Purification and Characterization of Poly(aspartic acid) Hydrolase from Sphingomonas sp. KT-1

Poly(aspartic acid) (PAA) hydrolase was purified from Sphingomonas sp. KT-1 (JCM10459). The purified hydrolase degraded thermally synthesized PAA to oligomers. The molecular mass of PAA hydrolase was 30 kDa and the isoelectric point was 8.9. The optimum values of pH and temperature for PAA degradati...

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Veröffentlicht in:	Biomacromolecules 2001, Vol.2 (4), p.1155-1160
Hauptverfasser:	Tabata, Kenji, Kajiyama, Mariko, Hiraishi, Tomohiro, Abe, Hideki, Yamato, Ichiro, Doi, Yoshiharu
Format:	Artikel
Sprache:	eng
Schlagworte:	Hydrogen-Ion Concentration Isoelectric Point Molecular Weight Peptide Fragments - analysis Peptides - metabolism Serine Endopeptidases - chemistry Serine Endopeptidases - isolation & purification Serine Endopeptidases - metabolism Sphingomonas Sphingomonas - enzymology Substrate Specificity
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Zusammenfassung:	Poly(aspartic acid) (PAA) hydrolase was purified from Sphingomonas sp. KT-1 (JCM10459). The purified hydrolase degraded thermally synthesized PAA to oligomers. The molecular mass of PAA hydrolase was 30 kDa and the isoelectric point was 8.9. The optimum values of pH and temperature for PAA degradation were 10.0 and 40 °C, respectively. The investigation of the effect of inhibitors for the PAA-degrading activities has revealed that the PAA hydrolase is a serine-type hydrolase. The structural analysis of PAA-degraded products using 1H and 13C nuclear magnetic resonances has indicated that the purified enzyme hydrolyzes selectively the β-amide linkage connecting with β-aspartic acid units in PAA.
ISSN:	1525-7797 1526-4602
DOI:	10.1021/bm0155468