actinomycosis/protease

In the course of systematic screening program for bioactive actinomycetes, an alkaline protease producing halophilic strain Actinopolyspora sp. VITSDK2 was isolated from marine saltern, Southern India. The strain was identified as Actinopolyspora based on its phenotypic and phylogenetic characters.

Two types of alkaline serine proteases were isolated from the culture filtrate of an alkalophilic actinomycete, Nocardiopsis dassonvillei OPC-210. The enzymes (protease I and protease II) were purified by acetone precipitation, DEAE-Sephadex A-50, CM-Sepharose CL-6B, Sephadex G-75 and

An alkaline protease from salt tolerant alkaliphilic actinomycetes, Nocardiopsis alba strain OK-5 was purified to homogeneity by 27 and 13 fold with a yield of 35 and 13% using two-steps and one-step method, respectively. The purification methods involved hydrophobic interaction on phenyl sapharose

Four hundred and fifteen actinomycete strains were screened for hyaluronidase activity in two plate assays media. In the first one, using hyaluronic acid as substrate and bovine serum albumin (BSA) to help precipitation of the nondegraded substrate, only strain 594 and hyaluronidase control were

This work was aimed at studying the interactions during the growth of Actinomyces rimosus producing proteases and Actinomyces violocinereus which did not synthesize secreted proteolytic enzymes. The production of proteases in the association of the actinomycetes was shown to be stimulated by

Proteases with the thrombolytic activity were studied in 212 strains of actinomycetes isolated from different soils of the Soviet Union. The cultures belonged to the genera Micromonospora, Nocardia and Streptomyces. Proteases were synthesized by 41% of the studied actinomycetes and some of their

Thermoactinomycetes vulgaris is a thermophilic actinomycetes growing optimally at 50 degrees C and Streptomyces albus, S. coelicolor, S. fasciculus and S. olivochromogenes are thermophilically disposed transition species of actinomycetes, which have optimum biomass at 40 degrees C. The acid/alkaline

The repression of alkaline protease synthesis from alkaliphilic actinomycete was studied by using glucose, peptone, yeast extract, KH2PO4 and amino acids; tyrosine, tryptophan, lysine, and arginine. There was a critical limit of stimulation of enzyme production by these components. Crude components

An alkaline serine protease from a newly isolated salt-tolerant alkaliphilic actinomycetes, Brachystreptospora xinjiangensis OM-6 was purified with 35- and 26-fold purification and 47% and 22% yield employing two steps and one step methods, respectively. The enzyme was quite stable at 80 °C in 30%

Exploiting the vast diversity of soil samples, we have isolated three actinomycetes strains producing alkaline protease inhibitors API-I (242 U/ml). API-II (116 U/ml) and API-III (186 U/ml). The inhibitors exhibited different properties in their molecular nature and in their pH and temperature

Cloning and expression of recombinant alkaline serine proteases from two salt tolerant alkaliphilic actinomycetes strains: OM-6 (EU710555.1) and OK-5 (HM560975) were successfully obtained in mesophilic host, Escherichia coli. The positive clones harboring protease genes were selected on the basis of

An alkaline protease from salt-tolerant alkaliphilic actinomycetes, Nocardiopsis alba OK-5 was purified by a single-step hydrophobic interaction chromatography and characterized. The purified protease with an estimated molecular mass of 20 kDa was optimally active at 70 °C in 0-3 M NaCl and 0-100 mM

Bacterial biofilms are associated with chronic infections due to their resistance to antimicrobial agents. Staphylococcus aureus is a versatile human pathogen and can form biofilms on human tissues and diverse medical devices. To identify novel biofilm inhibitors of S. aureus, the supernatants from

In the course of a screening program directed toward the isolation and evaluation of inhibitors of carboxyl (acid) proteinases, we have found 0.39% of the investigated strains of microorganisms as producers of pepsin inhibitors. In more than 1543 strains which were isolated from various geographical

A xylanase-coding gene (xynAHJ3, 1,104 bp) was cloned from Lechevalieria sp. HJ3 harbored in a saline soil sampled from Heijing town, aka the "town of salt", on the famous "Silk Route of the South". The gene encodes a 367-residue polypeptide (XynAHJ3) with the highest identity of 74.0 % with the