Melanocarpus albomyces

Figure 17.5 The protein environment around the Cu centers (gold spheres) of laccase from Melanocarpus albomyces (PDB file IGWO) showing a substrate O2 molecule bound in the trinuciear Cu site [Hakulinen et al., 2002], The protein is depicted in stick representation with atoms in their conventional coloring. (Courtesy of Armand W. J. W. Tepper.) (See color insert.)...

Hakulinen N, Kiiskinen LL, Kruus K, Saloheimo M, Paananen A, Koivula A, Rouvinen J. 2002. Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site. Nature Struct Biol 9 601-605. 

Saraswat, V and Bisaria, V S., Biosynthesis of xylanolytic and xylan-debranching enzymes in Melanocarpus albomyces IIS 68. J Fermentation Bioeng 1997, 83 (4), 352-357. 

Interestingly, an X-ray structure of a laccase derivative from Melanocarpus albomyces reveals what appears to be an O2 ligand spaced between all three T2/T3 copper ions (see Figure 14), although the Cu—O distances reported (2.4 to 2.6 A) are not in line with strong bonding interactions. 

Figure 14 Crystal structure of the T2/T3 cluster site of laccase from Melanocarpus albomyces (after...

FIGURE 5.1 Production of xylanase hy Melanocarpus albomyces IITD3A in 14 L bioreactor with pH cycling. Filled square, xylanase activity filled triangle, pH filled circle, dissolved oxygen and inverted filled triangle, dry mycelia mass (Biswas et al., 2010b). 

Melanocarpus albomyces IITD3A Wheat straw extract 45 7.0 SmF 14 550.0 24 Biswas et al. (2010a)... 

Biswas R, Sahai V, Mishra S, Bisaria VS. (2010a). Development of mutants of Melanocarpus albomyces for hyperproduction of xylanase. Biotechnol Bioprocess Eng, 15, 800-809. 

A carboxylesterase (EC 3.1.1.1) from T. fusca [8, 86] and a steryl esterase (EC 3.1.1.13) from Melanocarpus albomyces [59] have also shown activity with PET oligomers and fabrics. The enzyme from M. albomyces with high specificity for fatty acid esters of sterols increased the hydrophilicity of PET fabrics. The highly hydrophobic serine hydrolase from T. fusca with a catalytic triad composed of serine, glutamic acid, and histidine hydrolyzed CTR and PET nanoparticles. The esterase showed high specificity towards short and middle chain-length fatty acyl esters of p-nitrophenol. In addition, p-nitrobenzyl esterases from Bacillus subtilis and B. licheniformis that hydrolyzed short chain dialkylphthalates and PET nanoparticles have been reported [74, 87]. 

Kontkanen H, Saloheimo M, Pere J, Miettinen-Oinonen A, Reinikainen T (2(X)6) Characterization of Melanocarpus albomyces steiyl esterase produced in Trichoderma reesei and modification of fibre products with the enzyme. AppI Microbiol Biotechnol 72 696-704... 

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