Self-assembly of metal-cholesterol oxidase hybrid nanostructures and application in bioconversion of steroids derivative
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RESEARCH ARTICLE
Self-assembly of metal-cholesterol oxidase hybrid nanostructures and application in bioconversion of steroids derivatives Yu Xin (✉)1,2, Qiuyue Gao1, Yu Gu1, Mengyao Hao1, Guangming Fan1, Liang Zhang (✉)2 1 Key Laboratory of Industry Biotechnology (Ministry of Education), School of Biotechnology, Jiangnan University, Wuxi 214122, China 2 National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China
© Higher Education Press 2020
Abstract A cholesterol oxidase (COD) was hybridized with Ca2+, Zn2+, Al3+, Fe2+ and Mn2+. After precipitation with PO43– at 4 °C for 72 h, the resulting pellets were freeze-dried. In scanning electron microscopy assays, the metal-COD complexes revealed flower-like or granular structures after hybridization. Fourier transform infrared spectroscopy assay revealed the characteristic peaks of both the enzyme and metal materials. X-ray diffraction analysis indicated that COD was encapsulated in CaHPO4$2H2O-, Zn3(PO4)2$4H2O-, AlPO4-, FeP4- and Mn3(PO4)2$3H2O-based nanostructures, respectively. Differential scanning calorimetry assay indicated significant increases in thermo-denaturation temperatures from 60.5 °C to 167.02 °C, 167.02 °C, 137.70 °C, 172.85 °C and 160.99 °C, respectively. Using steroid derivatives as substrates, this enzyme could convert cholesterol, pregnenolone, dehydroepiandrosterone, ergosterol, b-sitosterol and stigmasterol to related single products. Hybridization in metal-based nanostructures could significantly enhance the initial conversion ratio and reaction stability of the enzyme. In addition, substrate selectivity could be affected by various metal materials. Briefly, using Ca2+, Zn2+, Al3+, Fe2+ and Mn2+ as hybrid raw materials could help to encapsulate COD in related metal-enzyme nanostructures, and could help to promote the stability and tolerant properties of the enzyme, while also enhancing its catalytic characteristics. Keywords cholesterol oxidase, metal-enzyme hybridization, nanostructures, sterol derivatives, bioconversion
Received June 21, 2020; accepted July 10, 2020 E-mails: [email protected] (Xin Y); [email protected] (Zhang L)
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Introduction
Steroid derivatives have recently become widely used in the pharmacological industry and fundamental medical research. A number of active compounds transformed from steroid derivatives have been reported to offer significant medical or biological functions [1,2], e.g., aiding tumor cell migration repression [3], as intermediate compounds of anabolic or contraceptive drugs [4,5], or aiding patients who suffer from amyotrophic lateral sclerosis [6] or spinal muscular atrophy [7]. Traditionally, industrial-scale steroid production has relied on chemical protocols with long production cycles and harmful byproducts [8,9]. Cholesterol oxidases (CODs) are a group of enzymes that convert cholesterol to cholestenone using flavin adenine dinucleotide or flavin mononucleotide as necessary coenzymes. CODs can be produced by various microorganisms [10–13]. Becau
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