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Development of a new Geobacillus lipase variant GDlip43 via directed evolution leading to identification of new activity-regulating amino acids.

Abstract：

:In this study three lipases GD-28, GD-95 and GD-66 (all 43 kDa in size), isolated from Geobacillus spp. were subjected to directed evolution experiments to yield a new synthetic lipolytic enzyme. This new lipase, obtained by DNA shuffling and epPCR, was named GDlip43 (also 43 kDa in size). It demonstrated increased thermoactivity, thermostability, an ability to hydrolyze short and long acyl chain p-NP esters and was activated by different organic solvents. Different activity of GDlip43 raised the hypothesis of new candidate amino acids which could be important for the activity of Geobacillus lipases. Based on the sequence alignment of parental and GDlip43 lipase, three candidate amino acids were selected. The importance of these amino acids, localized at positions 153, 154 and 247 (all of which are distant from the catalytic center of Geobacillus lipases) was investigated using site-directed mutagenesis. Directed evolution experiments also yielded another new lipase - GDlip30 (30 kDa in size). This low molecular mass derivative of GDlip43 had clearly detectable lipolytic activity (40 U/mg) and is the smallest currently known active Geobacillus lipase variant.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Druteika G,Sadauskas M,Malunavicius V,Lastauskiene E,Taujenis L,Gegeckas A,Gudiukaite R

doi

10.1016/j.ijbiomac.2019.10.163

subject

Has Abstract

pub_date

2020-05-15 00:00:00

pages

1194-1204

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)36608-5

journal_volume

151

pub_type

杂志文章

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