[1] Talekar, S., Desai, S., Pillai, M., & Nadar, S.S. (2013). Carrier free co-immobilization of glucoamylase and pullulanase as combi-cross linked enzyme aggregates (combi-CLEAs).
RSC Adv., 3(7), 2265-2271.
[2] Punia Bangar, S., Sunooj, K. V., Navaf, M., Phimolsiripol, Y., & Whiteside, W. S. (2024). Recent advancements in cross-linked starches for food applications- a review. Int. J. Food Prop., 27(1), 411-430.
[4] Rehman, S., Nawaz Bhatti, H., Bilal, M., & Asgher, M. (2016). Cross-linked enzyme aggregates (CLEAs) of Pencilluim notatum lipase enzyme with improved activity, stability, and reusability characteristics,
Int. J. Biol. Macromol., 91, 1161-1169.
https://doi.org/10.1016/j.ijbiomac.2016.06.081.
[5] Xu, M. Q., Wang, S. S., Li, L. N., Gao, J., & Zhang, Y. W. (2018). Combined coross-linked enzyme aggregates as biocatalysts,
Catalyst, 8, 460.
https://doi.org/10.3390/catal8100460.
[6] Min, Y., Yi, J., Dai, R., Liu, W., & Chen, H. (2023). A Novel Efficient Wet Process for Preparing Cross-Linked Starch: Impact of Urea on Cross-Linking Performance. Carbohydr. Polym., 320, 121247. DOI: 10.1016/j.carbpol.2023.121247.
[7] Torabizadeh, H., & Montazeri, E. (2020). Nano co-immobilization of α-amylase and Maltogenic amylase by nanomagnetic combi-cross-linked enzyme aggregates method for maltose production from corn starch.
Carbohydr. Res., 488, 107904.
https://doi.org/10.1016/j.carres.2019.107904.
[8] Torabizadeh, H., & Mahmoudi, A. (2018). Inulin hydrolysis by inulinase immobilized covalently on magnetic nanoparticles prepared with wheat gluten hydrolysates, Biotechnol. Reports., 17, 97–103. https://doi.org/10.1016/j.btre.2018.02.004.
[9] Mahmoudi, A., & Torabizadeh, H. (2018). Nanomagnetic wheat gluten hydrolysates a new carrier for nanoimmobilization of inulinase, Int. J. Biol. Macromol., 117, 108–113. https://doi.org/10.3390/catal8050174.
[10] Torabizadeh, H., & Mikani, M. (2018). Nano-magnetic cross-linked enzyme aggregates of naringinase an efficient nanobiocatalyst for naringin hydrolysis, Int. J. Biol. Macromol., 117, 134–143. https://doi.org/10.1016/J.IJBIOMAC.2018.05.162.
[11] Torabizadeh, H., & Mikani, M. (2018). Kinetic and thermodynamic features of nanomagnetic cross-linked enzyme aggregates of naringinase nanobiocatalyst in naringin hydrolysis, Int. J. Biol. Macromol., 119, 717–725. https://doi.org/10.1016/j.ijbiomac.2018.08.005.
[12] Torabizadeh, H., Tavakoli, M., & Safari, M. (2014). Immobilization of thermostable α-amylase from Bacillus licheniformis by cross-linked enzyme aggregates method using calcium and sodium ions as additives, J. Mol. Catal. B Enzym. 108, 13–20. https://doi.org/10.1016/J.MOLCATB.2014.06.005.
[13] Xie, W., & Wang, J. (2014). Enzymatic Production of Biodiesel from Soybean Oil by Using Immobilized Lipase on Fe3O4/Poly(styrene-methacrylic acid) Magnetic Microsphere as a Biocatalyst, EnFL., 28, 2624–2631.
https://doi.org/10.1021/EF500131S.
[14] Blanco-Llamero, C., Garcia-Garcia, P., & Senorans, F. J. (2021). Cross-linked enzyme aggregates and their application in enzymatic pretreatment of microalgae: comparison between CLEAs and combi-CLEAs,
Front. Bioeng. Biotechnol., 9, 1-11.
https://doi.org/10.3389/fbioe.2021794672.
[15] Cruz-Izquierdo, A., Picó, E. A., López, C., Serra, J. L., & Llama, M. J. (2014). Magnetic Cross-Linked Enzyme Aggregates (mCLEAs) of Candida antarctica lipase: An efficient and stable biocatalyst for biodiesel synthesis, PLoS One., 9, 1–22. https://doi.org/10.1371/journal.pone.0115202.
[16] Sheldon, R. A., Von Pelt, S., Kanbak-Aksu, S., & Janssen, S.M.H.A. (2013). Cross-linked enzyme aggregates (CLEAs) in organic sythesis, Aldrichim. ACTA., 46(3), 81-93.
[17] Miller, G. L. (1959). Use of dinitrosalicylic acid reagent fordetermination of reducing sugar. Anal. Chem., 31, 426e8.
19] Baltulionis, G., Blight, M., Robin, A., Charalampopoulos, D., & Watson, K. A. (2021). propeptide-mediated autoinhibition and intermolecular chaperone in the maturation of cognate catalytic domain in leucine aminopeptidase,
J. Struct. Biol., 213, 107741-107741.
https://doi.org/10.1016/j.jsb.2021.107741.
[20] Tutar, H., Yilmaz, E., Pehlivan, E., & Yilmaz, M. (2009). Immobilization of Candida rugosa lipase on sporopollenin from Lycopodium clavatum,
Int. J. Biol. Macromol., 45, 315–320.
https://doi.org/10.1016/J.IJBIOMAC.2009.06.014.
[21] Bié, J., Sepodes, B., Fernandes, P.C.B ., & Ribeiro, M.H.L. (2022). Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications,
Processes., 10(3), 494;
https://doi.org/10.3390/pr10030494.
[22] Perwez, M., Mazumder, J.A., Noori, R., & Sardar, M. (2021). Magnetic combi CLEA for inhibition of bacterial biofilm: A green approach, Int. J. Biol. Macromol., 186, 780–787. https://doi.org/10.1016/J.IJBIOMAC.2021.07.091.
[23] Yu, D., Ma, X., Huang, Y., Jiang, L., Wang, L., Han, C., & Yang, F. (2022). Immobilization of cellulase on magnetic nanoparticles for rice bran oil extraction in a magnetic fluidized bed, Int. J. Food Eng., 18, 15–26. https://doi.org/10.1515/ijfe-2021-0111.
[24] Mikani, M., Torabizadeh, H., & Rahmanian, R. (2018). Magnetic soy protein isolate–bovine serum albumin nanoparticles preparation as a carrier for inulinase immobilization,
IET Nanobiotechnol., 12, 633–639.
https://doi.org/10.1049/IET-NBT.2017.0188.
[25] Royhaila Mohamad, N., Haziqah, N., Marzuki, C., Buang, A., Huyop, F., & Wahab, R. A. (2015). An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes,
Agric. Environ. Biotechnol, 29(2), 205-220.
https://doi.org/10.1080/13102818.2015.1008192.
[26] Cruz-Izquierdo, A., Picó, E. A., Anton-Helas, Z., Boeriu, C. G., Llama, M. J., & Serra, J. L. (2012). Lipase immobilization to magnetic nanoparticles: methods, properties and applications for biobased products,
N. Biotechnol., 29, S100–S101.
https://doi.org/10.1016/J.NBT.2012.08.283.
[27] Sailaja AK, C. P., & Amareshwar P. (2011). Different techniques used for the preparation of nanoparticles using natural polymers and their application., Int J Pharm Pharm Sci., 3, 45–50.
[28] Torabizadeh, H., Habibi-Rezaei, M., Safari, M., Moosavi-Movahedi, A. A., &Razavi, S. H. (2010). Semi-rational chemical modification of endoinulinase by pyridoxal 5′-phosphate and ascorbic acid, J. Mol. Catal. B Enzym., 62, 257–264. https://doi.org/10.1016/J.MOLCATB.2009.10.007.
[29] Torabizadeh, H., Habibi-Rezaei, M., Safari, M., Moosavi-Movahedi, A. A., Sharifizadeh, A., Azizian, H., & Amanlou, M. (2011). Endo-inulinase Stabilization by Pyridoxal Phosphate Modification: A Kinetics, Thermodynamics, and Simulation Approach,
Appl. Biochem. Biotechnol., 165, 1661–1673.
https://doi.org/10.1007/S12010-011-9385-X.
[30] Barbosa, O., Ortiz, C., Berenguer-Murcia, A., Torres, R., Rodrigues, R. C., & Fernandez-Lafuente, R. (2015). Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts, Biotechnol. Adv., 33, 435–456. https://doi.org/10.1016/J.BIOTECHADV.2015.03.006.
[31] Mohamad, N.R., Marzuki, N.H.C., Buang, N.A.,Huyop, F., & Wahab, R. A. (2015). An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes, Biotechnol. Biotechnol. Equip., 29, 205–220. https://doi.org/10.1080/13102818.2015.1008192.
[32] Kochane, T., Zabarauske, I., Klimkeviciene, L., Straksys, A., Maciulyte, S., Navickaite, L., Gailiunaite, S., & Budriene, S. (2020). Starch hydrolysis using maltogenase immobilized via different techniques,
Int. J. Biol. Macromol., 144, 544-552.
https://doi.org/10.1016/j.ijbiomac.2019.12.131.
[33] Gupta, K., Kumar Jana, A., Kumar, S., & Maiti Jana, M. (2015). Solid state fermentation with recovery of amyloglucosidase from extract by direct immobilization in cross linked enzyme aggregates for starch hydrolysis,
Biocatal. Agric. Biotechnol., 4, 486-492.
https://doi.org/10.1016/j.bcab.2015.07.007.