Characterization of a Chitosanase from Jelly Fig (Ficus awkeotsang Makino) Latex and Its Application in the Production of Water-Soluble Low Molecular Weight Chitosans

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-e0150490
Hauptverfasser:	Chang, Chen-Tien, Lin, Yen-Lu, Lu, Shu-Wei, Huang, Chun-Wei, Wang, Yu-Ting, Chung, Yun-Chin
Format:	Artikel
Sprache:	eng
Schlagworte:	Ammonium Ammonium salts Ammonium sulfate Ammonium Sulfate - chemistry Antioxidants Benzothiazoles - antagonists & inhibitors Biological products Biology and Life Sciences Chemicals Chitin Chitin - chemistry Chitinase Chitosan Chitosan - analogs & derivatives Chitosan - chemical synthesis Chitosan - chemistry Chitosanase Chromatography Column chromatography Deacetylation Derivatives Electrophoresis Enzymes Ethylene glycol Ethylene glycols Ficus - chemistry Ficus awkeotsang Food Fractionation Free Radical Scavengers - chemistry Gel electrophoresis Glycoside Hydrolases - chemistry Glycoside Hydrolases - isolation & purification Hydrogen-Ion Concentration Hydrolysis Insects Isoelectric focusing Isoelectric Point Kinetics Latex Latex - chemistry Low molecular weights Microorganisms Molecular Weight Nutrition Peroxides - antagonists & inhibitors Peroxyl radicals pH effects Physical Sciences Plant Proteins - chemistry Plant Proteins - isolation & purification Polyimide resins Polymers Proteins Sodium lauryl sulfate Solubility Studies Substrate Specificity Substrates Sulfate Sulfates Sulfonic Acids - antagonists & inhibitors Superoxide Superoxides Superoxides - antagonists & inhibitors Water Water purification
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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