Unusual hydrophobic linker region of beta-glucosidase (BGLII) from Thermoascus aurantiacus is required for hyper-activation by organic solvents

Applied Microbiology and Biotechnology
Jiong HongHidehiko Kumagai

Abstract

A gene encoding a putative beta-glucosidase was isolated from Thermoascus aurantiacus IFO9748 and designated as bgl2. The recombinant enzyme showed beta-glucosidase activity when p-nitrophenyl-beta-glucose (pNP-Glc) was used as substrate. We also found that the enzyme activity was increased in the presence of organic solvents. An addition of 20 % (v/v) 1-octanol resulted in 54-fold higher activity of pNP-Glc hydrolysis, and transglycosylation activity was also found to be activated. The results of tryptophan fluorescence spectral analysis revealed the changes in the tertiary structure of the enzyme in the presence of 1-hexanol that may cause increased enzyme activity. BGLII has a distinctive hydrophobic linker region between N- and C-terminal domains. A chimeric enzyme in which the linker region was substituted by the corresponding region of another beta-glucosidase failed to be activated by organic solvents, suggesting that the hydrophobic linker region may act as a molecular switch in BGLII.

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Citations

Oct 6, 2006·Applied Microbiology and Biotechnology·Jiong HongHidehiko Kumagai
Mar 15, 2012·Applied Biochemistry and Biotechnology·Gurusamy RamaniParamasamy Gunasekaran
Aug 23, 2011·Journal of Bioscience and Bioengineering·Juanjuan LiuYazhong Xiao
Nov 26, 2015·Scientific Reports·Yang YangYazhong Xiao
Jan 17, 2016·International Journal of Biological Macromolecules·Shivangi ChamoliAshok Kumar Verma
Dec 5, 2018·Acta Crystallographica. Section F, Structural Biology Communications·Saeid KarkehabadiMikael Gudmundsson
Dec 12, 2017·The Journal of General and Applied Microbiology·Jing LengHuaming Mao
Oct 10, 2020·Applied Microbiology and Biotechnology·Hanchi ChenXiaolong Chen
Mar 9, 2018·International Journal of Biological Macromolecules·Francesca Anna FuscoDanila Limauro

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