BioChem - DOS

Creating an Efficient Methanol-Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel

ChemSusChem

Gihaz, Shalev; Weiser, Diá na; Dror, Adi; Sá torhelyi, Pé ter; Jerabek‐ Willemsen, Moran; Poppe, Lá szló Fishman, Ayelet

<P><B>Abstract</B></P><P>Two ternary sol&ndash;gel matrices, an octyltriethoxysilane&#8208;based aliphatic matrix and a phenyltriethoxysilane (PTEOS)&#8208;based aromatic matrix, were used to immobilize a methanol&#8208;stable variant of lipase from <I>Geobacillus stearothermophilus</I> T6 for the synthesis of biodiesel from waste oil. Superior thermal stability of the mutant versus the wildtype in methanol was confirmed by intrinsic protein fluorescence measurements. The influence of skim milk and soluble <I>E. coli</I> lysate proteins as bulking and stabilizing agents in conjunction with sol&ndash;gel entrapment were investigated. <I>E. coli</I> lysate proteins were better stabilizing agents of the purified lipase mutant than skim milk, as evidenced by reverse engineering of the aromatic&#8208;based system. This was also shown for commercial <I>Candida antarctica</I> lipase B (CaLB) and <I>Thermomyces lanuginosus</I> lipase (TLL). Uniform, dense, and nonaggregated particles imaged by scanning electron microscopy and a small particle size of 13 &mu;m pertaining to the system comprising PTEOS and <I>E. coli</I> lysate proteins correlated well with high esterification activity. Combining protein and immobilization engineering resulted in a durable biocatalyst with efficient recycling ability and high biodiesel conversion rates.</P>

2016

1864-5631

1864-564x

9

22

pp.3161-3170

10.1002/cssc.201601158

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART77556186

biodiesel; enzymes; immobilization; protein engineering; sol&#x2013; gel processes;