Recombinant Endopeptidases IdeS and IdeZ and Their Potential Application.

Endopeptidases IdeS and IdeZ (streptococcal virulence factors that specifically cleave IgG heavy chains) are of particular interest because of their potential use in biotechnology, medicine, and veterinary. Genes encoding these enzymes were cloned and expressed in Escherichia coli heterologous expression system (ideS was cloned from a Streptococcus pyogenes collection strain; ideZ from Streptococcus zooepidemicus was synthesized). The 6His-tag was introduced into the amino acid sequence of each endopeptidase, and IdeS and IdeZ were purified by metal affinity chromatography to an apparent homogeneity (according to polyacrylamide gel electrophoresis).

A rapid synthesis of nanofibrillar cellulose/polystyrene composite via ultrasonic treatment.

A new method of the synthesis of nanofibrillar cellulose/polystyrene composite based on ultrasonic treatment of styrene emulsion in cellulose-water solution was elaborated. A new approach does not require additional heating and proposes a significantly faster synthesis (15 min, 45 °C) of the target composite compared to the methods described previously. A comprehensive analysis did not reveal any significant differences between mechanical, physical and biodegradable properties of the composite obtained by ultrasonic method and that one obtained by conventional thermal method, which requires much higher temperature (above 75 °C) and reaction duration (from 3 h).

Influence of NaCl and pH on lysostaphin catalytic activity, cell binding, and bacteriolytic activity.

Peptidoglycan-degrading enzymes are a group of proteins intensively studied as novel antibacterials, with some of them having reached pre-clinical and clinical stages of research. Many peptidoglycan-degrading enzymes have modular organization and consist of a catalytic and a cell wall binding domain. This property has been exploited in enzyme engineering efforts, and many new peptidoglycan-degrading enzymes were generated through domain exchange.

A Simple Protocol for the Determination of Lysostaphin Enzymatic Activity.

Antibacterial lysins are enzymes that hydrolyze bacterial peptidoglycan, which results in the rapid death of bacterial cells due to osmotic lysis. Lysostaphin is one of the most potent and well-studied lysins active against important nosocomial pathogen . Similarly to most other lysins, lysostaphin is composed of enzymatic and peptidoglycan-binding domains, and both domains influence its antibacterial activity.

[Formation of protodioscin and deltoside isomers in suspension cultures of Nepal yam (Dioscorea deltoidea Wall.) cells].

Changes in the content of the furostanol glycosides protodioscin and deltoside, particularly that of the (25S)-isomers of the glycosides, during suspension cultivation of different lines of Nepal yam (Dioscorea deltoidea Wall.) cells of the strain IFR-DM-0.5 has been investigated.