depolymerase

de·pol·y·mer·ase

(dē-pol'i-mĕr-ās),
Name used originally, before hydrolytic action was understood, for an enzyme catalyzing the hydrolysis of a macromolecule to simpler components. See: nuclease.

de·pol·y·mer·ase

(dē-pol'i-mĕr-ās)
An enzyme catalyzing the hydrolysis of a macromolecule to simpler components.
See: nuclease
References in periodicals archive ?
Moreover, a novel poly(3-hydroxybutyrate) (PHB) depolymerase from a thermophilic Streptomyces sp.
Degradation rate of HA/PHBV nanofibrous films was investigated, it was found that in the presence of polyhydroxybutyrate depolymerase, the degradation rate was very fast.
A key bacterial enzyme called capsule depolymerase (CapD) anchors the capsule to the cell surface.
A breakthrough in PHB molecular biology was the presentation of the first three-dimensional X-ray structure of a type II extracellular single-domain depolymerase crystal.
Phenol, Polyhydroxyalkanoate, depolymerase, electron microscope.
In this process, the PHB-degrading bacteria and fungi excrete extracellular depolymerases that hydrolyze the solid polymer into water-soluble monomers and oligomers that are consumed as nutrients by the microorganisms [10].
Selection of the microbial source for pectinase production depends on several features, such as the type of culture (solid-state or submerged fermentation), number and type of the produced pectinases (esterases, hydrolytic depolymerases and eliminative depolymerases), pH and thermal stability of the enzymes [1,10-13].
Among the depolymerases, polygalacturonase is the major enzyme with a hydrolytic function and lyases (or transeleminases) which cleaves glycosidic bonds forming unsaturated product[DELTA](4,5-D-galacturonate) through transelimination reaction [34].
Increasing amounts of the 4-hydroxy- repeating unit decreases the well known brittleness of P(3HB) and leads to clear, tough films with good susceptibility to both PHA depolymerases and lipases for biodegradation.