Title of article
Production and characterization of lipases and immobilization of whole cell of the thermophilic Thermomucor indicae seudaticae N31 for transesterification reaction
Author/Authors
Ferrarezi، نويسنده , , Ana Lucia and Hideyuki Kobe Ohe، نويسنده , , Thiago and Borges، نويسنده , , Janaina Pires and Brito، نويسنده , , Rafaela Rodrigues and Siqueira، نويسنده , , Marcos Rechi and Vendramini، نويسنده , , Pedro Henrique and Quilles Jr.، نويسنده , , José Carlos and da Costa Carreira Nunes، نويسنده , , Christiane and Bonilla-Rodriguez، نويسنده , , Gustavo Orlando and Boscolo، نويسنده , , Mauricio and Da-Silva، نويسنده , , Roberto Dino Gomes، نويسنده , , Eleni، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2014
Pages
8
From page
106
To page
113
Abstract
Among 54 thermophilic fungi tested for lipase production, the highest yield was obtained for Thermomucor indicae seudaticae in submerged (SmF) and solid state fermentation (SSF), being that species selected for studies of fermentative parameters. Some modifications of the culture media afforded an improvement of 15 fold in the lipase activity in SSF and 8 fold in SmF. Furthermore, the lipases produced through both SSF and SmF exhibited maximum lipolytic activity at 40 °C but these lipases were different since the enzyme from SmF presented maximum activity at neutral pH (6.0–7.0) whereas the lipase from SSF displayed maximum activity at acidic pH (3.0–4.0). The fungus was grown on loofah sponges, and the immobilized hyphae showed 108 U g− lipolytic activity, a profile including both alkaline and acidic activities. The esterification and transesterification yields were 28% and 13.2% using oleic acid and soybean oil, respectively. Those are essential reactions for biodiesel production. Thus, the lipase production of both the immobilized whole cells as well as the cultivated fungus T. indicae seudaticae N31 may be considered promising in synthesis reactions.
Keywords
Thermomucor indicae seudaticae , Lipase , submerged fermentation , Solid state fermentation , Whole cell , Transesterification reaction
Journal title
Journal of Molecular Catalysis B Enzymatic
Serial Year
2014
Journal title
Journal of Molecular Catalysis B Enzymatic
Record number
1719017
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