While diversity studies and screening for enzyme activities are important elements of understanding fungal roles in the soil ecosystem, extracting purifying target from cellular system is also required to characterize enzyme. This is, particular, necessary before developing industrial-scale production. In present study, partially purified α-amylase was obtained strains Pseudogymnoascus sp. Anta...

Abstract Enzymes, the driving biocatalysts in living organisms, are typically not suited for large-scale industrial use. In last decade, enzyme engineering has evolved into key technology to design tailor-made enzymes chemical and pharmaceutical applications. We highlight current trends biocatalysis based on outstanding examples from industry.

We discuss, from an industrial point of view, the scope and possibilities of recombinant DNA technology for "diagnostic enzyme" production and application. We describe the construction of enzyme-overproducing strains and show how to simplify downstream processing, increase product quality and process profitability, improve diagnostic enzyme properties, and adjust enzymes to harsh assay conditio...

Although nature evolves its catalysts over millions of years, enzyme engineers try to do it a bit faster. Enzyme active sites provide highly optimized microenvironments for the catalysis of biologically useful chemical transformations. Consequently, changes at these centers can have large effects on enzyme activity. The prediction and control of these effects provides a promising way to access ...

Production of β-glucosidase from Fusarium oxysporum was investigated during degradation of some cellulosic substrates (Avicel, α-cellulose, carboxymethyl cellulose (CMC), and methylcellulose). Optimized production of β-glucosidase using the cellulosic substrate that supported highest yield of enzyme was examined over 192 h fermentation period and varied pH of 3.0-11.0. The β-glucosidase produce...

Recent advances in molecular and structural biology have improved the availability of virtually any biocatalyst in large quantity and have also provided an insight into the detailed structure-function relationships of many of them. These results allowed the rational exploitation of biocatalysts for use in organic synthesis. In this context, extremophilic enzymes are extensively studied for thei...

The thermal and solvent tolerance of enzymes is highly important for their industrial use. We show here that the enzyme lipase from Rhizopus oryzae exhibits exceptionally high thermal stability and high solvent tolerance and even increased activity in acetone when immobilized onto a graphene oxide (GO) nanosupport prepared by Staudenmaier and Brodie methods. We studied various forms of immobili...

Industrial enzymes are often immobilized via chemical cross-linking onto solid supports to enhance stability and facilitate repeated use in bioreactors. For starch-degrading enzymes, immobilization usually places constraints on enzymatic conversion due to the limited diffusion of the macromolecular substrate through available supports. This study describes the one-step immobilization of a highl...

In industrial fermentation processes, the yeast Saccharomyces cerevisiae is commonly used for ethanol production. However, it lacks the ability to ferment pentose sugars like d-xylose and l-arabinose. Heterologous expression of a xylose isomerase (XI) would enable yeast cells to metabolize xylose. However, many attempts to express a prokaryotic XI with high activity in S. cerevisiae have failed...

Thermostability is a characteristic of most of the enzymes available for bulk industrial usage. Thermophilic microorganisms are of special interest as a source of novel thermostable enzymes. A total of 50 bacterial strains, isolated from local hot springs and ash samples were screened for the extracellular enzyme production including amylase, lipase, esterase, cellulase and β-galactosidase. As ...