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Chaiyen, Pimchai

Phaisan, Suppalak

Phintha, Aisaraphon

Trisrivirat, Duangthip

English

Engineering Conferences International

ENZYMATIC PROPERTIES OF A NOVEL CYP152 FATTY ACID DECARBOXYLASE  Suppalak Phaisan, School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC),  Thailand Suppalak.p_s20@vistec.ac.th Duangthip Trisrivirat, School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC),Thailand  Aisaraphon Phintha, School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC),  Thailand  Pimchai Chaiyen, School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC),  Thailand   Key words: P450 enzyme, CYP152, Fatty acid decarboxylation, Peroxygenase, Monooxygenase  Bacterial P450s in CYP152 family are attractive to industries and various applications. They can convert a fatty acid to a terminal alkene which can be used as a building block for productions of lubricant, surfactant, and biofuel in a single step under mild conditions. We have identified and overexpressed a new CYP152 from Salinicoccus alkaliphilus (P450SA). P450SA is a heme-dependent enzyme and a homolog of CYP152L1 from Jeotgalicoccus sp. 8456, an extensively investigated fatty acid decarboxylation. In this study, we measured a melting temperature and thermostability of the purified P450SA. P450SA can catalyze decarboxylation via a hydrogen peroxide shunt pathway (peroxygenase activity) and redox partner system (monooxygenase activity) with various chain lengths of fatty acids as substrates. P450SA can use fatty acids of 10-18 carbon atoms to generate terminal alkenes. Decarboxylation activity is greater when using hydrogen peroxide than that of redox partner systems. Remarkably, P450SA demonstrated higher decarboxylation activity compared to CYP152L1 when using long-chain fatty acids such as hexadecenoic acid (16 carbon atoms) as substrates in the presence of solvent such as ethanol (10%(v/v)). We have also solved a crystal structure of P450SA in complex with arachidic acid (20 carbon atoms). The information is useful for guiding the engineering of P450SA to enhance activity and stability in the future to overcome challenges related to real applications.    

Enzymatic properties of a novel CYP152 fatty acid decarboxylase

https://dc.engconfintl.org/cgi/viewcontent.cgi?filename=0&article=1096&context=enzyme_xxvii&type=additional

Enzymatic properties of a novel CYP152 fatty acid decarboxylase

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Engineering Conferences International