Kinetics of papaya pectinesterase

Purified papaya (Carica papaya L. var. exotica) pectinesterase (EC 3.1.1.11) was investigated for its activity as a function of NaCl, pH and temperature, and determination of its kinetic parameters. The activity was linear up to 20 min with an enzyme concentration of up to 6.14 μg. Optimum activity...

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Main Authors: Fayyaz, A., Asbi, B.A., Ghazali, H.M., Che Man, Y.B., Jinap, S.
Format: Article
Language:English
Published: Elsevier 1995
Online Access:http://psasir.upm.edu.my/id/eprint/112703/
http://psasir.upm.edu.my/id/eprint/112703/1/112703.pdf
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author Fayyaz, A.
Asbi, B.A.
Ghazali, H.M.
Che Man, Y.B.
Jinap, S.
author_facet Fayyaz, A.
Asbi, B.A.
Ghazali, H.M.
Che Man, Y.B.
Jinap, S.
author_sort Fayyaz, A.
building UPM Institutional Repository
collection Online Access
description Purified papaya (Carica papaya L. var. exotica) pectinesterase (EC 3.1.1.11) was investigated for its activity as a function of NaCl, pH and temperature, and determination of its kinetic parameters. The activity was linear up to 20 min with an enzyme concentration of up to 6.14 μg. Optimum activity was obtained with 0.25 m NaCl concentration and the optimum pH was found to be 8. The energy of activation of enzyme was 5690 cal mol-1. A Q10 of 1.29 was observed in the temperature range of 30-50 °C and the optimum temperature for the enzyme activity was 65 °C. The Km value for citrus pectin was 0.11 mg/ml, corresponding to a Vmax value of 730 μmole/min/mg protein. The turnover number was calculated as 23 360 mole/(mole.min). Enzyme activity was found to be inhibited by the addition of polygalacturonic acid, alginic acid and sucrose in the reaction mixture and their Ki values were calculated as 0.019 mg/ml, 0.17 mg/ml and 29%, respectively. Polygalacturonic acid was found to act as a competitive inhibitor whereas alginic acid and sucrose showed a competitive-non-competitive and uncompetitive type of inhibition, respectively.
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spelling upm-1127032025-02-05T01:49:23Z http://psasir.upm.edu.my/id/eprint/112703/ Kinetics of papaya pectinesterase Fayyaz, A. Asbi, B.A. Ghazali, H.M. Che Man, Y.B. Jinap, S. Purified papaya (Carica papaya L. var. exotica) pectinesterase (EC 3.1.1.11) was investigated for its activity as a function of NaCl, pH and temperature, and determination of its kinetic parameters. The activity was linear up to 20 min with an enzyme concentration of up to 6.14 μg. Optimum activity was obtained with 0.25 m NaCl concentration and the optimum pH was found to be 8. The energy of activation of enzyme was 5690 cal mol-1. A Q10 of 1.29 was observed in the temperature range of 30-50 °C and the optimum temperature for the enzyme activity was 65 °C. The Km value for citrus pectin was 0.11 mg/ml, corresponding to a Vmax value of 730 μmole/min/mg protein. The turnover number was calculated as 23 360 mole/(mole.min). Enzyme activity was found to be inhibited by the addition of polygalacturonic acid, alginic acid and sucrose in the reaction mixture and their Ki values were calculated as 0.019 mg/ml, 0.17 mg/ml and 29%, respectively. Polygalacturonic acid was found to act as a competitive inhibitor whereas alginic acid and sucrose showed a competitive-non-competitive and uncompetitive type of inhibition, respectively. Elsevier 1995 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/112703/1/112703.pdf Fayyaz, A. and Asbi, B.A. and Ghazali, H.M. and Che Man, Y.B. and Jinap, S. (1995) Kinetics of papaya pectinesterase. Food Chemistry, 53 (2). pp. 129-135. ISSN 0308-8146; eISSN: 1873-7072 https://linkinghub.elsevier.com/retrieve/pii/0308814695907775 10.1016/0308-8146(95)90777-5
spellingShingle Fayyaz, A.
Asbi, B.A.
Ghazali, H.M.
Che Man, Y.B.
Jinap, S.
Kinetics of papaya pectinesterase
title Kinetics of papaya pectinesterase
title_full Kinetics of papaya pectinesterase
title_fullStr Kinetics of papaya pectinesterase
title_full_unstemmed Kinetics of papaya pectinesterase
title_short Kinetics of papaya pectinesterase
title_sort kinetics of papaya pectinesterase
url http://psasir.upm.edu.my/id/eprint/112703/
http://psasir.upm.edu.my/id/eprint/112703/
http://psasir.upm.edu.my/id/eprint/112703/
http://psasir.upm.edu.my/id/eprint/112703/1/112703.pdf