Magnetic cross-linked enzyme aggregates of acrylamidase from Cupriavidus oxalaticus ICTDB921 for biodegradation of acrylamide from industrial waste water.
作者： Dattatray K Bedade , Abhijeet B Muley , Rekha S Singhal , None
DOI: 10.1016/J.BIORTECH.2018.10.015
关键词:
摘要: Abstract Acrylamidase from Cupriavidus oxalaticus ICTDB921 was immobilized on magnetic nanoparticles (MNPs) for degradation of acrylamide (a group 2A carcinogen and an environmental contaminant) industrial waste water. Acrylamidase-MNPs were prepared (maximum recovery ∼94%) at optimized process parameters viz. 1.5:1 (v/v) acetone: crude acrylamidase/5 mM glutaraldehyde/90 min/1.5:1 enzyme: MNP ratio. MNPs acrylamidase-MNPs characterized by particle size analysis, FTIR, XRD, SEM vibrating sample magnetometer. showed a shift in optimum pH (8–8.5) temperature (60–65 °C) with higher pH/thermal stability vis-a-vis free enzyme. A significant increase kinetic constants, thermal inactivation constants thermodynamic noted acrylamidase-MNPs. complete ∼2100 mg/L achieved water under conditions batch the kinetics best represented Haldane model. retained >80% its initial activity after 4 cycles both pure
sci-hub.se 参考文章(47)
P. López-Serrano, L. Cao, F. van Rantwijk, R.A. Sheldon, Cross-linked enzyme aggregates with enhanced activity: application to lipases Biotechnology Letters. ,vol. 24, pp. 1379- 1383 ,(2002) , 10.1023/A:1019863314646
Johari Ramli, Mohd Arif Syed, Nor Aripin Shamaan, Muhajir Hamid, Neni Gusmanizar, Nina Suhaity Azmi, Mohd. Yunus Abd. Shukor, Isolation and characterization of an acrylamide-degrading Bacillus cereus. Journal of Environmental Biology. ,vol. 30, pp. 57- 64 ,(2009)
A. N. Gorbunova, Yu. G. Maksimova, G. V. Ovechkina, A. Yu. Maksimov, Catalytic and stereoselective properties of the immobilized amidase of Rhodococcus rhodochrous 4-1 Applied Biochemistry and Microbiology. ,vol. 51, pp. 482- 489 ,(2015) , 10.1134/S0003683815050075
Yun Liu, Hua Zhou, Liuyang Wang, Shihui Wang, Stability and catalytic properties of lipase immobilized on chitosan encapsulated magnetic nanoparticles cross‐linked with genipin and glutaraldehyde Journal of Chemical Technology & Biotechnology. ,vol. 91, pp. 1359- 1367 ,(2016) , 10.1002/JCTB.4732
Praveen Kumar Mehta, Shashi Kant Bhatia, Ravi Kant Bhatia, Tek Chand Bhalla, Bench scale production of nicotinic acid using a versatile amide-hydrolysing Geobacillus subterraneus RL-2a isolated from thermal spring of Manikaran, India Journal of Molecular Catalysis B: Enzymatic. ,vol. 105, pp. 58- 65 ,(2014) , 10.1016/J.MOLCATB.2014.04.001
Mona Weideborg, Torsten Källqvist, Knut E Ødegård, Line E Sverdrup, Eilen A Vik, Environmental risk assessment of acrylamide and methylolacrylamide from a grouting agent used in the tunnel construction of Romeriksporten, Norway. Water Research. ,vol. 35, pp. 2645- 2652 ,(2001) , 10.1016/S0043-1354(00)00550-9
N. Burteau, S. Burton, R.R. Crichton, Stabilisation and immobilisation of penicillin amidase FEBS Letters. ,vol. 258, pp. 185- 189 ,(1989) , 10.1016/0014-5793(89)81649-7
Preeti B. Subhedar, Parag R. Gogate, Enhancing the activity of cellulase enzyme using ultrasonic irradiations Journal of Molecular Catalysis B-enzymatic. ,vol. 101, pp. 108- 114 ,(2014) , 10.1016/J.MOLCATB.2014.01.002
J. P. Scott, P. D. Fawell, D. E. Ralph, J. B. Farrow, The shear degradation of high‐molecular‐weight flocculant solutions Journal of Applied Polymer Science. ,vol. 62, pp. 2097- 2106 ,(1996) , 10.1002/(SICI)1097-4628(19961219)62:12<2097::AID-APP12>3.0.CO;2-3
H Igisu, I Goto, Y Kawamura, M Kato, K Izumi, Acrylamide encephaloneuropathy due to well water pollution. Journal of Neurology, Neurosurgery, and Psychiatry. ,vol. 38, pp. 581- 584 ,(1975) , 10.1136/JNNP.38.6.581