Purification and properties of an extracellular esterase from a cold-adapted Pseudomonas mandelii.

Abstract:

:An extracellular esterase, EstK, was purified from the psychrotrophic bacterium Pseudomonas mandelii grown at 25°C. Prior to harvest, cells were treated with 0.2 M MgCl2 to precipitate lipopolysaccharides in the outer membranes, which otherwise form aggregates with the secreted enzymes. EstK was purified to homogeneity using standard procedures. It had substrate specificity towards esters of short-chain fatty acids, particularly, p-nitrophenyl acetate. Optimum activity of EstK was at 40°C; at 4°C the activity was ~50% of its maximum. EstK has a unique substrate preference for p-nitrophenyl acetate and remains active at low temperatures.

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Hong S,Lee C,Jang SH

doi

10.1007/s10529-012-0866-y

subject

Has Abstract

pub_date

2012-06-01 00:00:00

pages

1051-5

issue

6

eissn

0141-5492

issn

1573-6776

journal_volume

34

pub_type

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