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Entrapment of alpha-amylase in alginate beads: single step protocol for purification and thermal stabilization.

Sai Kumar, R. S. and Vishwanatha, K. S. and Sridevi Annapurna, Singh and Appu Rao, A. G. (2006) Entrapment of alpha-amylase in alginate beads: single step protocol for purification and thermal stabilization. Process Biochemistry, 41 (11). 2282-2288 ; 26 ref..

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Abstract

Purification of alpha-amylases using alginate as an affinity matrix is reported. This process involved affinity binding of the amylase to alginate, precipitation of amylase-alginate beads in the presence of CaCl2, and subsequent recovery of the enzyme following the addition of a solution of 0.5M NaCl containing 0.2M Ca2+. Initial tests were undertaken using 3 alpha-amylases from plant, bacterial and fungal sources (sorghum, Bacillus licheniformis and Aspergillus oryzae, respectively). However, only the fungal amylase bound to alginate, and so was used in further studies. After elution from the alginate beads, the amylase was recovered at a yield of 76%, and was purified approx. 9-fold to a specific activity of 1764 U/mg. Characteristics of the alginate-immobilized amylase were also determined. pH and temp. optima upon immobilization changed from 5.5 to 6.0 and 54 to 60C, respectively. Thermal stability of the amylase was improved; the midpoint for thermal inactivation increased by 6 1C to 63C after immobilization in alginate. Recycling was also possible for the immobilized amylase; beads with a diam. >1 mm were stable and could be reused 6 times retaining approx. 70% of their original activity.

Item Type: Article
Uncontrolled Keywords: AMYLASES-; ASPERGILLUS-; IMMOBILIZATION-; IMMOBILIZED-ENZYMES; PURIFICATION-; STABILITY-; alpha-AMYLASES; ASPERGILLUS-ORYZAE
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 06 Aug 2008 10:16
Last Modified: 17 Oct 2018 06:57
URI: http://ir.cftri.com/id/eprint/8092

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