Purification and Characterization of a Novel Extracellular Halophilic and Organic Solvent-tolerant Amylopullulanase from the Haloarchaeon, Halorubrum Sp. Strain Ha25

Overview

Journal Extremophiles

Publisher Springer

Date 2013 Oct 15

PMID 24122359

Citations 13

Authors

Maryam Siroosi

Mohammad Ali Amoozegar

Khosro Khajeh

Mostafa Fazeli

Mehran Habibi Rezaei

Affiliations

Soon will be listed here.

Abstract

A halophilic archaeon, Halorubrum sp. strain Ha25, produced extracellular halophilic organic solvent-tolerant amylopullulanase. The maximum enzyme production was at high salt concentration, 3-4 M NaCl. Optimum pH and temperature for enzyme production were 7.0 and 40 °C, respectively. Molecular mass of purified enzyme was estimated to be about 140 kDa by SDS-PAGE. This enzyme was active on pullulan and starch as substrates. The apparent Km for the enzyme activity on pullulan was 4 mg/ml and for soluble starch was 1.8 mg/ml. Optimum temperature for amylolytic and pullulytic activities was 50 °C. Optimum pH for amylolytic activity was 7 and for pullulytic activity was 7.5. This enzyme was active over a wide range of concentrations (0-4.5 M) of NaCl. The effect of organic solvents on the enzyme activities showed that this enzyme was more stable in the presence of non-polar organic solvents than polar solvents. This study is the first report on amylopullulanase production in halophilic bacteria and archaea.

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