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Journal articles on the topic 'Immobilized enzyme reactor (IMER)'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Liu, Xiaoxia, Jiqing Yang, and Li Yang. "Capillary electrophoresis-integrated immobilized enzyme reactors." Reviews in Analytical Chemistry 35, no. 3 (September 1, 2016): 115–31. http://dx.doi.org/10.1515/revac-2016-0003.

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AbstractOnline enzyme assay based on capillary electrophoresis (CE) offers several advantages for the assay, such as low consumption of samples, easy automation of all steps, and less requirement of sample work-up. As a widely used approach for online enzyme assay, CE-integrated immobilized enzyme microreactor (IMER) has been applied in almost all aspects of enzyme assays during the past two decades, including evaluation of the enzymatic activity and kinetics, screening of inhibitor, investigation of enzyme-mediated metabolic pathways, and proteome analysis. In a CE-integrated IMER, enzyme is bound to the capillary surface or a suitable carrier attached to the capillary and substrates/products of the enzymatic reaction are separated and online detected by CE at downstream of the capillary. Enzymatic reactions can be viewed as interaction between the stationary phase (immobilized enzyme) and the mobile phase (substrate(s)/co-enzyme(s) solution), in analogy to the well-known separation technique, capillary electrochromatography. From this point of view, CE-integrated IMERs can be categorized into open tubular capillary IMER, monolithic IMER, and packed capillary IMER. In this review, we have surveyed, analyzed, and discussed advances on fabrication techniques of the three categories of CE-integrated IMERs for online assays involving various enzymes in the past two decades (1992–2015). Some recent studies using microfluidic-based IMERs for enzyme assays have also been reviewed.

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2

Yin, Yuqing, Yun Xiao, Guo Lin, Qi Xiao, Zian Lin, and Zongwei Cai. "An enzyme–inorganic hybrid nanoflower based immobilized enzyme reactor with enhanced enzymatic activity." Journal of Materials Chemistry B 3, no. 11 (2015): 2295–300. http://dx.doi.org/10.1039/c4tb01697a.

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Ca₃(PO₄)₂–ChT hybrid nanoflowers were synthesized by a facile approach. The nanoflowers exhibited an enhanced enzymatic activity and can be used as an immobilized enzyme reactor (IMER) for highly efficient protein digestion.

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3

Lin, Zian, Yun Xiao, Ling Wang, Yuqing Yin, Jiangnan Zheng, Huanghao Yang, and Guonan Chen. "Facile synthesis of enzyme–inorganic hybrid nanoflowers and their application as an immobilized trypsin reactor for highly efficient protein digestion." RSC Adv. 4, no. 27 (2014): 13888–91. http://dx.doi.org/10.1039/c4ra00268g.

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Hybrid nanoflowers were synthesized by a novel approach. The nanoflowers exhibited an enhanced enzymatic activity and can be used as an immobilized enzyme reactor (IMER) for highly efficient protein digestion.

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4

Cardoso, Carmem L., Virginia V. Lima, Aderson Zottis, Glaucius Oliva, Adriano D. Andricopulo, Irving W. Wainer, Ruin Moaddel, and Quezia B. Cass. "Development and characterization of an immobilized enzyme reactor (IMER) based on human glyceraldehyde-3-phosphate dehydrogenase for on-line enzymatic studies." Journal of Chromatography A 1120, no. 1-2 (July 2006): 151–57. http://dx.doi.org/10.1016/j.chroma.2005.10.063.

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5

Calil, Felipe Antunes, Juliana Maria Lima, Arthur Henrique Cavalcante de Oliveira, Christiane Mariotini-Moura, Juliana Lopes Rangel Fietto, and Carmen Lucia Cardoso. "Immobilization of NTPDase-1 fromTrypanosoma cruziand Development of an Online Label-Free Assay." Journal of Analytical Methods in Chemistry 2016 (2016): 1–9. http://dx.doi.org/10.1155/2016/9846731.

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The use of IMERs (Immobilized Enzyme Reactors) as a stationary phase coupled to high performance chromatographic systems is an interesting approach in the screening of new ligands. In addition, IMERs offer many advantages over techniques that employ enzymes in solution. The enzyme nucleoside triphosphate diphosphohydrolase (NTPDase-1) fromTrypanosoma cruziacts as a pathogen infection facilitator, so it is a good target in the search for inhibitors. In this paper, immobilization of NTPDase-1 afforded ICERs (Immobilized Capillary Enzyme Reactors). A liquid chromatography method was developed and validated to monitor the ICER activity. The conditions for the application of these bioreactors were investigated, and excellent results were obtained. The enzyme was successfully immobilized, as attested by the catalytic activity detected in theTcNTPDase-1-ICER chromatographic system. Kinetic studies on the substrate ATP gaveKMof 0.317 ± 0.044 mmol·L−1, which still presented high affinity compared to in solution. Besides that, the ICER was stable for 32 days, enough time to investigate samples of possible inhibitors, including especially the compound Suramin, that inhibited 51% the enzyme activity at 100 µmol·L−1, which is in accordance with the data for the enzyme in solution.

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6

Zhu, Yujiao, Qingming Chen, Liyang Shao, Yanwei Jia, and Xuming Zhang. "Microfluidic immobilized enzyme reactors for continuous biocatalysis." Reaction Chemistry & Engineering 5, no. 1 (2020): 9–32. http://dx.doi.org/10.1039/c9re00217k.

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7

Regnier, Fred E., and JinHee Kim. "Accelerating trypsin digestion: the immobilized enzyme reactor." Bioanalysis 6, no. 19 (October 2014): 2685–98. http://dx.doi.org/10.4155/bio.14.216.

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8

Iwaniw, D., C. J. Findlay, and R. Y. Yada. "The Biobone Reactor — an Immobilized Enzyme System." Canadian Institute of Food Science and Technology Journal 21, no. 4 (October 1988): 363. http://dx.doi.org/10.1016/s0315-5463(88)70900-1.

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9

de Oliveira, Karina Bora, Keylla Lençone Mischiatti, José Domingos Fontana, and Brás Heleno de Oliveira. "Tyrosinase immobilized enzyme reactor: Development and evaluation." Journal of Chromatography B 945-946 (January 2014): 10–16. http://dx.doi.org/10.1016/j.jchromb.2013.11.042.

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10

Bernstein, H., and R. Langer. "Ex vivo model of an immobilized-enzyme reactor." Proceedings of the National Academy of Sciences 85, no. 22 (November 1, 1988): 8751–55. http://dx.doi.org/10.1073/pnas.85.22.8751.

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11

Harrington, T. J., J. L. Gainer, and D. J. Kirwan. "Ceramic membrane microfilter as an immobilized enzyme reactor." Enzyme and Microbial Technology 14, no. 10 (October 1992): 813–18. http://dx.doi.org/10.1016/0141-0229(92)90097-8.

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12

Hodgson, Richard J., Travis R. Besanger, Michael A. Brook, and John D. Brennan. "Inhibitor Screening Using Immobilized Enzyme Reactor Chromatography/Mass Spectrometry." Analytical Chemistry 77, no. 23 (December 2005): 7512–19. http://dx.doi.org/10.1021/ac050761q.

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13

Vallat, I., P. Monsan, and J. P. Riba. "Maltodextrin hydrolysis in a fluidized-bed immobilized enzyme reactor." Biotechnology and Bioengineering 28, no. 2 (February 1986): 151–59. http://dx.doi.org/10.1002/bit.260280202.

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14

Sung, Cynthia, Arthur Lavin, Alexander M. Klibanov, and Robert Langer. "An immobilized enzyme reactor for the detoxification of bilirubin." Biotechnology and Bioengineering 28, no. 10 (October 1986): 1531–39. http://dx.doi.org/10.1002/bit.260281011.

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15

Liang, Weina, Zhun Hou, Hairong Wang, Wenfang Xu, and Weihong Wang. "Immobilized Enzyme Reactor Chromatography for Online Gelatinase Inhibitors Screening." Chromatographia 78, no. 11-12 (May 3, 2015): 763–73. http://dx.doi.org/10.1007/s10337-015-2904-0.

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16

Lou, Yi-xin. "Studies on the kinetics of immobilized enzyme using a recycling enzyme reactor system." Biochimie 68, no. 10-11 (November 1986): 1237–43. http://dx.doi.org/10.1016/s0300-9084(86)80070-0.

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17

Mariotti, Marcela Panaro, Hideko Yamanaka, Angela Regina Araujo, and Henrique Celso Trevisan. "Hydrolysis of whey lactose by immobilized β-Galactosidase." Brazilian Archives of Biology and Technology 51, no. 6 (December 2008): 1233–40. http://dx.doi.org/10.1590/s1516-89132008000600019.

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Hydrolysis of whey lactose to glucose and galactose by immobilized galactosidase comes as an alternative to enlarge the possibilities of commercial use of this feedstock. To be applied at industrial scale, the process should be performed continuously .This work aimed to study the hydrolysis of whey lactose by an immobilized enzyme reactor. b-Galactosidase from Aspergillus oryzae was immobilized on silica and activity and stability were evaluated. The best immobilization results were attained by using glutaraldehyde as support's activator and enzyme stabilizer. The optimized enzyme proportion for immobilization was 15-20 mg g-1 of support. Treatments of whey were performed (microfiltration, thermal treatment and ultrafiltration), seeking the elimination of sludge, and the effects on operating the fixed bed reactor were evaluated. Ultrafiltration was the best treatment towards a proper substrate solution for feeding the reactor.

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18

Grant, Jennifer, Justin A. Modica, Juliet Roll, Paul Perkovich, and Milan Mrksich. "An Immobilized Enzyme Reactor for Spatiotemporal Control over Reaction Products." Small 14, no. 31 (July 3, 2018): 1800923. http://dx.doi.org/10.1002/smll.201800923.

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19

Lin, Sheng H. "Optimal feed temperature for an immobilized enzyme packed-bed reactor." Journal of Chemical Technology & Biotechnology 50, no. 1 (April 24, 2007): 17–26. http://dx.doi.org/10.1002/jctb.280500104.

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20

Park, Sung-Soo, Seung Il Cho, Min-Su Kim, Yong-Kweon Kim, and Byung-Gee Kim. "Integration of on-column immobilized enzyme reactor in microchip electrophoresis." ELECTROPHORESIS 24, no. 12 (January 2003): 200–206. http://dx.doi.org/10.1002/elps.200390015.

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21

Liu, Lina, Bo Zhang, Qian Zhang, Yanhong Shi, Liping Guo, and Li Yang. "Capillary electrophoresis-based immobilized enzyme reactor using particle-packing technique." Journal of Chromatography A 1352 (July 2014): 80–86. http://dx.doi.org/10.1016/j.chroma.2014.05.058.

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22

Song, Ju Yeong, and Soo Bae Chung. "Enzyme immobilized reactor design for ammonia removal from waste water." Biotechnology and Bioprocess Engineering 2, no. 2 (December 1997): 77–81. http://dx.doi.org/10.1007/bf02932328.

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23

Sanjay, G., and S. Sugunan. "Immobilization of α-amylase onto K-10 montmorillonite: characterization and comparison of activity in a batch and a fixed-bed reactor." Clay Minerals 40, no. 4 (December 2005): 499–510. http://dx.doi.org/10.1180/0009855054040187.

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Abstractα-amylase was immobilized on acid-activated montmorillonite K-10 via adsorption and covalent linkage. The immobilized enzymes were characterized by X-ray diffraction (XRD), surface area measurements, 27Al nuclear magnetic resonance (NMR) and scanning electron microscopy (SEM). Surface area measurements indicate pore blockage due to linking of the enzyme in the vicinity of the pore mouth. The XRD demonstrates intercalation of enzyme upon immobilization. The NMR studies indicate that, during adsorption, tetrahedral Al sites are involved, while covalent binding occurs exclusively on the octahedral Al sites. The SEM images depict the changed morphology of the clay surface due to immobilization. The efficiency of immobilized enzymes for starch hydrolysis was tested in a batch and a fixed-bed reactor and the performances were compared. The immobilized α-amylase showed a broad pH profile and improved stability characteristics in both reactor types when compared to the free enzyme. The effectiveness factor increased in the fixed-bed reactor, implying that diffusional restrictions to mass transfer operate in the heterogeneous reaction and the use of a fixed-bed reactor leads to a reduction in these diffusional resistances. In the continuous run, 100% initial activity was maintained for 72 h, and after 96 h, >80% activity was retained.

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24

Milosavic, Nenad, Radivoje Prodanovic, Slobodan Jovanovic, Vuk Maksimovic, and Zoran Vujcic. "Characterization of amyloglucosidase immobilized on the copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate in simulated industrial conditions." Chemical Industry 58, no. 11 (2004): 493–98. http://dx.doi.org/10.2298/hemind0411493m.

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The application of amyloglucosidase immobilized on the macroporous co-polymer of ethylene glycol dimethacrylate and glycidyl methacrylate (poly (GMA-co-EGDMA)) in an enzyme reactor was shown. The higher thermostability of immobilized glucoamylases than the soluble one was demonstrated. Immobilized amyloglucosidase obtained by the periodate method shows two times higher thermo stability than the soluble form. Glucoamylases immobilized on poly (GMA-co-EGDMA) have good mechanical and chemical features in the reactor and when applied in a continuous flow reactor for 28 days no changes are observed. In this period periodate immobilized amyloglucosidase shows no decrease in activity. It showed potential for the continuous production of glucose from starch over a prolonged period of time.

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25

Suga, Ken-ichi, Tomoko Sorai, Suteaki Shioya, and Fumihiro Ishimura. "Production of 6-Aminopenicillanic Acid in Immobilized Enzyme Reactor with Electrodialysis." JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 26, no. 6 (1993): 709–14. http://dx.doi.org/10.1252/jcej.26.709.

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26

Mandavilli, Satya Narayana. "Performance Characteristics of an Immobilized Enzyme Reactor Producing Ethanol from Starch." JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 33, no. 6 (2000): 886–90. http://dx.doi.org/10.1252/jcej.33.886.

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27

Hidaka, Nobuyuki, and Toshitatsu Matsumoto. "Gaseous Ethanol Oxidation by Immobilized Enzyme in a Packed Bed Reactor." Industrial & Engineering Chemistry Research 39, no. 4 (April 2000): 909–15. http://dx.doi.org/10.1021/ie990574g.

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28

YASUDA, Kenji, and Yoshinori TAKATA. "Determination of serum urea using an open-tubular immobilized enzyme reactor." Bunseki kagaku 39, no. 11 (1990): 755–60. http://dx.doi.org/10.2116/bunsekikagaku.39.11_755.

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29

Sung Kwan Yoon, Young Je Yoo, and Hyun-Ku Rhee. "Optimal temperature control in a multi-stage immobilized enzyme reactor system." Journal of Fermentation and Bioengineering 68, no. 2 (January 1989): 136–40. http://dx.doi.org/10.1016/0922-338x(89)90062-7.

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30

Hassan, M. M., M. Atiqullah, S. A. Beg, and M. H. M. Chowdhury. "Analysis of non-isothermal tubular reactor packed with immobilized enzyme systems." Chemical Engineering Journal and the Biochemical Engineering Journal 58, no. 3 (August 1995): 275–83. http://dx.doi.org/10.1016/0923-0467(95)06097-9.

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31

Moore, Stephanie, Stephanie Hess, and James Jorgenson. "Characterization of an immobilized enzyme reactor for on-line protein digestion." Journal of Chromatography A 1476 (December 2016): 1–8. http://dx.doi.org/10.1016/j.chroma.2016.11.021.

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32

Ruan, Guihua, Meiping Wei, Zhengyi Chen, Rihui Su, Fuyou Du, and Yanjie Zheng. "Novel regenerative large-volume immobilized enzyme reactor: Preparation, characterization and application." Journal of Chromatography B 967 (September 2014): 13–20. http://dx.doi.org/10.1016/j.jchromb.2014.07.008.

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33

Uttapap, Dudsadee, Yojiro Koba, and Ayaaki Ishizaki. "Continuous Hydrolysis of Starch in Membrane Unit Connected Immobilized Enzyme Reactor." Journal of the Faculty of Agriculture, Kyushu University 33, no. 3/4 (March 1989): 167–75. http://dx.doi.org/10.5109/23926.

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34

Yamamoto, Koki, Kyojiro Morikawa, Hiroyuki Imanaka, Koreyoshi Imamura, and Takehiko Kitamori. "Picoliter enzyme reactor on a nanofluidic device exceeding the bulk reaction rate." Analyst 145, no. 17 (2020): 5801–7. http://dx.doi.org/10.1039/d0an00998a.

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35

NAKAJIMA, Mitsutoshi, Atsuo WATANABE, Hiroshi NABETANI, Hiroyuki HORIKITA, and Shin-ichi NAKAO. "New enzyme reactor with forced flow of the substrate through an enzyme immobilized ceramic membrane." Agricultural and Biological Chemistry 52, no. 2 (1988): 357–65. http://dx.doi.org/10.1271/bbb1961.52.357.

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36

Nakajima, Mitsutoshi, Atsuo Watanabe, Hiroshi Nabetani, Hiroyuki Horikita, and Shin-ichi Nakao. "New Enzyme Reactor with Forced Flow of the Substrate through an Enzyme Immobilized Ceramic Membrane." Agricultural and Biological Chemistry 52, no. 2 (February 1988): 357–65. http://dx.doi.org/10.1080/00021369.1988.10868676.

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37

Cardinal-Watkins, Chantale, and Jim A. Nicell. "Enzyme-Catalyzed Oxidation of 17β-Estradiol Using Immobilized Laccase from Trametes versicolor." Enzyme Research 2011 (August 22, 2011): 1–11. http://dx.doi.org/10.4061/2011/725172.

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Many natural and synthetic estrogens are amenable to oxidation through the catalytic action of oxidative enzymes such as the fungal laccase Trametes versicolor. This study focused on characterizing the conversion of estradiol (E2) using laccase that had been immobilized by covalent bonding onto silica beads contained in a bench-scale continuous-flow packed bed reactor. Conversion of E2 accomplished in the reactor declined when the temperature of the system was changed from room temperature to just above freezing at pH 5 as a result of a reduced rate of reaction rather than inactivation of the enzyme. Similarly, conversion increased when the system was brought to warmer temperatures. E2 conversion increased when the pH of the influent to the immobilized laccase reactor was changed from pH 7 to pH 5, but longer-term experiments showed that the enzyme is more stable at pH 7. Results also showed that the immobilized laccase maintained its activity when treating a constant supply of aqueous E2 at a low mean residence time over a 12-hour period and when treating a constant supply of aqueous E2 at a high mean residence time over a period of 9 days.

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38

Valencia, Pedro, and Francisco Ibañez. "Estimation of the Effectiveness Factor for Immobilized Enzyme Catalysts through a Simple Conversion Assay." Catalysts 9, no. 11 (November 7, 2019): 930. http://dx.doi.org/10.3390/catal9110930.

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A novel methodology to estimate the effectiveness factor (EF) of an immobilized enzyme catalyst is proposed here. The methodology consists of the determination of the productivity of both the immobilized enzyme catalyst and its corresponding soluble enzyme, plotted as a function of the reaction conversion. The ratio of these productivities corresponds to the EF estimator of the catalyst. Conversion curves were simulated in a batch reactor with immobilized enzyme and soluble enzyme for different values of the S0/KM ratio and Thiele modulus (Φ) to demonstrate this hypothesis. Two different reaction orders were tested: first-order kinetic and Michaelis–Menten-based kinetic with product inhibition. The results showed that the ratio of productivities between the immobilized and soluble enzymes followed the behavior profile presented by the EF with satisfactory agreement. This simple methodology to estimate the EF is based on routine conversion experiments, thus avoiding the exhaustive kinetic and mass transfer characterization of the immobilized enzyme catalyst.

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39

Hegedüs, Imre, Marta Vitai, Miklós Jakab, and Endre Nagy. "Study of Prepared α-Chymotrypsin as Enzyme Nanoparticles and of Biocatalytic Membrane Reactor." Catalysts 10, no. 12 (December 11, 2020): 1454. http://dx.doi.org/10.3390/catal10121454.

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Biocatalytic kinetic effect of α-chymotrypsin enzyme has been investigated in its free and pretreated forms (it was covered by a very thin, porous polymer layer, called enzyme nanoparticle) as well as its immobilized form into pores of polysulfone/polyamide asymmetric, hydrophilic membrane. Trimethoxysilyl and acrylamide-bisacrylamide polymers have been used for synthesis of enzyme nanoparticles. Applying Michaelis-Menten kinetics, the KM and vmax values of enzyme-polyacrylamide nanoparticles are about the same, as that of free enzyme. On the other hand, enzyme nanoparticles retain their activity 20–80 fold longer time period than that of the free enzyme, but their initial activity values are reduced to 13–55% of those of free enzymes, at 37 °C. Enzyme immobilized into asymmetric porous membrane layer remained active about 2.3-fold longer time period than that of native enzyme (at pH = 7.4 and at 23 °C), while its reaction rate was about 8-fold higher than that of free enzyme, measured in mixed tank reactor. The conversion degree of substrate was gradually decreased in presence of increasing convective flux of the inlet fluid phase. Biocatalytic membrane reactor has transformed 2.5 times more amount of substrate than the same amount of enzyme nanoparticles and 19 times more amount of substrate than free enzyme, measured in mixed tank reactor.

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40

Bussamara, Roberta, Luciane Dall'Agnol, Augusto Schrank, Kátia Flávia Fernandes, and Marilene Henning Vainstein. "Optimal Conditions for Continuous Immobilization of Pseudozyma hubeiensis (Strain HB85A) Lipase by Adsorption in a Packed-Bed Reactor by Response Surface Methodology." Enzyme Research 2012 (January 23, 2012): 1–12. http://dx.doi.org/10.1155/2012/329178.

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This study aimed to develop an optimal continuous process for lipase immobilization in a bed reactor in order to investigate the possibility of large-scale production. An extracellular lipase of Pseudozyma hubeiensis (strain HB85A) was immobilized by adsorption onto a polystyrene-divinylbenzene support. Furthermore, response surface methodology (RSM) was employed to optimize enzyme immobilization and evaluate the optimum temperature and pH for free and immobilized enzyme. The optimal immobilization conditions observed were 150 min incubation time, pH 4.76, and an enzyme/support ratio of 1282 U/g support. Optimal activity temperature for free and immobilized enzyme was found to be 68°C and 52°C, respectively. Optimal activity pH for free and immobilized lipase was pH 4.6 and 6.0, respectively. Lipase immobilization resulted in improved enzyme stability in the presence of nonionic detergents, at high temperatures, at acidic and neutral pH, and at high concentrations of organic solvents such as 2-propanol, methanol, and acetone.

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41

UCHIYAMA, Shunichi, Yoshinobu TOFUKU, Shuichi SUZUKI, and Giichi MUTO. "Determination of adenosine phosphates by ion chromatography with an immobilized enzyme reactor." Bunseki kagaku 37, no. 2 (1988): 109–12. http://dx.doi.org/10.2116/bunsekikagaku.37.2_109.

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42

MURAKAMI, Kazuo, Michiko KAKEMOTO, Toshikatu HARADA, and Yosehu YAMADA. "High performance liquid chromatographic determination of glucose using an immobilized enzyme reactor." Bunseki kagaku 40, no. 3 (1991): 125–29. http://dx.doi.org/10.2116/bunsekikagaku.40.3_125.

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43

Nenkova, R., R. Atanasova, D. Ivanova, and T. Godjevargova. "Flow Injection Analysis for Amperometric Detection of Glucose with Immobilized Enzyme Reactor." Biotechnology & Biotechnological Equipment 24, no. 3 (January 2010): 1986–92. http://dx.doi.org/10.2478/v10133-010-0058-7.

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44

Cerqueira, Marcos Rodrigues Facchini, Lucio Angnes, and Renato Camargo Matos. "Electrochemical Measurements of Glucose Using a Micro Flow-Through Immobilized Enzyme Reactor." Electroanalysis 29, no. 5 (February 23, 2017): 1474–80. http://dx.doi.org/10.1002/elan.201700038.

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45

Ching, C. B., and K. H. Chu. "Modelling of a fixed bed and a fluidized bed immobilized enzyme reactor." Applied Microbiology and Biotechnology 29, no. 4 (October 1988): 316–22. http://dx.doi.org/10.1007/bf00265813.

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46

Hwang, Hoon, and Purnendu K. Dasgupta. "Flow injection analysis of trace hydrogen peroxide using an immobilized enzyme reactor." Mikrochimica Acta 87, no. 1-2 (January 1985): 77–87. http://dx.doi.org/10.1007/bf01201987.

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47

Shiraishi, F., T. Hasegawa, S. Kasai, N. Makishita, and H. Miyakawa. "Characteristics of apparent kinetic parameters in a packed-bed immobilized enzyme reactor." Chemical Engineering Science 51, no. 11 (June 1996): 2847–52. http://dx.doi.org/10.1016/0009-2509(96)00163-7.

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48

Tataruch, Mateusz, Patrycja Wójcik, Agnieszka M. Wojtkiewicz, Katarzyna Zaczyk, Katarzyna Szymańska, and Maciej Szaleniec. "Application of Immobilized Cholest-4-en-3-one Δ1-Dehydrogenase from Sterolibacterium Denitrificans for Dehydrogenation of Steroids." Catalysts 10, no. 12 (December 14, 2020): 1460. http://dx.doi.org/10.3390/catal10121460.

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Cholest-4-en-3-one Δ1-dehydrogenase (AcmB) from Sterolibacterium denitrificans was successfully immobilized on 3-aminopropyltrimethoysilane functionalized mesoporous cellular foam (MCF) and Santa Barbara Amorphous (SBA-15) silica supports using adsorption or covalently with glutaraldehyde or divinyl sulfone linkers. The best catalyst, AcmB on MCF linked covalently with glutaraldehyde, retained the specific activity of the homogenous enzyme while exhibiting a substantial increase of the operational stability. The immobilized enzyme was used continuously in the fed-batch reactor for 27 days, catalyzing 1,2-dehydrogenation of androst-4-en-3-one to androst-1,4-dien-3-one with a final yield of 29.9 mM (8.56 g/L) and 99% conversion. The possibility of reuse of the immobilized catalyst was also demonstrated and resulted in a doubling of the product amount compared to that in the reference homogenous reactor. Finally, it was shown that molecular oxygen from the air can efficiently be used as an electron acceptor either reoxidizing directly the enzyme or the reduced 2,4-dichlorophenolindophenol (DCPIPH2).

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49

Miyawaki, Osato, and Toshimasa Yano. "Dynamic affinity between dissociable coenzyme and immobilized enzyme in an affinity chromatographic reactor with single enzyme." Biotechnology and Bioengineering 39, no. 3 (February 5, 1992): 314–19. http://dx.doi.org/10.1002/bit.260390309.

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Besanger, Travis R., Richard J. Hodgson, James R. A. Green, and John D. Brennan. "Immobilized enzyme reactor chromatography: Optimization of protein retention and enzyme activity in monolithic silica stationary phases." Analytica Chimica Acta 564, no. 1 (March 2006): 106–15. http://dx.doi.org/10.1016/j.aca.2005.12.066.

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