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Properties of three purified alpha-amylases from malted finger millet (ragi, Eleusine coracana, Indaf-15).

Nirmala, M. and Muralikrishna, G. (2003) Properties of three purified alpha-amylases from malted finger millet (ragi, Eleusine coracana, Indaf-15). Carbohydrate Polymers, 54 (1). pp. 43-50.

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Abstract

Three alpha-amylases (EC 3.2.1.1) purified from ragi (Eleusine coracana, cv. Indaf-15) malt were investigated for their stability at different pH, temp. and concn. of CaCl2, EDTA, citric acid and oxalic acid. The enzymes (designated as alpha-1b, alpha-2 and alpha-3) were more stable at alkaline than acid pH, and were completely inactivated at pH <4.0. Both alpha-1b and alpha-3 retained >85% of their thermal stability after 15 min of heat treatment at 55C, whereas alpha-2 was completely inactivated; all 3 enzymes were inactivated at 75C, but thermal stability was enhanced by the presence of 5-7.5mM CaCl2. Enzyme activity was competitively inhibited by EDTA at mumol concn. in a temp. dependent manner, and both citric and oxalic acids completely inhibited the enzymes at concn. between 10 and 12.5mM.

Item Type: Article
Uncontrolled Keywords: ADDITIVES-; AMYLASES-; CALCIUM-; CHLORIDES-; CITRIC-ACID; MALT-; MILLET-; ORGANIC-ACIDS; PH-; STABILITY-; TEMPERATURE-; alpha-AMYLASES; CACL2-; OXALIC-ACID; RAGI-; TEMP.-
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 07 Enzyme Biochemistry
600 Technology > 08 Food technology > 21 Cereals > 05 Ragi (Finger Millet)
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 26 Jun 2009 06:01
Last Modified: 28 Dec 2011 09:59
URI: http://ir.cftri.com/id/eprint/7574

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