoderma reesei cellulases are important biocatalysts for a wide range of industrial applications that include the paper, feed, and textile industries. T. reesei endoglucanase 1 (egl1) was successfully expressed as an active and stable catalyst in Pichia pastoris for the first time. Codon optimization was applied to egl1 of T. reesei to enhance its expression levels in P. pastoris. When compared with the originally cloned egl1 gene of T. reesei, the synthetic codon optimized egl1 gene (egl1s) was expressed at a higher level in P. pastoris. Batch fermentations of both clones with the same copy number under controlled conditions indicated that codon optimized EGI enzyme activity increased to 1.24 fold after 72 h of methanol induction. Our research indicated that P. pastoris is a suitable host for cellulase production.
里氏木霉纤维素酶是广泛应用于造纸、饲料和纺织等工业领域的重要生物催化剂。里氏木霉内切葡聚糖酶 1（egl1）首次成功在巴斯德毕赤酵母中作为一种活性和稳定的催化剂进行表达。为了提高其在巴斯德毕赤酵母中的表达水平，对里氏木霉 egl1 进行了密码子优化。与里氏木霉原本克隆的 egl1 基因相比，合成的密码子优化的 egl1 基因（egl1s）在巴斯德毕赤酵母中的表达水平更高。在相同拷贝数的条件下，对两个克隆进行分批发酵，结果表明，经甲醇诱导 72 小时后，密码子优化的 EGI 酶活性增加了 1.24 倍。我们的研究表明，巴斯德毕赤酵母是一种适合生产纤维素酶的宿主。
