Opening lids: modulation of lipase immobilization by graphene oxides


Autoria(s): Mathesh, Motilal; Luan, Binquan; Akanbi, Taiwo; Weber, Jeffrey K; Liu, Jingquan; Barrow, Colin; Zhou, Ruhong; Yang, Wenrong
Data(s)

01/07/2016

Resumo

Lipases, which can be immobilized and reused for many reaction cycles, are important enzymes with many industrial applications. A key challenge in lipase immobilization for catalysis is to open the lipase lid and maintain it in an open conformation in order to expose its active site. Here we have designed "tailor-made" graphene-based nanosupports for effective lipase (QLM) immobilization through molecular engineering, which is in general a grand challenge to control biophysicochemical interactions at the nano-bio interface. It was observed that increasing hydrophobic surface increased lipase activity due to opening of the helical lid present on lipase. The molecular mechanism of lid opening revealed in molecular dynamics simulations highlights the role of hydrophobic interactions at the interface. We demonstrated that the open and active form of lipase can be achieved and tuned with an optimized activity through chemical reduction of graphene oxide. This research is a major step toward designing nanomaterials as a platform for enhancing enzyme immobilization/activity.

Identificador

http://hdl.handle.net/10536/DRO/DU:30085387

Idioma(s)

eng

Publicador

American Chemical Society

Relação

http://dro.deakin.edu.au/eserv/DU:30085387/mathesh-openinglids-2016.pdf

http://www.dx.doi.org/10.1021/acscatal.6b00942

Direitos

2016, American Chemical Society

Palavras-Chave #graphene oxides #lipase #hydrophobic #enzyme papers #simulation
Tipo

Journal Article