Food Lipids: Chemistry, Nutrition, and Biotechnology

VII. SUMMARY
Lipases are exceedingly interesting enzymes because the relationship between their
structure and activity presents an intellectual challenge and because their versatility
offers a broad range of possible industrial applications. However, interest in the
lipases has begun to move from academic curiosity to full commercialization in terms
of the availability of lipases and their industrial use. For example, 50 tons per year
of the chiral intermediate methyl methoxyphenyl glycidate is produced based on a
lipase-catalyzed process (141).
Although lipases have high potential for a variety of industrial applications, their
use at the present time is limited by several factors, such as lack of cost-effective
systems or processes for producing sufficient enzyme, heterogeneity of available
preparations, and absence of lipases with properties required for certain applications
(130). As with proteases, protein engineering can be applied to lipases to target
numerous specific characteristics. Alteration of amino acid sequences will result in
variants with modified specific activity, increased kcat, altered pH and thermal activity
profiles, increased stability (with respect to temperature, pH, and chemical agents
such as oxidants and proteases), and show altered pI, surface hydrophobicity, and
substrate specificity (160,161). Currently, lipase genes from fungal sources (e.g., G.
candidum and C. rugosa) are being cloned and subjected to site-directed mutation
to gain insight into structure–activity relationships, mainly with respect to selectivity,
on which to base protein engineering strategies. Despite the enormous progress that
has been made in this regard, the molecular basis for selectivity is still not well
understood.
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