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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.