Biotechnological relevance of the lipase A from Candida antarctica

This review intends to present some of the latest studies on the lipase A from Candida antarctica (CALA). This lipase is among the most stable ones and has some capability to attack the sn-2 position of triglycerides. This makes it a very interesting lipase, especially considering that it is commerc...

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Bibliographic Details
Published in:Catalysis Today
Main Authors: Monteiro, Rodolpho R.C., Virgen-Ortiz, Jose J., Berenguer-Murcia, Ángel, Rocha, Thays N. da, Santos, Jose Cleiton S. dos, Alcántara, Andrés R., Fernández Lafuente, Roberto
Other Authors: Universidad de Alicante. Departamento de Química Inorgánica, Universidad de Alicante. Instituto Universitario de Materiales, Materiales Carbonosos y Medio Ambiente
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier 2021
Subjects:
Online Access:http://hdl.handle.net/10045/111131
https://doi.org/10.1016/j.cattod.2020.03.026
Description
Summary:This review intends to present some of the latest studies on the lipase A from Candida antarctica (CALA). This lipase is among the most stable ones and has some capability to attack the sn-2 position of triglycerides. This makes it a very interesting lipase, especially considering that it is commercially available. The cloning and production of the enzyme together with some structural facts and applications will be discussed in this review. Special focus will be put on the immobilization of the enzyme. The use of the commercially available crosslinked enzyme aggregates of this enzyme will be explained, together with the use of the enzyme in some new trends in enzyme immobilization, such as bio-imprinting of the open form of CALA by detergents and the fixation of the open structure, the design of heterofunctional supports able to take full advantage of the immobilization via interfacial activation but preventing enzyme release, or the design of strategies for the preparation of multiple layers of lipase enzymes (using just CALA or combining CALA with other lipases). ABM (RTI2018-095291-B-I00, MINECO/FEDER) and RFL (project number CTQ2017-86170-R). Thank MICINN for financial support, ABM also thanks Generalitat Valenciana (PROMETEOII/2018/076). JJVO thanks to CONACYT (Mexico) for the financial support to the basic science project number, CB-2016-01, 286,992. JCSS thanks to Brazilian Agencies for Scientific and Technological Development, Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico (FUNCAP), project number BP3-0139-00005.01.00/18 and Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Project number 422942/2016-2. The continous support supply of lipases from R. Martinez (Novozym Spain) is gratefully recognized.