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Characterization of Invertase from Saccharomyces cerevisiae MK obtained from toddy sample
Research article
  

Characterization of Invertase from Saccharomyces cerevisiae MK obtained from toddy sample


T. Shankar, P. Thangamathi, R. Rama, T. Sivakumar

Department of Microbiology, Ayya Nadar Janaki Ammal College, Sivakasi-626124,


Corresponding author :

T. Shankar,
Department of Microbiology,
Ayya Nadar Janaki Ammal College,
Sivakasi, India-626124,
Email:

Received: February 15, 2014,   Accepted: March 20, 2014,   Published: March 21, 2014.


Abstract:

Activity and stability of invertase obtained from Saccharomyces cerevisiae MK were characterized with the following parameters like pH, temperature, metal ions, surfactants and chemical inhibitors. The pH stability of this enzyme was observed between pH 2 to pH 9 with an average of 80 percent retaining activity for 24 hours. The crude enzyme showed optimum activity at pH 6 and 30ºC. Enzyme activity was increased in the presence of 5mM CaCl2 (92.74%). Maximum invertase activity of 35.88% was recorded at polyethylene glycol (1%). Maximum invertase activity of 29.16% was recorded at EDTA for Saccharomyces cerevisiae MK. The kinetic parameters (Km and Vmax) were determined at 30°C and pH 6 for Saccharomyces cerevisiae MK invertase for concentrations ranging between 0.5 to 5 mg/ml of sucrose as substrate the Km and Vmax of Saccharomyces cerevisiae MK invertase are 0.3410 mg/ml and 0.5953 μm/min/mg.


Keywords: Saccharomyces cerevisiae MK, invertase, specific activity, relative activity, Enzyme characterization


Citation:

T. Shankar, et al (2014) Characterization of Invertase from Saccharomyces cerevisiae MK obtained from toddy sample. J. of Bioprocessing and Chemical Engineering. V1I2. DOI: 10.15297/JBCE.V1I2.01


Copyright:

© 2014 T. Shankar. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


      
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      Journal of Bioprocessing and Chemical Engineering