Optimal parameters for laccase-mediated destaining of Coomassie Brilliant Blue R-250-stained polyacrylamide gels

Jie Yang; Xiaodan Yang; Xiuyun Ye; Juan Lin

doi:10.1016/j.dib.2016.01.029

Optimal parameters for laccase-mediated destaining of Coomassie Brilliant Blue R-250-stained polyacrylamide gels

Data Brief. 2016 Jan 29:7:1-7. doi: 10.1016/j.dib.2016.01.029. eCollection 2016 Jun.

Authors

Jie Yang¹, Xiaodan Yang¹, Xiuyun Ye¹, Juan Lin¹

Affiliation

¹ Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou University, Fuzhou, Fujian 350116, China.

Abstract

The data presented in this article are related to the research article entitled "Destaining of Coomassie Brilliant Blue R-250-stained polyacrylamide gels with fungal laccase" [1]. Laccase is a class of multicopper oxidases that can catalyze oxidation of recalcitrant dyestuffs. This article describes optimal parameters for destaining of polyacrylamide gels, stained with Coomassie Brilliant Blue R-250, with laccase from basidiomycete Cerrena sp. strain HYB07. Effects of laccase activity, mediator type and concentration, temperature and time on destaining of polyacrylamide gels were evaluated with respect to gel background intensity and protein band signals, and the optimal destaining effects were obtained with 15 U mL(-1) laccase and 2 μM ABTS at 37 °C after 2 h.

Keywords: ABTS, 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonate); ACE, acetosyringone; BSA, bovine serum albumin; CBBR, Coomassie Brilliant Blue R-250; Coomassie Brilliant Blue R-250; Destaining; HBT, 1-hydroxybenzotriazole; Laccase; Polyacrylamide gel; SYA, syringic acid; SYD, syringaldehyde.