Goodarzi_2014_Appl.Biochem.Biotechnol_174_339

Reference

Title : Protein Engineering of Bacillus thermocatenulatus Lipase via Deletion of the alpha5 Helix - Goodarzi_2014_Appl.Biochem.Biotechnol_174_339
Author(s) : Goodarzi N , Karkhane AA , Mirlohi A , Tabandeh F , Torktas I , Aminzadeh S , Yakhchali B , Shamsara M , Ghafouri MA
Ref : Appl Biochem Biotechnol , 174 :339 , 2014
Abstract :

Lipases from Bacillus thermocatenulatus are a member of superfamily of alpha/beta hydrolase, but there are structural differences between them. In this work, we focused on the alpha5 helix of B. thermocatenulatus lipase (BTL2) which is absent in canonical alpha/beta hydrolase fold. In silico study showed that the alpha5 helix is a region that causes disorder in BTL2 protein. So, the alpha5 helix (residues 131 to 150) has been deleted from the B. thermocatenulatus lipase gene (BTL2) and the remain (Deltaalpha5-BTL2) has been expressed in Pichia pastoris yeast. The alpha5 deletion results in increase of enzyme-specific activity in the presence of tributyrin, tricaproin, tricaprylin, tricaprin, trilaurin, and olive oil (C18) substrates by 1.4-, 1.7-, 2.0-, 1.2-, 1.75-, and 1.95-fold, respectively. Also, deletion leads to increase in enzyme activity in different temperatures and pHs, whereas it did not significantly affect on enzyme activity in the presence of organic solvents, metal ions, and detergents.

PubMedSearch : Goodarzi_2014_Appl.Biochem.Biotechnol_174_339
PubMedID: 25064134
Gene_locus related to this paper: bactc-lipas

Related information

Substrate Tricaprin    Trihexanoin
Gene_locus Tricaprin    Trihexanoin    bactc-lipas

Citations formats

Goodarzi N, Karkhane AA, Mirlohi A, Tabandeh F, Torktas I, Aminzadeh S, Yakhchali B, Shamsara M, Ghafouri MA (2014)
Protein Engineering of Bacillus thermocatenulatus Lipase via Deletion of the alpha5 Helix
Appl Biochem Biotechnol 174 :339

Goodarzi N, Karkhane AA, Mirlohi A, Tabandeh F, Torktas I, Aminzadeh S, Yakhchali B, Shamsara M, Ghafouri MA (2014)
Appl Biochem Biotechnol 174 :339