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Journal articles on the topic 'Enzymatic immobilisation'

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Author: Grafiati

Published: 14 March 2023

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1

Schartner, Jonas, Jörn Güldenhaupt, Sarah Katharina Gaßmeyer, Katharina Rosga, Robert Kourist, Klaus Gerwert, and Carsten Kötting. "Highly stable protein immobilizationviamaleimido-thiol chemistry to monitor enzymatic activity." Analyst 143, no. 10 (2018): 2276–84. http://dx.doi.org/10.1039/c8an00301g.

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2

Küchler, Andreas, Jozef Adamcik, Raffaele Mezzenga, A. Dieter Schlüter, and Peter Walde. "Enzyme immobilization on silicate glass through simple adsorption of dendronized polymer–enzyme conjugates for localized enzymatic cascade reactions." RSC Advances 5, no. 55 (2015): 44530–44. http://dx.doi.org/10.1039/c5ra06268c.

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3

Agustian, Joni, and Lilis Hermida. "The Optimised Statistical Model for Enzymatic Hydrolysis of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica." Bulletin of Chemical Reaction Engineering & Catalysis 14, no. 2 (August 1, 2019): 380. http://dx.doi.org/10.9767/bcrec.14.2.3078.380-390.

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Enzymatic hydrolysis of starches using free glucoamylase to reducing sugars have difficulties in recovering and recycling of the enzyme, hence immobilisation on inert supports were widely studied. However, effectiveness of the immobilised glucoamylase were merely observed only on soluble starches. It was considered a valuable thing to know performance of glucoamylase on Mesostructured Cellular Foam (MCF) silica in hydrolysing of tapioca. An optimised study on enzymatic hydrolysis of tapioca using glucoamylase on MCF silica (9.2T-3D) and its kinetics were described including justification of the predicted model as it was required to develop in large scale operations. Central Composite Design was used to model the process by studying effects of three factors on DE values after enzyme immobilisation. Immobilisation of glucoamylase on this support gave up to 82% efficiency with the specific activity of 1,856.78 U.g-1. Its used to hydrolysis of tapioca resulted DE values of 1.740-76.303% (w/w) where the highest DE was obtained at pH of 4.1, temperature of 70 ℃ and agitation speed of 140 rpm. The optimisation produced a polynomial quadratic model having insignificant lack-of-fit and low standard deviation, so that it was applicable and reliable in simulating the DE with only 0.80% of data were not described. Temperature affected the process highly, but the buffer pH, agitation speed and factorial interactions were considered not important. KM value for immobilised enzyme was better than the free glucoamylase, however, its reaction rate was slower than the free glucoamylase catalysis. Copyright © 2019 BCREC Group. All rights reserved

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4

Wang, Yichao, Shuang Zhang, Enamul Haque, Bao Yue Zhang, Jian Zhen Ou, Jing Liu, Zhongqing Liu, et al. "Immobilisation of microperoxidase-11 into layered MoO3 for applications of enzymatic conversion." Applied Materials Today 16 (September 2019): 185–92. http://dx.doi.org/10.1016/j.apmt.2019.05.008.

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5

Avci Duman, Yonca, Gamze Tufan, and A. Uğur Kaya. "Immobilisation of cellulase on vermiculite and the effects on enzymatic kinetics and thermodynamics." Applied Clay Science 197 (November 2020): 105792. http://dx.doi.org/10.1016/j.clay.2020.105792.

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6

Campanella, L., G. Favero, M. P. Sammartino, and M. Tomassetti. "Enzymatic immobilisation in kappa-carrageenan gel suitable for organic phase enzyme electrode (OPEE) assembly." Journal of Molecular Catalysis B: Enzymatic 7, no. 1-4 (September 1999): 101–13. http://dx.doi.org/10.1016/s1381-1177(99)00035-1.

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7

Pramparo, L., F. Stüber, J. Font, A. Fortuny, A. Fabregat, and C. Bengoa. "Immobilisation of horseradish peroxidase on Eupergit®C for the enzymatic elimination of phenol." Journal of Hazardous Materials 177, no. 1-3 (May 2010): 990–1000. http://dx.doi.org/10.1016/j.jhazmat.2010.01.017.

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8

Hannig, C., B. Spitzmüller, H. C. Lux, M. Altenburger, A. Al-Ahmad, and M. Hannig. "Efficacy of enzymatic toothpastes for immobilisation of protective enzymes in the in situ pellicle." Archives of Oral Biology 55, no. 7 (July 2010): 463–69. http://dx.doi.org/10.1016/j.archoralbio.2010.03.020.

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9

Grosová, Z., M. Rosenberg, and M. Rebroš. "Perspectives and applications of immobilised β-galactosidase in food industry – a review." Czech Journal of Food Sciences 26, No. 1 (February 19, 2008): 1–14. http://dx.doi.org/10.17221/1134-cjfs.

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β-Galactosidase is an important industrial enzyme in the hydrolysis of milk and whey lactose. The enzymatic hydrolysis of lactose allows to avoid health and environmental problems posed by this disaccharide. In addition, this enzyme catalyses the formation of galacto-oligosaccharides, which are prebiotic additives for the so-called “healthy foods”. β-Galactosidase is one of the relatively few enzymes that have been used in large-scale processes in both free and immobilised forms. This article presents a review of recent trends in immobilisation of β-galactosidase and their application in food industry.

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10

Hannig, C., B. Spies, B. Spitzmüller, and M. Hannig. "Efficacy of enzymatic mouth rinses for immobilisation of protective enzymes in the in situ pellicle." Archives of Oral Biology 55, no. 1 (January 2010): 1–6. http://dx.doi.org/10.1016/j.archoralbio.2009.10.004.

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11

Czyzewska, Katarzyna, and Anna Trusek. "Critical Parameters in an Enzymatic Way to Obtain the Unsweet Lactose-Free Milk Using Catalase and Glucose Oxidase Co-Encapsulated into Hydrogel with Chemical Cross-Linking." Foods 12, no. 1 (December 26, 2022): 113. http://dx.doi.org/10.3390/foods12010113.

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The presented work involves obtaining and characterising a two-enzymatic one-pot bioreactor, including encapsulated (co-immobilised) glucose oxidase and catalase. The enzymatic capsules were applied to produce unsweet, lactose-free milk during low-temperature catalysis. Furthermore, operational conditions, like pH and aeration, were selected in the paper, which sorts out discrepancies in literature reports. All experiments were carried out at 12 °C, corresponding to milk storage and transportation temperature. Preliminary studies (for reasons of analytical accuracy) were carried out in a buffer (pH, concentration of sugars mimicking conditions in the lactose-free milk, the initial glucose concentration 27.5 g/L) verified by processes carried out in milk in the final stage of the study. The presented results showed the need for regulating pH and the aeration of the reaction mixture in the continuous mode during the process. The procedure of co-immobilisation was performed in an alginate matrix with the cross-linking of glutaraldehyde or carbodiimide while carbodiimide showed better enzymes retention inside alginate capsules. Co-encapsulated enzymes could be used for nine cycles, preserving finally about 40% of the initial activity.

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12

Ikechukwu Iloh Udema. "Association-dissociation equations, distinct from Michaelis-Menten equation for the quantification of the net flux of reactants with or without immobiliser." GSC Biological and Pharmaceutical Sciences 13, no. 1 (October 30, 2020): 231–43. http://dx.doi.org/10.30574/gscbps.2020.13.1.0335.

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The formation of enzyme-substrate complex, often in connection with the adsorption of the enzyme leading to either partial immobilisation in which the enzymes are adsorbed on a colloid or total immobilisation in which the enzyme is adsorbed on a rigid immobile phase is the concern of some researchers. The interest in immobilised substrate common in biological system is not very common. The objectives of this theoretical research are the rederivation of the equations of association and dissociation of reactants in the presence of adsorbents, insoluble larger macro-or supra-molecule and elucidation of why such equations are important and generalisable. The derivations produced two different equations that describe mathematically the net flux of either the substrate where the enzyme is adsorbed or the net flux of the enzyme where the substrate is adsorbed. The derivation also produced equations of translational velocities, given the probabilities that reactions occur following complex formation or that an escape of bullet molecules or dissociation reactions occur. In conclusion two different equations need separate derivation for association and dissociation of reactants. The needs for the flux of reactants have both biological and industrial relevance, respectively due to importance of time-dependent digestive processes and for the optimisation of the production of desired products of enzymatic action. The equations describing net flux seem generalisable in that information about the physicochemical properties of both crowding agent and immobilisers may not be needed for calculations.

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13

Boland, Susan, and Dónal Leech. "A glucose/oxygen enzymatic fuel cell based on redox polymer and enzyme immobilisation at highly-ordered macroporous gold electrodes." Analyst 137, no. 1 (2012): 113–17. http://dx.doi.org/10.1039/c1an15537g.

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14

Hou, Juan, Xingkang Li, Michal Kaczmarek, Pengyu Chen, Kai Li, Peng Jin, Yuanmei Liang, and Maurycy Daroch. "Accelerated CO2 Hydration with Thermostable Sulfurihydrogenibium azorense Carbonic Anhydrase-Chitin Binding Domain Fusion Protein Immobilised on Chitin Support." International Journal of Molecular Sciences 20, no. 6 (March 25, 2019): 1494. http://dx.doi.org/10.3390/ijms20061494.

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Carbonic anhydrases (CAs) represent a group of enzymes that catalyse important reactions of carbon dioxide hydration and dehydration, a reaction crucial to many biological processes and environmental biotechnology. In this study we successfully constructed a thermostable fusion enzyme composed of the Sulfurihydrogenibium azorense carbonic anhydrase (Saz_CA), the fastest CA discovered to date, and the chitin binding domain (ChBD) of chitinase from Bacillus circulans. Introduction of ChBD to the Saz_CA had no major impact on the effect of ions or inhibitors on the enzymatic activity. The fusion protein exhibited no negative effects up to 60 °C, whilst the fusion partner appears to protect the enzyme from negative effects of magnesium. The prepared biocatalyst appears to be thermally activated at 60 °C and could be partially purified with heat treatment. Immobilisation attempts on different kinds of chitin-based support results have shown that the fusion enzyme preferentially binds to a cheap, untreated chitin with a large crystallinity index over more processed forms of chitin. It suggests significant potential economic benefits for large-scale deployment of immobilised CA technologies such as CO2 utilisation or mineralisation.

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15

Karunakaran, Chandran, Murugesan Karthikeyan, Marimuthu Dhinesh Kumar, Ganesan Kaniraja, and Kalpana Bhargava. "Electrochemical Biosensors for Point of care Applications." Defence Science Journal 70, no. 5 (October 8, 2020): 549–56. http://dx.doi.org/10.14429/dsj.70.16359.

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Biosensor refers to powerful and innovative analytical tool involving biological sensing element and transducer with broad range of applications, such as diagnosis, drug discovery, biomedicine, food safety and processing, environmental monitoring, security and defense. Recent advances in the field of biotechnology, microelectronics, and nanotechnology have improved the development of biosensors. Glucometers utilizing the electrochemical determination of oxygen or hydrogen peroxide employing immobilised glucose oxidase electrode seeded the discovery and development of biosensors. Molecular recognition based on geometry and forces of interaction play an important role in the biosensor development. The advent of nanotechnology led to highly efficient and sensitive biosensors. They also provide an effective immobilisation matrix for the various bioreceptors. Enzymatic and their mimetic (metalloporphyrin)-based biosensors for reactive oxygen, nitrogen species and cytochrome c will also be discussed. The role of antibodies and their applications in immunosensors development for cytochrome c and superoxide dismutase will be highlighted. The electrochemical biosensors are less expensive, miniaturised and used for point-of-care applications. Further, the fabrication of labVIEW based virtual biosensor instrumentation and microcontroller based portable biosensor for wide variety of applications also devices will be presented.

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16

McCormick, Wesley, Pádraig McDonagh, John Doran, and Denis McCrudden. "Covalent Immobilisation of a Nanoporous Platinum Film onto a Gold Screen-Printed Electrode for Highly Stable and Selective Non-Enzymatic Glucose Sensing." Catalysts 11, no. 10 (September 26, 2021): 1161. http://dx.doi.org/10.3390/catal11101161.

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Progress in the development of commercially available non-enzymatic glucose sensors continues to be problematic due to issues regarding selectivity, reproducibility and stability. Overcoming these issues is a research challenge of significant importance. This study reports a novel fabrication process using a double-layer self-assembly of (3 mercaptopropyl)trimethoxysilane (MPTS) on a gold substrate and co-deposition of a platinum–copper alloy. The subsequent electrochemical dealloying of the less noble copper resulted in a nanoporous platinum structure on the uppermost exposed thiol groups. Amperometric responses at 0.4 V vs. Ag/AgCl found the modification to be highly selective towards glucose in the presence of known interferants. The sensor propagated a rapid response time <5 s and exhibited a wide linear range from 1 mM to 18 mM. Additionally, extremely robust stability was attributed to enhanced attachment due to the strong chemisorption between the gold substrate and the exposed thiol of MPTS. Incorporation of metallic nanomaterials using the self-assembly approach was demonstrated to provide a more reproducible and controlled molecular architecture for sensor fabrication. The successful application of the sensor in real blood serum samples displayed a strong correlation with clinically obtained glucose levels.

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17

Fapyane, Deby, Yooseok Lee, Chyi Yan Lim, Jou-Hyeon Ahn, Seon-Won Kim, and In Seop Chang. "Immobilisation of Flavin-Adenine-Dinucleotide-Dependent Glucose Dehydrogenase α Subunit in Free-Standing Graphitised Carbon Nanofiber Paper Using a Bifunctional Cross-Linker for an Enzymatic Biofuel Cell." ChemElectroChem 1, no. 11 (June 4, 2014): 1844–48. http://dx.doi.org/10.1002/celc.201402035.

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18

Hoyle, F. C., and D. V. Murphy. "Seasonal changes in microbial function and diversity associated with stubble retention versus burning." Soil Research 44, no. 4 (2006): 407. http://dx.doi.org/10.1071/sr05183.

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The long-term (16-year) effect of stubble management (i.e. retained or burnt) on the size of the microbial community (microbial biomass-C and -N), microbial community structure (PLFA), and function (CO2-C evolution, gross N transformation rates, enzymatic activity, and community level physiological profiles) was investigated on 4 occasions during a single wheat-growing season using soil collected from the low-rainfall (<250 mm) region of Western Australia. Significant differences (P < 0.001) in microbial community structure and function were determined for different sampling times by phospholipid fatty acid (PLFA) analyses and community level physiological profiles (CLPP). However, neither PLFA nor CLPP analyses identified differences between stubble treatments. In contrast to total soil organic matter-C, for which no treatment differences were evident, microbial biomass-C was 34% and CO2-C evolution 61% greater in stubble-retained treatments than in burnt-stubble treatments in the 0–0.05 m soil layer. Seasonal increases in microbial biomass-C (P < 0.001) were on average twice as large and CO2-C evolution (P < 0.001) nearly 4 times greater in September during crop flowering compared with other sampling times. In contrast, microbial biomass-N remained constant throughout the entire sampling period. Stubble-retained treatments also demonstrated significantly greater (P < 0.05) levels of arginine ammonification, acid phosphatase and β-glucosidase enzyme activity on average compared with burnt-stubble treatments. However, the effect (P = 0.05) of stubble treatment on gross N mineralisation, nitrification, or immobilisation rates was seasonally dependent with burnt-stubble treatments demonstrating lower gross N mineralisation rates than retained-stubble treatments in November. Gross N mineralisation was lower (37–83% on average) than potential gross nitrification rates (estimated in the presence of excess NH4+) measured from May to September. The rate of potential gross nitrification was observed to decline significantly (P = 0.06) in November and as a result, more closely matched gross N mineralisation rates. Potential gross nitrification rates were also up to 6 times greater than microbial immobilisation of NH4+, indicating that this would be the primary consumptive process in the presence of NH4+. Whilst potential nitrification rates in the presence of excess NH4+ were high, low soil NO3– concentrations indicate that plant/microbial demand for NO3– and NH4+ exceeded the supply capacity. For example, actual gross nitrification rates (determined in the presence of 15N-labelled NO3-) were only greater than gross N mineralisation in May, indicating N supply constrained nitrification at other sampling times. Findings illustrate that increased wheat yields of 31% in this study were associated with the retention of stubble. Further they demonstrate that changes in stubble management significantly influenced the mass and activity of microorganisms (and in some cases N cycling), whilst having little influence on community diversity.

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19

Dimcheva, Nina D., and Elena G. Horozova. "Electrochemical enzymatic biosensors based on metal micro-/nanoparticles-modified electrodes: a review." Chemical Papers 69, no. 1 (January 1, 2015). http://dx.doi.org/10.1515/chempap-2015-0011.

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AbstractThe functions of metal structures of micro- or nano-dimensions in the sensing mechanisms of amperometric enzyme-based biosensors are considered in the light of the principles of detection of the latter. The applications of metal mono- or bimetallic nanoparticles-modified materials as catalytic electrodes in the fabrication of first-generation and the role which metal nanoparticles play in promoting or enhancing the electron transfer rates in third-generation electrochemical biosensors are reviewed. Some examples of gold NPs functionalised with enzymes via gold-thiol chemistry as a strategy for enzyme immobilisation and spatial orientation when developing amperometric biosensors are also discussed.

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20

Labus, Karolina, Aleksandra Drozd, and Anna Trusek-Holownia. "Preparation and characterisation of gelatine hydrogels predisposed to use as matrices for effective immobilisation of biocatalysts." Chemical Papers, January 5, 2015. http://dx.doi.org/10.1515/chempap-2015-0235.

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AbstractPhysical, enzymatic and chemical methods were used to develop an efficient procedure for preparing gelatine hydrogels of appropriate strength and elastic properties for applications as enzyme carriers. The concentrations of the crosslinking enzyme (transglutaminase), the initial amount of gelatine, the production time and the effect of additional crosslinking with glutaraldehyde were examined. As a result, the following conditions were selected: 0.1 g cm

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21

Gutierrez-Nunez, Deborah Valeria, and Paul Kilmartin. "Immobilisation of an Enzymatic System on a Pedot-Modified Electrode to Quantify L-Malic Acid." SSRN Electronic Journal, 2022. http://dx.doi.org/10.2139/ssrn.4187464.

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22

Esteves, C., P. Fareleira, M. A. Castelo-Branco, I. G. Lopes, M. Mota, D. Murta, and R. Menino. "Black soldier fly larvae frass increases the soil’s residual nutrient content and enzymatic activity – a lettuce production trial." Journal of Insects as Food and Feed, May 31, 2022, 1–10. http://dx.doi.org/10.3920/jiff2022.0005.

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The aim of this study was to evaluate the potential agronomic value of black soldier fly larvae frass (BSFF) as an organic fertiliser in short-cycle crops, using lettuce as the test plant. Treatments consisted in applying different fertilisers (BSFF and mineral) at different doses and combinations. The experiment was carried out for 42 days and plants were analysed in terms of biomass production, while the soil was chemically characterised before and after fertilisation, in order to assess the residual nutrient concentrations. In addition, soil microbial activity was assessed through the activity of the enzymes dehydrogenase and β-glucosidase. The highest yields were obtained with an exclusive mineral fertilisation (162.5±61.8 g fresh weight) and with a mixture of organic/mineral fertilisation (144.5±16.8 g) in comparison to exclusive fertilisation with BSFF, probably due to the immobilisation and slow mineralisation rate of the N provided by frass, along with the choice of the short-cycle plant, which requires readily available nutrients. Nevertheless, the BSFF increased the soil’s organic matter and residual nutrient content after 42 days of experiment, as well as the enzymatic activity of dehydrogenase and β-glucosidase, by at least 121 and 24% in the soils fertilised with BSFF, respectively. Thus, despite not being effective as an exclusive fertiliser for a short cycle culture, the BSFF included in a mixture with mineral fertilisation, may compete with exclusive mineral fertilisation with the benefit of improving the sustainability of soil fertility and crop production.

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23

Chandola, Jyoti, Vandana Semwal, Narotam Sharma, and Pooja Singh. "Isolation, Biochemical Characterization and Production of Immobilised β-Amylase Chitosan Beads Using Bacteria from Waste Water Effluents for its Industrial Production Aspect." Microbiology Research Journal International, December 31, 2020, 111–16. http://dx.doi.org/10.9734/mrji/2020/v30i930270.

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Aims: An amylase, the enzyme that catalyses the hydrolysis of starch into sugars are produced in both animals and plants and as well as in some bacteria also. Nowadays, the use of amylase enzyme in different industrial sectors and particularly in controlling the industrial water pollution has been increased as this enzyme is effective against different types of industrial effluents such as wastes from dairies, confectionaries, municipal wastes, bakery and so on which are expelled out in water without giving any proper treatment. As, the production of synthetic amylase enzyme for this purpose is quite costly, in this study, the waste water effluent was used to isolate the amylase producing bacteria, hence, decreasing the cost. Methodology: The samples were taken from drains coming from bakery, municipal waste, etc, and five bacterias were isolated at dilution 10-6 which were named accordingly as Tan1, Tan2, Tan3, Tan4 and Tan5 further followed by Gram staining and biochemical characterization tests for further confirmation of amylase producing bacteria followed by the immobilisation of the β-amylase enzyme produced by the bacteria. Results and Conclusion: Two bacterias were identified as amylase producing, Tan1 and Tan2, in which Gram positive bacteria showed higher amylase production at 30°C(Tan1). Compared to the free β-amylase, the immobilised β-amylase enzyme showed broader pH and temperature ranges, enhanced thermal stability, better storage stability, reusability and higher accessibility of the substrate to the immobilised β-amylase. Improved activity recovery and enzymatic properties of immobilised β-amylase chitosan beads in present study holds a promising future in industrial applications.

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24

Chandola, Jyoti, Vandana Semwal, Narotam Sharma, and Pooja Singh. "Isolation, Biochemical Characterization and Production of Immobilised β-Amylase Chitosan Beads Using Bacteria from Waste Water Effluents for its Industrial Production Aspect." Microbiology Research Journal International, December 31, 2020, 111–16. http://dx.doi.org/10.9734/mrji/2020/v30i930270.

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Aims: An amylase, the enzyme that catalyses the hydrolysis of starch into sugars are produced in both animals and plants and as well as in some bacteria also. Nowadays, the use of amylase enzyme in different industrial sectors and particularly in controlling the industrial water pollution has been increased as this enzyme is effective against different types of industrial effluents such as wastes from dairies, confectionaries, municipal wastes, bakery and so on which are expelled out in water without giving any proper treatment. As, the production of synthetic amylase enzyme for this purpose is quite costly, in this study, the waste water effluent was used to isolate the amylase producing bacteria, hence, decreasing the cost. Methodology: The samples were taken from drains coming from bakery, municipal waste, etc, and five bacterias were isolated at dilution 10-6 which were named accordingly as Tan1, Tan2, Tan3, Tan4 and Tan5 further followed by Gram staining and biochemical characterization tests for further confirmation of amylase producing bacteria followed by the immobilisation of the β-amylase enzyme produced by the bacteria. Results and Conclusion: Two bacterias were identified as amylase producing, Tan1 and Tan2, in which Gram positive bacteria showed higher amylase production at 30°C(Tan1). Compared to the free β-amylase, the immobilised β-amylase enzyme showed broader pH and temperature ranges, enhanced thermal stability, better storage stability, reusability and higher accessibility of the substrate to the immobilised β-amylase. Improved activity recovery and enzymatic properties of immobilised β-amylase chitosan beads in present study holds a promising future in industrial applications.

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25

Xu, Lili, Yimin Qin, Yufeng Song, Aixing Tang, and Youyan Liu. "Glutaraldehyde-crosslinked Rhizopus oryzae whole cells show improved catalytic performance in alkene epoxidation." Microbial Cell Factories 22, no. 1 (February 22, 2023). http://dx.doi.org/10.1186/s12934-023-02026-0.

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Abstract Background Existing methods for alkene epoxidation are based on lipase-catalysed perhydrolysis. However, the inactivation of the expensive lipase enzyme is problematic for enzymatic epoxidation at large scales due to the use of hydrogen peroxide and peracids at high concentrations in the reaction. The immobilisation of whole cells appears to be a promising approach to alleviate this problem. Results A green oxidation system containing hydrogen peroxide, Na3C6H5O7, an acyl donor, and glutaraldehyde (GA)-crosslinked cells of Rhizopus oryzae was developed for the epoxidation of alkenes. GA-crosslinked cells of Rhizopus oryzae were adopted as a biocatalyst into the epoxidation system. A variety of alkenes were oxidised with this system, with a 56–95% analytical yield of the corresponding epoxides. The catalytic performance of the crosslinked treated cells was substantially improved compared to that of the untreated cells and the initial reaction rate increased from 126.71 to 234.72 mmol/L/h, retaining 83% yields even after four batches of reactions. The addition of 3.5 mmol Na3C6H5O7 not only acts as an acid-trapping reagent to eliminate the negative effect of the carboxylic acid on the alkene oxide but also forms a saturated salt solution with the aqueous phase, affecting the concentration of H2O2 in the three phases and thus the epoxidation reaction. Organic solvents with a logP value > 0.68 were good at producing hydroxy peracids; however, this method is only suitable for oxidation in a two-liquid phase. Conclusions Compared with other lipase biocatalysts, the GA-crosslinked whole-cell biocatalyst is inexpensive, readily available, and highly stable. Therefore, it can be considered promising for industrial applications.

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