1 3
Topics in Current Chemistry (2020) 378:12
108. Fortes CCS, Daniel-da-Silva AL, Xavier AMRB, Tavares APM (2017) Optimization of enzyme
immobilization on functionalized magnetic nanoparticles for laccase biocatalytic reactions. Chem
Eng Process Process Intensif 117:1–8. https ://doi.org/10.1016/j.cep.2017.03.009
109. Poorakbar E, Shafiee A, Saboury AA et al (2018) Synthesis of magnetic gold mesoporous silica
nanoparticles core shell for cellulase enzyme immobilization: improvement of enzymatic activity
and thermal stability. Process Biochem 71:92–100. https ://doi.org/10.1016/j.procb io.2018.05.012
110. Badgujar KC, Bhanage BM (2017) Investigation of deactivation thermodynamics of lipase immobilized on polymeric carrier. Bioprocess Biosyst Eng 40:741–757. https ://doi.org/10.1007/s0044
9-017-1740-z
111. Nadar SS, Rathod VK (2016) Magnetic macromolecular cross linked enzyme aggregates
(CLEAs) of glucoamylase. Enzyme Microb Technol 83:78–87. https ://doi.org/10.1016/j.enzmi
ctec.2015.10.009
112. Facin BR, Valério A, Bresolin D et al (2018) Improving reuse cycles of Thermomyces lanuginosus lipase (NS-40116) by immobilization in flexible polyurethane. Biocatal Biotransf 36:372–380.
https ://doi.org/10.1080/10242 422.2018.14588 42
113. Leidner A, Bauer J, Ebrahimi Khonachah M et al (2019) Oriented immobilization of a delicate
glucose-sensing protein on silica nanoparticles. Biomaterials 190:76–85. https ://doi.org/10.1016/j.
bioma teria ls.2018.10.035
114. Nicolás P, Lassalle V, Ferreira ML (2018) Immobilization of CALB on lysine-modified magnetic
nanoparticles: influence of the immobilization protocol. Bioprocess Biosyst Eng 41:171–184. https
://doi.org/10.1007/s0044 9-017-1855-2
115. Liu DM, Chen J, Shi YP (2018) Tyrosinase immobilization on aminated magnetic nanoparticles by
physical adsorption combined with covalent crosslinking with improved catalytic activity, reusability and storage stability. Anal Chim Acta 1006:90–98. https ://doi.org/10.1016/j.aca.2017.12.022
116. Tabarzad M, Sharafi Z, Javidi J (2018) Covalent immobilization of coagulation factor VIII on magnetic nanoparticles for aptamer development. J Appl Biomater Funct Mater 16:161–170. https ://
doi.org/10.1177/22808 00018 76504 6
117. Waifalkar PP, Parit SB, Chougale AD et al (2016) Immobilization of invertase on chitosan coated
γ-Fe 2 O 3 magnetic nanoparticles to facilitate magnetic separation. J Colloid Interface Sci 482:159–
164. https ://doi.org/10.1016/j.jcis.2016.07.082
118. Ortiz E, Gallay P, Galicia L et al (2019) Nanoarchitectures based on multi-walled carbon nanotubes non-covalently functionalized with Concanavalin A: a new building-block with supramolecular recognition properties for the development of electrochemical biosensors. Sensors Actuators, B
Chem 292:254–262. https ://doi.org/10.1016/j.snb.2019.04.114
119. Kadu K, Ghosh G, Panicker L et al (2019) Role of surface charges on interaction of rod-shaped
magnetic hydroxyapatite nanoparticles with protein. Colloids Surfaces B Biointerfaces 177:362–
369. https ://doi.org/10.1016/j.colsu rfb.2019.02.021
120. Li D, Huang X, Wu Y et al (2016) Preparation of pH-responsive mesoporous hydroxyapatite nanoparticles for intracellular controlled release of an anticancer drug. Biomater Sci 4:272–280. https ://
doi.org/10.1039/c5bm0 0228a
121. Satzer P, Svec F, Sekot G, Jungbauer A (2016) Protein adsorption onto nanoparticles induces conformational changes: particle size dependency, kinetics, and mechanisms. Eng Life Sci 16:238–
246. https ://doi.org/10.1002/elsc.20150 0059
122. Martínez-Carmona M, Lozano D, Colilla M, Vallet-Regí M (2018) Lectin-conjugated pH-responsive mesoporous silica nanoparticles for targeted bone cancer treatment. Acta Biomater 65:393–
404. https ://doi.org/10.1016/j.actbi o.2017.11.007
123. Koshkina O, Lang T, Thiermann R et al (2015) Temperature-triggered protein adsorption on polymer-coated nanoparticles in serum. Langmuir 31:8873–8881. https ://doi.org/10.1021/acs.langm
uir.5b005 37
124. Cortés FB, Montoya T, Acevedo S et al (2018) Adsorption-desorption of n–C7 asphaltenes over
micro- and nanoparticles of silica and its impact on wettability alteration. CTF Cienc Tecnol
Futuro 6:89–106. https ://doi.org/10.29047 /01225 383.06
125. Cao Y, Wen L, Svec F et al (2016) Magnetic AuNP@Fe3O4 nanoparticles as reusable carriers for reversible enzyme immobilization. Chem Eng J 286:272–281. https ://doi.org/10.1016/j.
cej.2015.10.075
126. Meissner J, Prause A, Bharti B, Findenegg GH (2015) Characterization of protein adsorption onto
silica nanoparticles: influence of pH and ionic strength. Colloid Polym Sci 293:3381–3391. https ://
doi.org/10.1007/s0039 6-015-3754-x
125
Reprinted from the journal
Topics in Current Chemistry (2020) 378:12
108. Fortes CCS, Daniel-da-Silva AL, Xavier AMRB, Tavares APM (2017) Optimization of enzyme
immobilization on functionalized magnetic nanoparticles for laccase biocatalytic reactions. Chem
Eng Process Process Intensif 117:1–8. https ://doi.org/10.1016/j.cep.2017.03.009
109. Poorakbar E, Shafiee A, Saboury AA et al (2018) Synthesis of magnetic gold mesoporous silica
nanoparticles core shell for cellulase enzyme immobilization: improvement of enzymatic activity
and thermal stability. Process Biochem 71:92–100. https ://doi.org/10.1016/j.procb io.2018.05.012
110. Badgujar KC, Bhanage BM (2017) Investigation of deactivation thermodynamics of lipase immobilized on polymeric carrier. Bioprocess Biosyst Eng 40:741–757. https ://doi.org/10.1007/s0044
9-017-1740-z
111. Nadar SS, Rathod VK (2016) Magnetic macromolecular cross linked enzyme aggregates
(CLEAs) of glucoamylase. Enzyme Microb Technol 83:78–87. https ://doi.org/10.1016/j.enzmi
ctec.2015.10.009
112. Facin BR, Valério A, Bresolin D et al (2018) Improving reuse cycles of Thermomyces lanuginosus lipase (NS-40116) by immobilization in flexible polyurethane. Biocatal Biotransf 36:372–380.
https ://doi.org/10.1080/10242 422.2018.14588 42
113. Leidner A, Bauer J, Ebrahimi Khonachah M et al (2019) Oriented immobilization of a delicate
glucose-sensing protein on silica nanoparticles. Biomaterials 190:76–85. https ://doi.org/10.1016/j.
bioma teria ls.2018.10.035
114. Nicolás P, Lassalle V, Ferreira ML (2018) Immobilization of CALB on lysine-modified magnetic
nanoparticles: influence of the immobilization protocol. Bioprocess Biosyst Eng 41:171–184. https
://doi.org/10.1007/s0044 9-017-1855-2
115. Liu DM, Chen J, Shi YP (2018) Tyrosinase immobilization on aminated magnetic nanoparticles by
physical adsorption combined with covalent crosslinking with improved catalytic activity, reusability and storage stability. Anal Chim Acta 1006:90–98. https ://doi.org/10.1016/j.aca.2017.12.022
116. Tabarzad M, Sharafi Z, Javidi J (2018) Covalent immobilization of coagulation factor VIII on magnetic nanoparticles for aptamer development. J Appl Biomater Funct Mater 16:161–170. https ://
doi.org/10.1177/22808 00018 76504 6
117. Waifalkar PP, Parit SB, Chougale AD et al (2016) Immobilization of invertase on chitosan coated
γ-Fe 2 O 3 magnetic nanoparticles to facilitate magnetic separation. J Colloid Interface Sci 482:159–
164. https ://doi.org/10.1016/j.jcis.2016.07.082
118. Ortiz E, Gallay P, Galicia L et al (2019) Nanoarchitectures based on multi-walled carbon nanotubes non-covalently functionalized with Concanavalin A: a new building-block with supramolecular recognition properties for the development of electrochemical biosensors. Sensors Actuators, B
Chem 292:254–262. https ://doi.org/10.1016/j.snb.2019.04.114
119. Kadu K, Ghosh G, Panicker L et al (2019) Role of surface charges on interaction of rod-shaped
magnetic hydroxyapatite nanoparticles with protein. Colloids Surfaces B Biointerfaces 177:362–
369. https ://doi.org/10.1016/j.colsu rfb.2019.02.021
120. Li D, Huang X, Wu Y et al (2016) Preparation of pH-responsive mesoporous hydroxyapatite nanoparticles for intracellular controlled release of an anticancer drug. Biomater Sci 4:272–280. https ://
doi.org/10.1039/c5bm0 0228a
121. Satzer P, Svec F, Sekot G, Jungbauer A (2016) Protein adsorption onto nanoparticles induces conformational changes: particle size dependency, kinetics, and mechanisms. Eng Life Sci 16:238–
246. https ://doi.org/10.1002/elsc.20150 0059
122. Martínez-Carmona M, Lozano D, Colilla M, Vallet-Regí M (2018) Lectin-conjugated pH-responsive mesoporous silica nanoparticles for targeted bone cancer treatment. Acta Biomater 65:393–
404. https ://doi.org/10.1016/j.actbi o.2017.11.007
123. Koshkina O, Lang T, Thiermann R et al (2015) Temperature-triggered protein adsorption on polymer-coated nanoparticles in serum. Langmuir 31:8873–8881. https ://doi.org/10.1021/acs.langm
uir.5b005 37
124. Cortés FB, Montoya T, Acevedo S et al (2018) Adsorption-desorption of n–C7 asphaltenes over
micro- and nanoparticles of silica and its impact on wettability alteration. CTF Cienc Tecnol
Futuro 6:89–106. https ://doi.org/10.29047 /01225 383.06
125. Cao Y, Wen L, Svec F et al (2016) Magnetic AuNP@Fe3O4 nanoparticles as reusable carriers for reversible enzyme immobilization. Chem Eng J 286:272–281. https ://doi.org/10.1016/j.
cej.2015.10.075
126. Meissner J, Prause A, Bharti B, Findenegg GH (2015) Characterization of protein adsorption onto
silica nanoparticles: influence of pH and ionic strength. Colloid Polym Sci 293:3381–3391. https ://
doi.org/10.1007/s0039 6-015-3754-x
125
Reprinted from the journal