Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase

作者: Xinzhe Wang , Huihua Ge , Dandan Zhang , Shuyu Wu , Guangya Zhang

DOI: 10.1186/S12896-017-0380-3

关键词: Wild typeCombinatorial chemistryCatalytic efficiencyHydrolysisBiochemistryBiologyCatalysisMonomerEnzymeXylanaseProtein engineering

摘要: Effective and simple methods that lead to higher enzymatic efficiencies are highly sough. Here we proposed a foldon-triggered trimerization of the target enzymes with significantly improved catalytic performances by fusing foldon domain at C-terminus via elastin-like polypeptides (ELPs). The comprises 27 residues can forms trimers high stability. Lichenase xylanase hydrolyze lichenan xylan produce value added products biofuels, they have great potentials as biotechnological tools in various industrial applications. We took them examples compared kinetic parameters engineered trimeric those monomeric wild type ones. When ones, efficiency (k cat /K m ) lichenase increased 4.2- 3.9- fold. constant 1.8- fold 5.0- than their corresponding wild-type counterparts. Also, specific activities 149% 94% Besides, recovery 12.4% 6.1% during purification process using ELPs non-chromatographic tag. possible reason is reduce transition temperature ELPs. induced advantages performances. were easier purify decreased loss Trimerizing triggered could improve facilitate purification, which represents effective enzyme-engineering tool. It should exciting both laboratory scales.

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