Thermomyces lanuginosus is a real thermophilic fungus and can be isolated worldwide from various substances mainly from compost or soil, thus it is able to grow and utilise numerous complex and natural substrates. This fungus have been reported to produce of high levels of different enzymes (cellulase-free xylanase, lipase, amylolytic enzymes, galactosidases etc.) that are stable up to 60-70 oC for several hours in broad range of pH. These enzymes are appearing to be more thermostable than similar ones from mesophilic fungi. X-ray crystal structures of lipase, xylanase and fatty acid synthase (multienzyme system) from T. lanuginosus now are available in Protein Database Bank. The catalytic triad in active centre of lipase was formed like one from serine protease and is secluded by an α-helical lid. The presence of extra disulfide bridge in structure of xylanase from T. lanuginosus might contribute to thermostability of it. The genes coding xylanase (XylA) or phytase (PhyA) have been cloned and expressed in other protein expression systems, thus giving opportunity to discover and explorer genetical background of T. lanuginosus. Due to intensive development by Novozymes A/S, lipase produced by this fungus is commercially available in two forms: soluble form known as Lipolase® and immobilised form as Lipozyme®. Overall, thermophilic fungus T. lanuginosus has high potential to be good source for production of thermostable enzymes having significant important in biotechnology.
|Title of host publication||Biotechnology of Microbial Enzymes|
|Publisher||Nova Science Publishers, Inc.|
|Number of pages||35|
|Publication status||Published - Sep 1 2012|
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)