Open AccessPurification, Characterization of L-Methioninase fromCandida tropicalis, and Its Application as an Anticancer
Author(s) -
Mohsen H. Selim,
El-Zahraa Karm Eldin,
Moataza M. Saad,
El-Sayed E. Mostafa,
Yosrea Hassan Shetia,
Amany Ahmed Hassabo Anise
Publication year - 2015
Publication title -
biotechnology research international
Language(s) - English
Resource type - Journals
eISSN - 2090-3138
pISSN - 2090-3146
DOI - 10.1155/2015/173140
Subject(s) - candida tropicalis , size exclusion chromatography , enzyme , substrate (aquarium) , chromatography , enzyme assay , thermal stability , ion chromatography , chemistry , yeast , biochemistry , biology , ecology , organic chemistry
The aim of the present study is to purify L-methioninase from Candida tropicalis 34.19-fold with 27.98% recovery after ion exchange chromatography followed by gel filtration. The purified enzyme revealed a single band on SDS-PAGE gel with a molecular weight of 46 KDa. Its optimum temperature was 45 to 55 and thermal stability was 55°C for 15 min. The enzyme had optimum pH at 6.5 and stability at a pH range of 5.5 to 7.0 for 24 hr. The maximum activity was observed with substrate concentration of 30 µ M and Km was 0.5 mM. The enzyme was strongly inhibited by Cd +2 and Cu +2 while it was enhanced by Na + , Ni +2 , and Mg +2 at 10 mM while Ca +2 had slight activation at 20 mM. In addition, the potential application of the L-methioninase as an anticancer agent against various types of tumor cell lines is discussed.
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