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Bioresources and Bioprocessing

Table 3 Activities of AbOPH and AbOPHI211A toward various substrates

From: Marked enhancement of Acinetobacter sp. organophosphorus hydrolase activity by a single residue substitution Ile211Ala

Substrates

AbOPH (μmol min−1 mg−1)

AbOPHI211A (μmol min−1 mg−1)

Phosphoesters

 Methyl-parathion

ND

1.68 ± 0.08

 Ethyl-paraoxon

ND

0.072 ± 0.012

 Fenitrothion

0.048 ± 0.011

0.543 ± 0.045

 Malathion

ND

ND

 Dimethoate

ND

ND

 Diazinon

ND

ND

Lactones

 3,4-Dihydrocoumarin

996 ± 22

389 ± 10

 δ-Decanolactone

54.1 ± 6.1

3.74 ± 0.56

 γ-Nonanolactone

14.8 ± 2.0

1.64 ± 0.12

Esters

 para-Nitrophenyl butyrate

3.73 ± 0.11

3.04 ± 0.50

 2-Naphthyl acetate

3.52 ± 0.46

2.53 ± 0.16

  1. Data were obtained with purified proteins
  2. ND no enzymatic activity was detected except spontaneous hydrolysis regardless of the high enzyme loading (2 mg/mL)
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