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Title of Journal: Eur Food Res Technol

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Abbravation: European Food Research and Technology

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Springer Berlin Heidelberg

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DOI

10.1007/s11282-012-0101-5

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1438-2385

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Purification and characterisation of thermoalkali

Authors: Mehrnoush Amid Yazid Manap Khanani Zohdi
Publish Date: 2014/03/05
Volume: 239, Issue: 1, Pages: 21-29
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Abstract

The thermoalkaline pectinase enzyme from Hylocereus polyrhizus was purified 2323fold with a 733  recovery through ammonium sulphate precipitation gel filtration and ion exchange chromatography Ion exchange chromatography combined with sodium dodecyl sulphate gel electrophoresis SDSPAGE revealed that the enzyme was monomeric with a molecular weight of 342 kDa The pectinase exhibited broad specificity towards polygalacturonic acid arabinan oat spelt xylan and pNPαglucopyranoside The optimum pH and temperature were 80 and 75 °C respectively This enzyme was stable over a wide pH range 30–110 and at relatively high temperature 85 °C for 1 h The Km and Vmax values of pectinase towards polygalacturonic acid were 27 mg/ml and 3430 U/mg proteins respectively In addition the enzyme activity was inhibited by Ni2+ Al3+ and Fe2+ and was increased in the presence of Ca2+ and Mg2+ by 120 and 112  respectively The purified pectinase demonstrated robust stability in response to surfactants and oxidising agents EDTA which is a powerful chelating agent did not exert any significant effect on the enzyme stability Thus enzymes with these unique properties may be widely used in different types of industries and biotechnological applicationsWe gratefully appreciate the financial support of this work by the Ministry of Science Technology and Innovation of Malaysia through Science Fund 020104SF1800 We would like to thank the staff of the Enzyme Laboratory in Food Science and Technology Faculty of University Putra Malaysia for their help support and the use of all facilities which were needed in conducting this study

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