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 ?
Depending on the substrate, it can be divided into three types: two types (Pectinesterase and polygalacturonase) exist in higher plants and microorganisms, and one type (Pectin Depolymerase) exists in microorganisms, especially in pathogenic microorganisms that infect plants.
However, the literature reports that the use of specific enzymes to degrade the PHB, is the case of PHB depolymerase, that can be secreted by various microorganisms and have an important role in the metabolism of PHB in the environment [2].
Polysaccharide depolymerase is a very important part of the phage tail and many tail spike proteins have endoglycosidase activity by breaking down their polysaccharide receptors through hydrolyzation (40).
Taylor, "Treatment of experimental Escherichia coli infection with recombinant bacteriophage-derived capsule depolymerase," The Journal of Antimicrobial Chemotherapy, vol.
Wang, "Isolation of a Bacteriophage Specific for a New Capsular Type of Klebsiella pneumoniae and Characterization of Its Polysaccharide Depolymerase," PLoS ONE, vol.
Under unfavorable growth conditions Poly AY-hydroxybutyrate (PHB) is accumulated intracellular by many bacteria and the principal enzyme for the degradation of PHB is PHB depolymerase. A number of thermophilic actinomycetes have been screened for PHB degradation on agar plats.
Moreover, a novel poly(3-hydroxybutyrate) (PHB) depolymerase from a thermophilic Streptomyces sp.
Hughes K, Sutherland I, Lones M (1998) Biofilm susceptibility to bacteriophage attack: the role of phage-borne polysaccharide depolymerase. Microbiology Journal 144: 3039-3047
Hydrolysis activity of an extracellular depolymerase from Aspergillus fumigatus with bacterial and synthetic polyesters.
Several amphiphilic proteins have been identified to be located on the surface of in vivo PHA granules including PhaC synthase, poly-beta-hydroxybutyrate depolymerase (PhaZ), and granule-associated protein (PhaP) (44).
Effect of Methanobrevibacter sp MF1 Inoculation on Glycoside Hydrolase and Polysaccharide Depolymerase Activities, Wheat Straw Degradation and Volatile Fatty Acid Concentrations in the Rumen of Gnotobiotically-reared Lambs.
[12] found that P(3HB-co-3HV) degraded faster than P(3HB) in a medium with PHA depolymerase. However, Boyandin et al.