. 1996; 9(2): 31-36

Purification and Some Properties of Invertases from Achras Sapota Fruit

M. U. Dahot1, M. Hanif Noomrio2
1From Department of Biochemistry, Enzyme and Fermentation Biotechnology Research Laboratory, Institute of Chemistry, University of Sindh, Jamshoro, Pakistan.
2From Department of Chemistry, Shah Abdul Latif University, Khairpur Sindh, Pakistan.

Invertase (E.C. 3.2.1.26) from the Achras sapota fruit was 6.5% and at temperature 20°C. The activity of both invertases were found heat labile and were completely inactivated at 45°C and 70°C within 10 minutes. Invertase I and II activities were increased in the presence of MnCI2, CoCI2 and CaCI2 but completely inhibited with EDTA due to chelation with metal ions. Raffinose and stachyose were hydrolyzed at the rate of 59.52% and 33% with invertase I and 88.88% and 83.33% with invertase II relative to sucrose whereas cellobiose, inulin and maltose were not hydrolyzed with Invertase I and II.

Keywords: Achras sapota, Invertase, Purification.


M. U. Dahot, M. Hanif Noomrio. Purification and Some Properties of Invertases from Achras Sapota Fruit. . 1996; 9(2): 31-36

Sorumlu Yazar: M. U. Dahot, Pakistan


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