NDLI: α-Amylase activity from the halophilic archaeon Haloferax mediterranei

Content Provider	Springer Nature Link
Author	Pérez Pomares, F. Bautista, V. Ferrer, J. Pire, C. Marhuenda Egea, F. C. Bonete, M. J.
Copyright Year	2003
Abstract	The halophilic archaeon Haloferax mediterranei is able to grow in a minimal medium containing ammonium acetate as a carbon and nitrogen source. When this medium is enriched with starch, α-amylase activity is excreted to the medium in low concentration. Here we report methods to concentrate and purify the enzyme. The relative molecular mass of the enzyme, determined by gel filtration, is 50±4 kDa, and on SDS-PAGE analysis a single band appeared at 58 kDa. These results indicated that the halophilic α-amylase is a monomeric enzyme. The enzyme showed a salt requirement for both stability and activity, being stable from 2 to 4 M NaCl, with maximal activity at 3 M NaCl. The enzyme displayed maximal activity at pHs from 7 to 8, and its optimal temperature was in a range from 50 °C to 60 °C. The results also implicated several prototropic groups in the catalytic reaction.
Starting Page	299
Ending Page	306
Page Count	8
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	7
Issue Number	4
e-ISSN	14334909
Language	English
Publisher	Springer-Verlag
Publisher Date	2003-04-24
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	α-Amylase Archaea Extracellular Haloferax mediterranei Purification
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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α-Amylase activity from the halophilic archaeon Haloferax mediterranei