7APP

Structure of Lipase TL from capillary grown crystal in the presence of agarose

7APP の概要

• エントリーDOI: 10.2210/pdb7app/pdb
• 関連するPDBエントリー: 7APN
• 分子名称: Lipase, 2-acetamido-2-deoxy-beta-D-glucopyranose, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: lipase, reinforced crosslinked lipase crystals, clecs, hydrolase
• 由来する生物種: Thermomyces lanuginosus (Humicola lanuginosa)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59886.73

構造登録者

Gavira, J.A.,Martinez-Rodriguez, S.,Fernande-Penas, R.,Verdugo-Escamilla, C. (登録日: 2020-10-19, 公開日: 2021-03-03, 最終更新日: 2024-11-13)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.7 Å)