Bioinformatics and enzymatics investigation of Trametes laccase for optical biosensing application

• Published in: Journal of materials science Vol. 54; no. 6; pp. 4970 - 4983
• Main Authors: Wang, Yang, Chen, Zhi-Hui
• Format: Journal Article
• Language: English
• Published: New York Springer US 01.03.2019; Springer; Springer Nature B.V
• Subjects: absorbance; Bioinformatics; Bonds (Securities); Characterization and Evaluation of Materials; Chemistry and Materials Science; Classical Mechanics; Computational biology; Crystallography and Scattering Methods; disulfide bonds; enzyme activity; enzyme stability; Enzymes; Fluorescence; freeze-thaw cycles; glycosylation; Investigations; Laccase; Materials for Life Sciences; Materials Science; Optical properties; Oxidases; oxidation; Polymer Sciences; Solid Mechanics; Stability; Trametes; Fungal Laccases; CAZy Database; Laccase Production; Optical Biosensing Applications; Yeast Malt Extract Agar (YMA)
• ISSN: 0022-2461; 1573-4803
• DOI: 10.1007/s10853-018-03187-9

Laccase has recently drawn a considerable attention as a promising tool for optical biosensing application, mainly due to its attractive intrinsic optical properties. The discovery of a laccase with great enzyme stability is the principal step for enzyme-based optical biosensing application in in vitro environments. In this paper, we found that Trametes sp . SQ1 laccase retained more than 150% activity after storage in different conditions for 96 h, and the laccase activity was not affected by freeze–thaw. The reduced form of enzyme showed a new maximal increase in absorbance peak at 400 nm, while the fluorescence intensity of the oxidized form of enzyme was much stronger than that of the reduced enzyme. Therefore, Trametes sp . SQ1 laccase with good stability and optical properties will be a competitive candidate for optical biosensing application. Moreover, bioinformatics analysis on Trametes laccases revealed that the enzymes may be modified by N-glycosylation and have intermolecular disulfide bond for forming functional oligomer, which plays a role in stabilizing enzyme function. The results indicate that Trametes laccases are able to be with good stability. It will provide a guide in searching stable laccases for optical biosensing application.