7APP
Structure of Lipase TL from capillary grown crystal in the presence of agarose
Summary for 7APP
| Entry DOI | 10.2210/pdb7app/pdb |
| Related | 7APN |
| Descriptor | Lipase, 2-acetamido-2-deoxy-beta-D-glucopyranose, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | lipase, reinforced crosslinked lipase crystals, clecs, hydrolase |
| Biological source | Thermomyces lanuginosus (Humicola lanuginosa) |
| Total number of polymer chains | 2 |
| Total formula weight | 59886.73 |
| Authors | Gavira, J.A.,Martinez-Rodriguez, S.,Fernande-Penas, R.,Verdugo-Escamilla, C. (deposition date: 2020-10-19, release date: 2021-03-03, Last modification date: 2024-11-13) |
| Primary citation | Fernandez-Penas, R.,Verdugo-Escamilla, C.,Martinez-Rodriguez, S.,Gavira, J.A. Production of Cross-Linked Lipase Crystals at a Preparative Scale. Cryst.Growth Des., 21:1698-1707, 2021 Cited by PubMed Abstract: The autoimmobilization of enzymes via cross-linked enzyme crystals (CLECs) has regained interest in recent years, boosted by the extensive knowledge gained in protein crystallization, the decrease of cost and laboriousness of the process, and the development of potential applications. In this work, we present the crystallization and preparative-scale production of reinforced cross-linked lipase crystals (RCLLCs) using a commercial detergent additive as a raw material. Bulk crystallization was carried out in 500 mL of agarose media using the batch technique. Agarose facilitates the homogeneous production of crystals, their cross-linking treatment, and their extraction. RCLLCs were active in an aqueous solution and in hexane, as shown by the hydrolysis of -nitrophenol butyrate and α-methylbenzyl acetate, respectively. RCLLCs presented both high thermal and robust operational stability, allowing the preparation of a packed-bed chromatographic column to work in a continuous flow. Finally, we determined the three-dimensional (3D) models of this commercial lipase crystallized with and without phosphate at 2.0 and 1.7 Å resolutions, respectively. PubMed: 34602865DOI: 10.1021/acs.cgd.0c01608 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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