ArticleBMC biotechnology2017
Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase.
Article in BMC biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 15 citations in OpenAlex.
- Rational Design of a Foldon-Derived Heterotrimer Guided by Quantitative Native Mass Spectrometry.Journal of the American Chemical Society · 2025Article
- Bacillus subtilis: a universal cell factory for industry, agriculture, biomaterials and medicine.Microbial cell factories · 2020Review
- Improvement in catalytic activity and thermostability of a GH10 xylanase and its synergistic degradation of biomass with cellulase.Biotechnology for biofuels · 2019Article
- Insight into the functional roles of Glu175 in the hyperthermostable xylanase XYL10C-ΔN through structural analysis and site-saturation mutagenesis.Biotechnology for biofuels · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundEffective 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 a foldon domain at the C-terminus of the enzymes via elastin-like polypeptides (ELPs). The foldon domain comprises 27 residues and can forms trimers with high stability.
resultsLichenase and xylanase can hydrolyze lichenan and xylan to produce value added products and biofuels, and they have great potentials as biotechnological tools in various industrial applications. We took them as the examples and compared the kinetic parameters of the engineered trimeric enzymes to those of the monomeric and wild type ones. When compared with the monomeric ones, the catalytic efficiency (k
conclusionThe trimeric lichenase and xylanase induced by foldon have advantages in the catalytic performances. Besides, they were easier to purify with increased purification fold and decreased the loss of activities compared to their corresponding monomeric ones. Trimerizing of the target enzymes triggered by the foldon domain could improve their activities and facilitate the purification, which represents a simple and effective enzyme-engineering tool. It should have exciting potentials both in industrial and laboratory scales.
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