penicillin g acylase
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2021 ◽  
Vol ahead-of-print (ahead-of-print) ◽  
Author(s):  
Hongyi Tu ◽  
Donglei Liu ◽  
Zhenbin Chen ◽  
Chunli Liu

Purpose Using a reversible addition fragmentation chain transfer reaction, a series of resins were prepared by using N, N-diethyl acrylamide (DEA), poly (ß-hydroxyethyl methacrylate) (PHEMA) as hydrophilic blocks and poly (glycidyl methacrylate) (PGMA) as hydrophobic blocks (and as a target for immobilizing penicillin G acylase [PGA]) and the low critical solution temperature (LCST) of which could be adjusted by changing the segment length of blocks. Design/methodology/approach To make the catalytic conversion temperature of immobilized PGA fallen into the temperature range of the sol state of thermosensitive block resin, a type of thermosensitive block resin, i.e. PDEA-b-PHEMA-b-PGMA (DHGs) was synthesized to immobilize PGA, and the effect of segment order of block resin was investigated on the performance of PGA. Findings Carrier prepared with monomers molar ratio of n(DEA) : n(HEMA): n(GMA) = 100: 49: 36 presented loading capacity (L) and enzyme activity recovery ratio (Ar) of 110 mg/g and 90%, respectively, and a block resin with LCST value of 33 °C was essential for keeping higher Ar of PGA. Originality/value PGA has become an important biocatalyst in modern chemistry industry. However, disadvantages include difficulty in separation, poor repeatability and high cost, which limits the scope of PGA applications. The effective method is to immobilize the enzyme to the carrier, which could overcome the disadvantage of free enzyme.


NANO ◽  
2021 ◽  
pp. 2150122
Author(s):  
Hongyi Tu ◽  
Yongshan Zhou ◽  
Chunli Liu ◽  
Zhenbin Chen

This work designed and prepared a novel type of carrier for immobilization of penicillin G acylase (PGA), and then the performances of the immobilized PGA were studied in detail. The process is presented as follows: First, dopamine (DA), an adhesive biological secondary metabolite, was adopted to form a polydopamine (PDA) coating on the surface of Fe3O4 nanoparticles (NPs) prepared by the inverse microemulsion method to generate Fe3O4@PDA NPs through in-situ polymerization. After that, the obtained Fe3O4@PDA NPs were modified by reversible addition fragmentation chain transfer (RAFT) reagent containing carboxyl groups on its surface. Then, taking N,N diethyl acrylamide (DEA) as the temperature-sensitive monomer, [Formula: see text]-hydroxyethyl methacrylate (HEMA) as the hydrophilic monomer, glycidyl methacrylate (GMA) as the target monomer and methyl methacrylate (MMA) as the monomer controlling the distance between targets, through the “Grafting from” strategy and the RAFT polymerization method, the magnetic temperature-sensitive polymer composite, Fe3O4@PDA-g-PDEA-b-PHEMA-b-P(MMA-co-GMA) NPs with different feeding ratios of MMA/GMA, was prepared to realize the immobilization of penicillin G acylase (PGA). Based on samples prepared at each stage of the carrier, the structure and performances were characterized by Fourier Infrared Spectroscopy (FTIR), Transmission Electron Microscope (TEM), X-ray Diffraction (XRD), and Vibration Specimen Magnetometer (VSM), respectively. Besides, the content of RAFT graft Fe3O4@PDA was also quantitatively characterized by ICP, and the molecular weight of the polymer was characterized by mass spectrometry. Result showed that the target space influenced enzyme load capacity (ELC), enzyme activity (EA) and enzyme activity recovery rate (EAR) at a large degree, and there was no positive relationship between ELC to EA and EAR. Last, performances of the immobilized PGA, including relative enzyme activity ([Formula: see text]) of immobilized PGA, were 83.9% after storing for 90 days, and 90.3% of the initial activities were still retained after 12 times of repeated use, and the catalytic stability (temperature, pH) and Michaelis–Menten const [Formula: see text] were investigated with free PGA as control if operation was allowed.


Author(s):  
Chunli Liu ◽  
Xudong Wang ◽  
Zhenbin Chen ◽  
Yongshan Zhou ◽  
Juan M Ruso ◽  
...  

2021 ◽  
Vol 312 ◽  
pp. 110762
Author(s):  
Yi Liu ◽  
Haiyan Zhang ◽  
Xuyang Xu ◽  
Xiaoxiao Zhu ◽  
Juan Liu ◽  
...  

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