title: An insight into plant lipase research - challenges encountered.
abstract: 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.
authors.affiliation: Department of Biotechnology, Indian Institute of Technology Guwahati, Assam 781 039, India.
authors.forename: Sonali
authors.initials: S
authors.lastname: Seth
authors.affiliation: Department of Biotechnology, Indian Institute of Technology Guwahati, Assam 781 039, India.
authors.forename: Debamitra
authors.initials: D
authors.lastname: Chakravorty
authors.affiliation: Department of Biotechnology, Indian Institute of Technology Guwahati, Assam 781 039, India.
authors.forename: Vikash Kumar
authors.initials: VK
authors.lastname: Dubey
authors.affiliation: Department of Biotechnology, Indian Institute of Technology Guwahati, Assam 781 039, India. Electronic address: sanjukta@iitg.ernet.in.
authors.forename: Sanjukta
authors.initials: S
authors.lastname: Patra
mesh_terms: D003001:Cloning, Molecular; D008049:Lipase; D010940:Plant Proteins; D015202:Protein Engineering; D011994:Recombinant Proteins
chemical_list: D010940:Plant Proteins; D011994:Recombinant Proteins; D008049:Lipase
keywords: Industrial applications; Limitations; Lipases; Plant; Protein engineering; Purification; Recombinant proteins