Cross-linked enzyme aggregates of arylamidase from Cupriavidus oxalaticus ICTDB921: process optimization, characterization, and application for mitigation of acrylamide in industrial wastewater

作者: Nidhi H Kulkarni , Abhijeet B Muley , Dattatray K Bedade , Rekha S Singhal , None

DOI: 10.1007/S00449-019-02240-4

关键词:

摘要: Acrylamidase produced by Cupriavidus oxalaticus ICTDB921 was recovered directly from the fermentation broth ammonium sulfate (40–50%) precipitation and then stabilized cross-linking with glutaraldehyde. The optimum conditions for preparation of cross-linked enzyme aggregates acrylamidase (acrylamidase-CLEAs) were using 60 mM glutaraldehyde 10 min at 35 °C initial pH 7.0. Acrylamidase-CLEAs characterized SDS-PAGE, FTIR, particle size analyzer SEM. Cross-linking shifted optimal temperature 70 to 50 °C 5–7 6–8, respectively. It also altered secondary structure fractions, thermal stability along kinetic constants, Km Vmax, A complete degradation acrylamide ~ 1.75 g/L in industrial wastewater achieved after 60 min a batch process under operating conditions, kinetics best represented Edward model (R2 = 0.70). retained ~ 40% its activity three cycles both pure acrylamide wastewater, stable 15 days 4 °C, retaining ~ 25% original activity.

参考文章(47)
Kapish Gupta, Asim Kumar Jana, Sandeep Kumar, Mithu Maiti Jana, Solid state fermentation with recovery of Amyloglucosidase from extract by direct immobilization in cross linked enzyme aggregate for starch hydrolysis Biocatalysis and agricultural biotechnology. ,vol. 4, pp. 486- 492 ,(2015) , 10.1016/J.BCAB.2015.07.007
Johari Ramli, Mohd Arif Syed, Nor Aripin Shamaan, Neni Gusmanizar, Mohd Yunus Abd. Shukor, W. P. MacCormack, Isolation and characterization of an acrylamide-degrading Antarctic bacterium. Journal of Environmental Biology. ,vol. 30, pp. 107- 112 ,(2009)
Sachin Talekar, Amol Pandharbale, Mayur Ladole, Shamraja Nadar, Mosin Mulla, Kshitija Japhalekar, Kishori Pattankude, Devika Arage, Carrier free co-immobilization of alpha amylase, glucoamylase and pullulanase as combined cross-linked enzyme aggregates (combi-CLEAs): a tri-enzyme biocatalyst with one pot starch hydrolytic activity. Bioresource Technology. ,vol. 147, pp. 269- 275 ,(2013) , 10.1016/J.BIORTECH.2013.08.035
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
Wenhai Chu, Naiyun Gao, Daqiang Yin, Stuart W. Krasner, Michael R. Templeton, Trace determination of 13 haloacetamides in drinking water using liquid chromatography triple quadrupole mass spectrometry with atmospheric pressure chemical ionization Journal of Chromatography A. ,vol. 1235, pp. 178- 181 ,(2012) , 10.1016/J.CHROMA.2012.02.074
Soofia Khanahmadi, Faridah Yusof, Azura Amid, Safa Senan Mahmod, Mohd Khairizal Mahat, Optimized preparation and characterization of CLEA-lipase from cocoa pod husk Journal of Biotechnology. ,vol. 202, pp. 153- 161 ,(2014) , 10.1016/J.JBIOTEC.2014.11.015
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
Jing-Qi Lai, Zhang-Li Hu, Roger A. Sheldon, Zhen Yang, Catalytic performance of cross-linked enzyme aggregates of Penicillium expansum lipase and their use as catalyst for biodiesel production Process Biochemistry. ,vol. 47, pp. 2058- 2063 ,(2012) , 10.1016/J.PROCBIO.2012.07.024