Assay for Laccase activity by microcalorimetry: Laccase was extracted from China lacquer of Rhus vernicifera

A new and sensitive catalytic resonance scattering spectral assay for the detection of laccase using guaiacol as substrate

“…Under the optimal condition, the working curve between laccase activity (U laccase/mL) and DI was drawn, with a regression equation of DI = 734.0 Ulaccase -9.7, linear range of 0.10-1.2 U/mL, a correlation coefficient of 0.9920, and a detection limit of 0.05 U/mL. Compared with the reported assays (5,(7)(8)(9)12,13), as shown in Table 2, this RS assay was more sensitive. In addition, the substrate is commonly used and easy to obtain.…”

“…It is necessary to develop a rapid and sensitive assay to detect laccase activity in screening for the fungi. So far, the most commonly used method for the detection of laccase activity has been spectrophotometric assay (3–7); additional methods include flow injection technique (8), microcalorimetry (9), O 2 measuring method (10), fluorescence spectrometry (11), electrochemistry (12,13) and atomic absorption spectrometry (14). On the basis of the laccase catalytic effect on the color reaction between guaiacol and 3‐methyl‐benzothiazolinonehydrazone, an initial rate method (7) was reported for the assay of 5–30 µmol/L laccase; this method was simple but not sensitive.…”

High Level Secretion of Laccase (LccH) from a Newly Isolated White-Rot Basidiomycete, Hexagonia hirta MSF2

“…Laccases (benzenediol: oxygen oxidoreductase EC 1.10.3.2) are glycosylated blue oxidases, that oxidizes wide range of substrates including aromatic amines, diamines, diphenols, polyphenols, and highly recalcitrant environmental pollutants with simultaneous reduction of molecular oxygen to water ( Baldrian, 2006 ; You et al, 2013 ). Although laccases from plants, fungi, prokaryotes, arthropods ( Wang et al, 2000 ), and archaea ( Uthandi et al, 2010 ) are widely described, white-rot fungi are the most predominant group that are known for high level secretion of laccases ( Wu et al, 2010 ; Yang et al, 2013b ). Due to their capability to oxidize a wide range of compounds, laccases in the last decade have been considered as potential enzyme for industrial applications such as cellulose pulping, dye decolourization, detoxification of phenolics from industrial effluents, biosensor applications, food and beverage industries, cosmetic industry and nano biotechnology, and bioremediation of soils ( Soden and Dobson, 2001 ; Morozova et al, 2007 ; Shraddha et al, 2011 ; Diwaniyan et al, 2012 ; Virk et al, 2012 ; Ba et al, 2013 ; Christopher et al, 2014 ).…”

Microfluidic devices and true‐color sensor as platform for glucose oxidase and laccase assays

“…Monitoring enzyme activity is especially important in medical diagnosis or for the development of new pharmaceutical products 9. Microtiter plate formats 10, 11 or continuous flow devices 12, 13 have been previously integrated with microcalorimetric, spectrophotometric, fluorescence methods and used for glucose oxidase (GOx) 11, 14 laccase (Lac) 15, cellobiose dehydrogenase 16 and adenylyl cyclase 17 activity screening. Recently, (bio)electrochemical sensors have been designed for the monitoring the enzyme activity such as β‐galactosidase 18 and Lac 19.…”