Lipases from bacterial, fungal, and animal sources have been purified to homogeneity with very few of them being contributed from plants. Plant lipases are mostly found in energy reserve tissues, for example, oilseeds. They act as biocatalysts which are attractive due to their high substrate specificity, low production cost and easy pharmacological acceptance due to their eukaryotic origin. Hence plant lipases represent better potential for commercial applications in organic synthesis, food, detergent and pharmacological industries. However, low expression, uneconomical fold purity and the plethora of difficulties related to their recombinant expression has been limiting their commercial applicability and posing challenges to many researchers. This article focuses on comprehensive approaches that have been reported to date to address these challenges.
Keywords: Industrial applications; Limitations; Lipases; Plant; Protein engineering; Purification; Recombinant proteins.
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