Enhancement of acetyl xylan esterase activity on cellulose acetate through fusion to a family 3 cellulose binding module

Enzyme and Microbial Technology
Galina Mai-GisondiEmma R Master

Abstract

The current study investigates the potential to increase the activity of a family 1 carbohydrate esterase on cellulose acetate through fusion to a family 3 carbohydrate binding module (CBM). Specifically, CtCBM3 from Clostridium thermocellum was fused to the carboxyl terminus of the acetyl xylan esterase (AnAXE) from Aspergillus nidulans, and active forms of both AnAXE and AnAXE-CtCBM3 were produced in Pichia pastoris. CtCBM3 fusion had negligible impact on the thermostability or regioselectivity of AnAXE; activities towards acetylated corncob xylan, 4-methylumbelliferyl acetate, p-nitrophenyl acetate, and cellobiose octaacetate were also unchanged. By contrast, the activity of AnAXE-CtCBM3 on cellulose acetate increased by two to four times over 24 h, with greater differences observed at earlier time points. Binding studies using microcrystalline cellulose (Avicel) and a commercial source of cellulose acetate confirmed functional production of the CtCBM3 domain; affinity gel electrophoresis using acetylated xylan also verified the selectivity of CtCBM3 binding to cellulose. Notably, gains in enzyme activity on cellulose acetate appeared to exceed gains in substrate binding, suggesting that fusion to CtCBM3 increases functional...Continue Reading

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Citations

May 12, 2016·Applied Microbiology and Biotechnology·Shun-Hua ZhouGuang-Lei Liu
Oct 6, 2016·Enzyme and Microbial Technology·Fiyinfoluwa A AdesioyeDon A Cowan
Aug 20, 2016·Applied Microbiology and Biotechnology·Haiquan YangFei Xu
Mar 16, 2019·Frontiers in Bioengineering and Biotechnology·Erick Miguel Ramos-MartinezYumiko Sakuragi

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