journal6 ›› 2004, Vol. 25 ›› Issue (4): 44-48.

• Doctoral Forum • Previous Articles     Next Articles

Isolation,Purification and Properties of Chondroitinase From Serratia Marcescens


  1.  (1.College of Life Science Sichuan University,Chengdu  610064,China;2.Chengdu Chuangxin Bio-technology Institute,Sichuan University,Chengdu 610064,China)
  • Online:2004-12-15 Published:2012-09-22

Abstract: Chondroitinase was isolated and purified from Serratia marcescens and its kinetic property was examined.The Chondroitinase was purified by salting-out,DEAE-Sepharose FF ion-exchange chromatogram,and gel filtrition with Sephacryl S-200 chromatogram.The purified enzyme moved as a single electrophoretic band in PAGE.The specific activity was 81.23 U/mg.It’s subunit weight was 35 KD with SDS-PAGE,moleculer weight was 70.20 KD with gel filtrition on Sephacryl S-300(AKTA FPLC).The optimum pH value for the enzyme was 7.5.The optimum temperature for the enzyme was about 40 ℃.The Michealis-Menton constant(Km) was 3.98×10-4 mol/L with 4-Chondroitin Sulfate as its substrate.

Key words: Serratia marcescens, chondroitinase, isolation and purification

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