Poly(aspartic acid) (PAA) hydrolases and PAA biodegradation: current knowledge and impact on applications.
Appl Microbiol Biotechnol
; 100(4): 1623-1630, 2016 Feb.
Article
en En
| MEDLINE
| ID: mdl-26695157
ABSTRACT
Thermally synthesized poly(aspartic acid) (tPAA) is a bio-based, biocompatible, biodegradable, and water-soluble polymer that has a high proportion of ß-Asp units and equivalent moles of D- and L-Asp units. Poly(aspartic acid) (PAA) hydrolase-1 and hydrolase-2 are tPAA biodegradation enzymes purified from Gram-negative bacteria. PAA hydrolase-1 selectively cleaves amide bonds between ß-Asp units via an endo-type process, whereas PAA hydrolase-2 catalyzes the exo-type hydrolysis of the products of tPAA hydrolysis by PAA hydrolase-1. The novel reactivity of PAA hydrolase-1 makes it a good candidate for a biocatalyst in ß-peptide synthesis. This mini-review gives an overview of PAA hydrolases with emphasis on their biochemical and functional properties, in particular, PAA hydrolase-1. Functionally related enzymes, such as poly(R-3-hydroxybutyrate) depolymerases and ß-aminopeptidases, are compared to PAA hydrolases. This mini-review also provides findings that offer an insight into the catalytic mechanisms of PAA hydrolase-1 from Pedobacter sp. KP-2.
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Base de datos:
MEDLINE
Asunto principal:
Biopolímeros
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Serina Endopeptidasas
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Ácido Aspártico
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Pedobacter
Idioma:
En
Revista:
Appl Microbiol Biotechnol
Año:
2016
Tipo del documento:
Article