Characterization of a Chitosanase from Jelly Fig

A chitosanase was purified from jelly fig latex by ammonium sulfate fractionation (50-80% saturation) and three successive column chromatography steps. The purified enzyme was almost homogeneous, as determined by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and gel activity staining. The molecu...

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Veröffentlicht in:PloS one 2016-03, Vol.11 (3), p.e0150490
Hauptverfasser: Chang, Chen-Tien, Lin, Yen-Lu, Lu, Shu-Wei, Huang, Chun-Wei, Wang, Yu-Ting, Chung, Yun-Chin
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Sprache:eng
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Zusammenfassung:A chitosanase was purified from jelly fig latex by ammonium sulfate fractionation (50-80% saturation) and three successive column chromatography steps. The purified enzyme was almost homogeneous, as determined by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and gel activity staining. The molecular mass of the enzyme was 20.5 kDa. The isoelectric point (pI) was
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0150490