NDLI: Purification and characterization of a novel extracellular halophilic and organic solvent-tolerant amylopullulanase from the haloarchaeon, Halorubrum sp. strain Ha25

Content Provider	Springer Nature Link
Author	Siroosi, Maryam Amoozegar, Mohammad Ali Khajeh, Khosro Fazeli, Mostafa Habibi Rezaei, Mehran
Copyright Year	2013
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 K m 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.
Starting Page	25
Ending Page	33
Page Count	9
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	18
Issue Number	1
e-ISSN	14334909
Language	English
Publisher	Springer Japan
Publisher Date	2013-10-12
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Extreme halophilic archaea Halophilic amylopullulanase Halorubrum Organic solvent tolerance Protein purification Microbiology Biotechnology Biochemistry Microbial Ecology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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