Purification and characterization of a psychrophilic catalase from Antarctic Bacillus.

Abstract:

:Catalase from Bacillus sp. N2a (BNC) isolated from Antarctic seawater was purified to homogeneity. BNC has a molecular mass of about 230 kDa and is composed of four identical subunits of 56 kDa. The catalase showed optimal activity at 25 degrees C and at a pH range of 6-11. The enzyme could be inhibited by azide, hydroxylamine, and mercaptoethanol. These characteristics suggested that BNC is a small-subunit monofunctional catalase. The activation energy of BNC was 13 kJ/mol and the apparent kcat/Km values were 3.6 x 10(6) and 4 x 10(6) L.mol(-1).s(-1) at 4 and 25 degrees C, respectively. High catalytic efficiency of BNC at low temperatures enables this bacterium to scavenge H2O2 efficiently. BNC exhibited activation energy, catalytic efficiency, and thermostability comparable with some mesophilic homologues. Such similarity of enzymatic characteristics to mesophilic homologues, although uncommon among the cold-adapted enzymes in general, has also been observed in other psychrophilic small-subunit monofunctional catalases.

journal_name

Can J Microbiol

authors

Wang W,Sun M,Liu W,Zhang B

doi

10.1139/w08-066

subject

Has Abstract

pub_date

2008-10-01 00:00:00

pages

823-8

issue

10

eissn

0008-4166

issn

1480-3275

pii

w08-066

journal_volume

54

pub_type

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