RT Journal Article
T1 A Novel, Highly Potent NADPH-Dependent Cytochrome P450 Reductase from Waste Liza klunzingeri Liver
A1 Bahramian Nasab, Soudeh
A1 Homaei, Ahmad
A1 Fernandez-Lafuente, Roberto
A1 Del Arco, Jon
A1 Fernández Lucas, Jesús
AB The use of marine enzymes as catalysts for biotechnological applications is a topical subject. Marine enzymes usually display better operational properties than their animal, plant or bacterial counterparts, enlarging the range of possible biotechnological applications. Due to the fact that cytochrome P450 enzymes can degrade many different toxic environmental compounds, these enzymes have emerged as valuable tools in bioremediation processes. The present work describes the isolation, purification and biochemical characterization of a liver NADPH-dependent cytochrome P450 reductase (CPR) from the marine fish Liza klunzingeri (LkCPR). Experimental results revealed that LkCPR is a monomer of approximately 75 kDa that is active in a wide range of pH values (6–9) and temperatures (40–60 °C), showing the highest catalytic activity at pH 8 and 50 °C. The activation energy of the enzyme reaction was 16.3 kcal mol−1 K−1. The KM values for cytochrome C and NADPH were 8.83 μM and 7.26 μM, and the kcat values were 206.79 s−1 and 202.93 s−1, respectively. LkCPR displayed a specific activity versus cytochrome C of 402.07 µmol min−1 mg1, the highest activity value described for a CPR up to date (3.2–4.7 times higher than the most active reported CPRs) and showed the highest thermostability described for a CPR. Taking into account all these remarkable catalytic features, LkCPR offers great potential to be used as a suitable biocatalyst
PB MDPI
SN 1660-3397
YR 2023
FD 2023
LK https://hdl.handle.net/20.500.14352/108726
UL https://hdl.handle.net/20.500.14352/108726
LA eng
NO Bahramian Nasab, Soudeh, et al. «A Novel, Highly Potent NADPH-Dependent Cytochrome P450 Reductase from Waste Liza Klunzingeri Liver». Marine Drugs, vol. 21, n.o 2, enero de 2023, p. 99. DOI.org (Crossref), https://doi.org/10.3390/md21020099.
NO This work was financially supported by grant from University of Hormozgan, Iran (Grant No. 96.200.146).
NO University of Hormozgan (Iran)
DS Docta Complutense
RD 17 abr 2025