Leptospirosis is a worldwide zoonosis caused by Leptospira interrogans. This study was conducted toevaluate serologic and bacteriologic findings of leptospirosis in clinically-suspected cows. 380 sera and 33urine samples were collected from 6 industrial dairy farms in Tehran suburb, from December 2004 to June2005. The prevalence of disease was determined by microscopic agglutination test (MAT),...

We report here the genome assembly of a psychrotolerant bacterium, Chryseobacterium polytrichastri ERMR1:04, which secretes cold-active proteases. The bacterium was isolated from a pristine location, the East Rathong Glacier in the Sikkim Himalaya. The 5.53-Mb genome provides insight into the cold-active industrial enzyme and adaptation in the cold environment.

An l-aminopeptidase of Pseudomonas putida, used in an industrial process for the hydrolysis of d,l-amino acid amide racemates, was purified to homogeneity. The highly l-enantioselective enzyme resembled thiol reagent-sensitive alkaline serine proteinases and was strongly activated by divalent cations. It possessed a high substrate specificity for dipeptides and alpha-H amino acid amides, e.g., ...

We report the isolation of a keratinolytic-producing Bacillus subtilis strain and the characterization of the exceptional dehairing properties of its subtilisin-like keratinase. This enzyme can be an alternative to sodium sulfide, the major pollutant from tanneries, and may completely replace it. Its unique nonactivity upon collagen enhances its industrial potential.

Here we report the draft genome sequence of Streptomyces exfoliatus DSMZ 41693, which includes a gene encoding a poly(3-hydroxyoctanoate) depolymerase, an enzyme which can be used for the industrial synthesis of chiral (R)-3-hydroxyalkanoic acids. In addition, the genome carries numerous genes involved in the biosynthesis of secondary metabolites, including polyketides and terpenes.

In this review, a comprehensive discussion exclusively on bacterial xylanases; their gene organization; different factors and conditions affecting enzyme yield and activity; and their commercial application have been deliberated in the light of recent research findings and extensive information mining. Improved understanding of biological properties and genetics of bacterial xylanase will enabl...

A novel esterase was identified through functional screening of a metagenomic library in Escherichia coli obtained from Antarctic desert soil. The 297-amino-acid sequence had only low (<29%) similarity to a putative esterase from Burkholderia xenovorans. The enzyme was active over a temperature range of 7 to 54 degrees C and at alkaline pH levels and is a potential candidate for industrial appl...

This study mainly aims to find the optimal conditions for immobilizing a non-commercial β-glucosidase from Aspergillus niger via cross-linked enzyme aggregates (CLEAs) by investigating effect of cross-linking agent (glutaraldehyde) concentration and soy protein isolate/enzyme ratio (or spacer/enzyme ratio) on catalytic performance through central composite rotatable design (CCRD). The influence...

Nanoporous gold (referred to as np-Au or NPG) has emerged over the past 10 years as a new support for enzyme immobilization. The material has appealing features of ease of preparation, tunability of pore size, high surface to volume ratio, and compatibility with multiple strategies for enzyme immobilization. The np-Au material is especially of interest for immobilization of redox enzymes for bi...

The core of an enzyme molecule is its active site from the viewpoints of both academic research and industrial application. To reveal the structural and functional mechanism of an enzyme, one needs to know its active site; to conduct structure-based drug design by regulating the function of an enzyme, one needs to know the active site and its microenvironment as well. Given the atomic coordinat...