Mutanase Enzyme from RSP02: Characterization and Application as a Biocontrol Agent.

Mutanases are enzymes that have the ability to cleave α-1,3 linkages in glucan polymer. In the present investigation, mutanase enzyme purified from the culture filtrate of was evaluated for biofilm degradation and antimicrobial activity against pathogenic fungi along with enzyme kinetics, activation energies, pH and thermal stability. Biochemical and molecular characterization depicted that the enzyme showed optimum activity at pH 5.

Complete Genome Sequence of α-1,3-Glucanase-Producing Strain RSP-02.

A mutanase (α-1,3 glucanase)-producing bacterial strain of Paracoccus mutanolyticus was isolated from soil samples rich in cellulosic waste. Here, we report the whole-genome sequencing and annotation of P. mutanolyticus, which has a genome size of around 3.

The "excluding" suture technique for surgical closure of ventricular septal defects: A retrospective study comparing the standard technique.

Background: Conventional methods of closure of ventricular septal defects involve placement of sutures 4-5 mm from the posterior inferior margin. This study compares the conventional method with an alternative technique wherein sutures are placed along the edge of the defect thereby "excluding" the conduction system and the tensor apparatus of the tricuspid valve from the suture line.

Materials And Methods: Between January 2013 and January 2016, 409 consecutive patients were retrospectively reviewed and divided into two matched groups.

Formulation and Evaluation of Controlled Release Floating Microballoons of Stavudine.

The aim of this study was to formulate and evaluate stavudine floating microballoons for controlled drug release. Initially, the drug-loaded low-density granular pellets were prepared with hydroxypropyl methylcellulose E5 grade and by using isopropyl alcohol as a granulating fluid. Further, the low-density granular pellets were subjected to microencapsulation by an emulsion evaporation technique using ethyl cellulose 7 cps and Eudragit S 100 as coating polymers and 1% w/v polyethylene glycol 400 as aqueous phase.

Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12.

Bacterial peptidoglycan (PG or murein) is a single, large, covalently cross-linked macromolecule and forms a mesh-like sacculus that completely encases the cytoplasmic membrane. Hence, growth of a bacterial cell is intimately coupled to expansion of murein sacculus and requires cleavage of pre-existing cross-links for incorporation of new murein material. Although, conceptualized nearly five decades ago, the mechanism of such essential murein cleavage activity has not been studied so far.