Thermoresponsive magnetic nanoparticles (MNPs) were synthesized using a magnetosome display system. An elastin-like polypeptide decamer of VPGVG (ELP), which is hydrophobic above the transition temperature ( T) and can form an insoluble aggregation, was immobilized on biogenic MNPs in the magnetotactic bacterium, Magnetospirillum magneticum AMB-1. It was suggested that hydrophobicity of the MNP surface increased at 60 °C compared with 20 °C by the immobilization of ELP. Size distribution analysis indicated that the immobilization of ELP onto MNPs induced the increased hydrophobicity with increasing temperatures up to 60 °C, promoting aggregation of the particles by hydrophobic and magnetic interactions. These results suggest that the acceleration of magnetic collection at 60 °C was caused by particle aggregation promoted by hydrophobic interaction between ELP-MNPs. Furthermore, the immobilization of ELP on MNPs gave a quick magnetic collection at 60 °C by external magnetic field. The thermoresponsive properties will further expand the utility of biotechnological applications of biogenic MNPs.
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http://dx.doi.org/10.1021/acs.bioconjchem.8b00195 | DOI Listing |
Biochim Biophys Acta Gen Subj
January 2024
Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S.A.S. Nagar, Mohali 160062, Punjab, India. Electronic address:
Background: L-asparaginase (ASNase) has played a key role in the management of acute lymphoblastic leukaemia (ALL). As an amidohydrolase, it catalyzes the hydrolysis of L-asparagine, a crucial step in the treatment of ALL. Various ASNase variants have evolved from diverse sources since it was first used in paediatric patients in the 1960s.
View Article and Find Full Text PDFFront Bioeng Biotechnol
June 2022
Institute of Process Engineering in Life Sciences, Section IV: Molecular Separation Engineering, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.
Elastin-like proteins (ELPs) are polypeptides with potential applications as renewable bio-based high-performance polymers, which undergo a stimulus-responsive reversible phase transition. The ELP investigated in this manuscript-ELP[V2Y-45]-promises fascinating mechanical properties in biomaterial applications. Purification process scalability and purification performance are important factors for the evaluation of potential industrial-scale production of ELPs.
View Article and Find Full Text PDFJ Agric Food Chem
July 2021
School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang 212013, P. R. China.
Today, we are seeking an efficient biotransformation of cellulosic material into sustainable biochemical products to meet the increasing global energy demand. Herein, we report the fabrication of multienzyme hybrid nanoflowers (ECG-NFs) by co-immobilizing three recombinant enzymes (cellobiohydrolase (CBH), endo-glucanase (EG), and β-glucosidase (BG)) integrating a binary tag composed of elastin-like polypeptide (ELP) and His-tag to act as a tri-enzyme biocatalyst, which catalyzes the hydrolysis of cellulose into glucose. The prepared ECG-NFs exhibited excellent performance in terms of pH stability, thermal stability, storage stability, and catalytic efficiency compared to free multienzyme system.
View Article and Find Full Text PDFJ Biomed Mater Res B Appl Biomater
August 2020
Department of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
There is growing interest in the functional roles of the extracellular matrix (ECM) in regulating the fate of pluripotent stem cells (PSCs). An artificially bioengineered ECM provides an excellent model for studying the molecular mechanisms underlying self-renewal and differentiation of PSCs, without multiple unknown and variable factors associated with natural substrates. Here, we have engineered multifunctional fusion proteins that are based on peptides from laminin, including p20, RGD, and elastin-like polypeptide (ELP), where laminin peptides work as cell adhesion molecules (CAMs) and ELP to promote anchorage.
View Article and Find Full Text PDFSoft Matter
December 2019
Department of Chemical Engineering, University of New Hampshire, Durham, NH, USA.
Elastin-like polymers (ELPs) are frequently used in a variety of bioengineering applications because of their stimuli-responsive properties. Above their transition temperature, ELPs will adopt different structures that promote intra- and intermolecular hydrophobic contacts to minimize unfavorable interactions with an aqueous environment. We electrochemically characterize the stimuli-responsive behavior of surface-immobilized ELPs corresponding to two proposed states: extended and collapsed.
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