Genes Coding Industrially Relevant Enzymes in Fungi: Isolation and Protein Engineering of Laccases

نویسنده

  • Vincenza Faraco
چکیده

Fungi are sources of several enzymes susceptible of applications in many and diverse industrial segments such as food, beverage, textile, leather, paper and pulp, animal feed and fuel industry. These microorganisms are safe, display efficient growth under industrial production conditions and are able to secrete ample quantities of enzymes. The main fungal enzymes having industrial relevance include cellulases, xilanases, amylases, proteases, lipases, laccases, etc. Among these, laccases are blue multicopper oxidases (MCO), using the distinctive redox ability of copper ions to catalyze the oxidation of a wide range of aromatic substrates concomitantly with the reduction of molecular oxygen to water. Catalytic properties of laccases and their low substrate specificity allow their wide application in several industrial sectors such as pulp and paper, textile and cosmetic industries, for detoxification and decoloration of sewage, in organic synthesis, for degradation of xenobiotics and bioremediation, in production of wood-fiber plates, wood blocks, and cardboard without using toxic linkers, for production of detergents and in elaboration of biosensors.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Comparison of biochemical properties of recombinant endoglucanase II of Trichoderma reesei in methylotrophic yeasts, Pichia pastoris and Hansenula polymorpha

Bioconversion of cellulosic material into bioethanol needs cellulase complex enzymesthat contain endoglucanase, exoglucanase and beta glucosidase. One of the most important organisms that produce cellulases is the filamentous fungi, Trichoderma reesei which able to secrete large amounts of different cellulases. These enzymes are probably the most widely used cellulases industrially, however, th...

متن کامل

Phylogenomic analyses reveal the diversity of laccase-coding genes in Fonsecaea genomes

The genus Fonsecaea comprises black yeast-like fungi of clinical relevance, including etiologic agents of chromoblastomycosis and cerebral phaeohyphomycosis. Presence of melanin and assimilation of monoaromatic hydrocarbons and alkylbenzenes have been proposed as virulence factors. Multicopper oxidase (MCO) is a family of enzymes including laccases, ferroxidases and ascorbate oxidases which are...

متن کامل

Engineering Laccases: In Search for Novel Catalysts

Laccases (p-diphenol oxidase, EC 1.10.3.2) are blue multicopper oxidases that catalyze the reduction of dioxygen to water, with a concomitant oxidation of small organic substrates. Since the description at the end of the nineteenth century of a factor catalyzing the rapid hardening of the latex of the Japanese lacquer trees (Rhus sp.) exposed to air laccases from different origins (plants, fung...

متن کامل

Computational Identification of Micro RNAs and Their Transcript Target(s) in Field Mustard (Brassica rapa L.)

Background: Micro RNAs (miRNAs) are a pivotal part of non-protein-coding endogenous small RNA molecules that regulate the genes involved in plant growth and development, and respond to biotic and abiotic environmental stresses posttranscriptionally.Objective: In the present study, we report the results of a systemic search for identifi cation of new miRNAs in B. rapa using homology-based ...

متن کامل

Determination of lignin-modifying enzymes (LMEs) in Hyphodermella species using biochemical and molecular techniques

White-rot basidiomycetes are one of the most important lignolytic microorganisms. These fungi have been reported to secrete three main classes of lignin degrading enzymes: lignin peroxidases (LiPs), manganese peroxidases (MnPs) and laccases. In this study, for the first time the lignin degrading capability of two plant pathogens i.e. Hyphodermella rosae and H. corrugata was evaluated using both...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره 12  شماره 

صفحات  -

تاریخ انتشار 2011