Laccase Case Study

Fig: 1. Mode of Action of Laccase
Despite widespread use of laccases, demand for the laccases were increasing every year and so the gap between production and demand is widening. Keeping in view the industrial importance of laccases, we are more and more focusing on discovering novel substrate to meet out the prevailing demand. Therefore the study was aimed at strain improvement, exploration of two different substrate for solid state fermentation, process optimization for production of laccase and purification. Mostly plants and fungi are important resources for laccase (Thakker et al., 1992). In the last decade, there have been reports stating laccase was found in some bacteria such as S.lavendulae, S.cyaneus,
In plants, laccase plays a role in lignifications whereas in fungi it has been implicated in delignification, sporulation, pigment production, fruiting body formation, and plant pathogenesis (Thurston et al., 1994; Yaver et al., 2001). These biocatalysts may have advantageous properties compared to classical laccases; an example is CotA, which has a much higher thermo stability than fungal laccases (Martins et al., 2002). Claus (2003), stated that only few bacterial laccases have been studied, through rapid progress in genome analysis suggests that these enzymes are also widespread in bacteria. The most well-known representative is CotA from Bacillus subtilis, an endospore coat protein with high thermostability (Hullo et al., 2001). Other laccases have been found in Pseudomonas maltophila (Isono and Hoshino, 1989), P.syringae (copA) (Cha and Chooksey, 1991), Azospirillum lipoferum (Givaudan et al., 1993), Xanthomonas campesteris (Lee et al., 1994), Bacillus sp. (mnx G) (Van Waasbergen et al., 1996), B.sphaericus (Claus and Filip, 1997), P.fluorescences GB-1 (Okazaki et al., 1997), Aquifex aeolicus (Deckert et al., 1998), P.putida GB1 (Brouwers et al., 1999), A. lipoferum (Diamantidis et al., 2000),