Features and applications of bilirubin oxidases

Abstract

Discovered in 1981 by Tanaka and Murao (Agric Biol Chem 45:2383-2384, 1981), bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu(+/2+) ions. It catalyzes the oxidation of bilirubin to biliverdin, hence the classification of bilirubin oxidase, and has been primarily used in the determination of bilirubin in serum and thereby in the diagnostic of jaundice. Unlike laccases, the most studied MCOs, BODs display a high activity and stability at neutral pH, a high tolerance towards chloride anions and other chelators, and for some species, a high thermal tolerance. Therefore, BODs could potentially be an alternative to laccase which are so far mainly restricted to applications in acid media. Because of growing interest in BODs for numerous applications under mild pH conditions, based on the number of patents and publications published in the last 5 years, here I will summarize the available data on the biochemical properties of BODs, their occurrence, and their possible biotechnological use in (1) the field of Healthcare for the elaboration of biofuel cells or bilirubin sensors or (2) the field of environmentally desirable applications such as depollution, decolorization of dyes, and pulp bleaching.

Biohydrogen for a New Generation of H2/O2 Biofuel Cells: A Sustainable Energy Perspective

“…[38,39] Furthermore, BODs are quite stable at neutral pH. [68,69] They have been identified in various fungi and bacteria, and can exhibit chloride, urate, dithiothreitol (DTT) and ethylenediaminetetraacetic acid (EDTA) tolerance. Some of them also present thermostable properties.…”

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

“…Since its conception in 1978 where DET between a multicopper oxidase (MCO) (laccase) and a carbon electrode afforded enzymatic O 2 reduction, DET has evolved into an established ET pathway for many oxidoreductases, most commonly (but not limited to) laccase, bilirubin oxidase (BOx), nitrate reductase, hydrogenase and fructose dehydrogenase [31][32][33][34].…”

Increasing the catalytic activity of Bilirubin oxidase from Bacillus pumilus: Importance of host strain and chaperones proteins

“…They catalyze the four electron reduction of O 2 to water without releasing H 2 O 2 . This feature makes them the perfect candidate to elaborate O 2 reducing cathode in glucose/O 2 biofuel cells (Mano, 2012;Mano and Edembe, 2013;Rasmussen et al, 2016) which may power in the near future implanted medical devices (Falk et al, 2013;Leech et al, 2012). Up to now, this reaction was mostly catalyzed by laccases but Bilirubin oxidases (BODs) are getting more attention because they have the advantage to be more active and stable in physiological conditions (Beyl et al, 2011;Kavanagh et al, 2008).…”