Lipase Improvement: Goals and Strategies

Tuning the catalytic properties of lipases immobilized on divinylsulfone activated agarose by altering its nanoenvironment

“…Even with these very good possibilities, lipase properties, like those of most enzymes, need to be improved in many instances before its industrial implementation [25]. For example, in most cases it is convenient to have the enzyme in a heterogeneous form, as a simple way to separate the enzyme from the reaction media and to reuse it [26,27].…”

Cold active lipases – an update

“…They are enzymatic or chemical modifications, use of additives, immobilization, directed evolution and protein engineering (Zhang 2003;Eijsink et al 2004;Siddiqui & Cavicchioli 2005;Lafranconi et al 2008). Directed evolution with random mutagenesis based on error-prone PCR (ep-PCR) and iterative saturation mutagenesis guided by rational design are more frequently employed nowadays to enhance the thermostability (Bassegoda et al 2012). The factors commonly considered to increase thermal stability are the hydrophobicity, number of hydrogen bonds, amino acid composition, amino acid distribution and interactions in the protein (Vielle & Zeikus 2001).…”

In vitro stability evaluation of coated lipase

“…As the temperature rose, CT-LIP protected by coating showed a stronger thermostability than the free one. The stability is a key factor in estimating the economic feasibility of commercial enzymes [21,22]. High pressure steam, which provides the appropriate heat and moisture required for thermal modification of starch and protein in pellet processing, would produce certain damage to the activity of supplemented lipase.…”