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Table 1 Substrate specificity of the purified LipA on various substrates

From: The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor

Substrate

Specific activitya(U/mg)

Xylose tetra-acetate

58.84 ± 2.32

Oat spelt xylan

14.12 ± 4.34

p NP acetate (C 2 )

0.14 ± 0.03

p NP butyrate (C 4 )

2.80 ± 0.04

p NP caprylate (C 8 )

6.52 ± 0.13

p NP myristate (C 14 )

2.56 ± 0.17

p NP palmitate (C 16 )

1.29 ± 0.02

p NP arabino-pyranoside

ND b

p NP arabino-furanoside

ND

p NP xylopyranoside

ND

Methyl ferulate

ND

Methyl cafeate

ND

Methyl sinapinate

ND

Methyl p -coumarate

ND

  1. a Unit definition: 1 unit of activity is the amount necessary to hydrolyze 1.0 μmol of substrate per minute at 40°C and pH 7.0. Values are the mean ± the standard deviation (SD) of three independent experiments. b ND = not detectable. Deacetylation of xylose tetra-acetate and oat spelt xylan was evaluated by determining the amount of acetyl group released per milligram of protein and the hydrolysis of p NP substrates was expressed relative to the amount of p-nitrophenol liberated pre milligram of LipA.
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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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