Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7APN

Structure of Lipase TL from bulk agarose grown crystal

Summary for 7APN
Entry DOI10.2210/pdb7apn/pdb
DescriptorLipase, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (6 entities in total)
Functional Keywordslipase, reinforced crosslinked lipase crystals, clecs, hydrolase
Biological sourceThermomyces lanuginosus (Humicola lanuginosa)
Total number of polymer chains2
Total formula weight59642.22
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: 2024-01-31)
Primary citationFernandez-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: 34602865
DOI: 10.1021/acs.cgd.0c01608
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon