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Title of Journal: Appl Microbiol Biotechnol

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Abbravation: Applied Microbiology and Biotechnology

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Springer-Verlag

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DOI

10.1016/0014-2964(81)90124-9

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1432-0614

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Purification and characterization of arylsulfatase

Authors: JH Kim DS Byun J S Godber JS Choi WC Choi HR Kim
Publish Date: 2003/11/05
Volume: 63, Issue: 5, Pages: 553-559
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Abstract

Arylsulfatase was purified from Sphingomonas sp AS6330 through ionic exchange hydrophobic and gelchromatographies The purity increased 12800fold with approximately 191 yield against cell homogenate The enzyme was a monomeric protein with apparent molecular weight of 62 kDa as determined by sodium dodecylsulfatepolyacrylamide gel electrophoresis and 41 kDa as determined by gel filtration The enzyme had optimum reaction conditions for hydrolysis of sulfate ester bonds in agar and pnitrophenyl sulfate NPS at pH 70 and 45°C with a specific activity of 393 and 972 U respectively The enzyme showed higher activity towards agar than other sulfated marine polysaccharides such as porphyran fucoidan and carrageenan The K m and V max of the enzyme for hydrolysis of NPS were 549 μM and 113 mM/min respectively With reaction of 200 g agar with 100 U arylsulfatase for 8 h at 45°C gel strength increased 244fold and 977 of the sulfate in the agar was hydrolyzed

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