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Journal ArticleDOI: 10.1016/J.IJBIOMAC.2021.02.146

Covalent immobilization of lipase from Candida rugosa on epoxy-activated cloisite 30B as a new heterofunctional carrier and its application in the synthesis of banana flavor and production of biodiesel

02 Mar 2021-International Journal of Biological Macromolecules (Elsevier)-Vol. 178, pp 569-579
Abstract: In this paper, an epoxy-activated cloisite (ECL) was prepared as a new heterofunctional carrier via a reaction between cloisite 30B (CL) and epichlorohydrin and utilized for covalent immobilization of lipase from Candida rugosa. The lipase immobilized on the ECL (LECL) was successfully used in the olive oil hydrolysis, synthesis of isoamyl acetate (banana flavor), and biodiesel production. The TGA, FT-IR, SEM, and XRD were used to characterize CL, ECL, and LECL. The influences of temperature, pH, thermal stability, and storage capacity were examined in the olive oil hydrolysis. The effects of solvent, temperature, time, water content, and substrates molar ratio on the yields of ester and biodiesel were also investigated. In the optimized conditions, the hydrolytic activity of LECL was 1.85 ± 0.05 U/ mg, and the maximum yield of ester and biodiesel was 91.6% and 95.4%, respectively. The LECL showed good thermal stability and storage capacity compared to the free lipase. Additionally, LECL was reusable for both esterification and transesterification after being used for nine cycles.

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Topics: Lipase (55%), Biodiesel production (55%), Isoamyl acetate (54%) ... read more
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13 results found


Journal ArticleDOI: 10.1016/J.MOLLIQ.2021.116543
Abstract: The work focused on estimating the band gap energy (Eg) for various electronic transitions in the CdS/g-C3N4 coupled sample and the potential positions of the valence and conduction bands Based on the data obtained and the effects of the scavenging agents, suitable energy diagrams were constructed for illustrating the photodegradation mechanism pathway The coupled catalyst showed a red shift in Eg-value concerning the g-C3N4 alone (Eg (eV): CdS: 188, g-C3N4: 283, CdS/g-C3N4: 217) The pHpzc values of 51, 62, and 54 were estimated for CdS, g-C3N4, and CdS/g-C3N4, respectively The highest methyl orange MO degradation was achieved at acidic pH 3–5 In this pH range, the zwitterion MO species is the predominant MO species in media which the catalyst can adsorb via hydrogen bonding by the MO sulfonic group The photogenerated e- ≈ photogenerated h+ > superoxide radicals > hydroxyl radicals trend was obtained for the importance of the reactive species in MO photodegradation In the proposed system, MO degradation can begin by both reduction and oxidation processes, and both are more efficient when the direct Z-scheme mechanism is considered >85% of MO molecules can be degraded at conditions of catalyst dose: 05 g/L, pH: 3, CMO: 2 ppm, and irradiation time: 90 min No considerable hydroxyl radicals can be produced by the system based on the potential positions of the species (E (eV): CdS-VB: 193, g-C3N4-VB: 163, OH /OH–: 19) The direct Z-scheme pathway can prove the H2-production and O2-evolution by the proposed system

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Topics: Methyl orange (54%), Photodegradation (54%), Catalysis (50%)

11 Citations


Journal ArticleDOI: 10.1016/J.CHEMPHYS.2021.111305
01 Oct 2021-Chemical Physics
Abstract: The coupled FeO onto the clinoptilolite nanoparticles (CNP) was prepared and characterized briefly by XRD, FTIR, and DRS techniques. The average crystallite size of the CNP and FeO-CNP samples was estimated at 56 and 59 nm by the Scherrer equation, respectively. The pHpzc of the catalyst was also determined at 3.7. The supported catalyst showed a boosted photocatalytic effect in the photodegradation of 2,4-dichloroaniline (DCA) in an aqueous solution concerning the bulk FeO. The kinetics of the photodegradation process obeyed the Hinshelwood model, and thus, the rate of the process was followed by the change in the experimental variables. When the loaded FeO reached 13%, the highest degradation rate was obtained. The highest photodegradation rate was received at the optimal conditions of the catalyst dose: 0.5 g/L, CDCA: 15 ppm, and the initial pH: 5. HPLC chromatograms showed appearance new peaks for the photodegraded DCA solutions. The decrease in the main peak at the retention time of 2.87 min confirmed that 69 and 82% DCA molecules degraded after 180 and 300 min. The stability of FeO-CNP catalyst was studied, and the results showed good photocatalytic activity retained at drying temperatures of 25, 150, and 270 °C after three reusing runs, especially at higher drying temperatures.

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Topics: Photodegradation (52%), Photocatalysis (51%)

1 Citations


Journal ArticleDOI: 10.1016/J.IJBIOMAC.2021.07.101
Abstract: The development of new biocatalytic systems to replace the chemical catalysts, with suitable characteristics in terms of efficiency, stability under high temperature reactions and in the presence of organic solvents, reusability, and eco-friendliness is considered a very important step to move towards the green processes. From this basis, the use of lipase as a catalyst is highly desired for many industrial applications because it offers the reactions in which could be used, stability in harsh conditions, reusability and a greener process. Therefore, the introduction of temperature-resistant and solvent-tolerant lipases have become essential and ideal for industrial applications. Temperature-resistant and solvent-tolerant lipases have been involved in many large-scale applications including biodiesel, detergent, food, pharmaceutical, organic synthesis, biosensing, pulp and paper, textile, animal feed, cosmetics, and leather industry. So, the present review provides a comprehensive overview of the industrial use of lipase. Moreover, special interest in biotechnological and biochemical techniques for enhancing temperature-resistance and solvent-tolerance of lipases to be suitable for the industrial uses.

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1 Citations


Journal ArticleDOI: 10.1016/J.FOODCHEM.2021.131425
30 Mar 2022-Food Chemistry
Abstract: In this paper, α-amylase from Bacillus subtilis was successfully immobilized on three supports. First, α-amylase was immobilized on cloisite 30B via the adsorption method. Then cloisite 30B was activated with tosyl chloride and epichlorohydrin. These activated supports were used for covalent immobilization of α-amylase, and their enzymatic activities were effectively tested in the starch hydrolysis. The results demonstrated that the specific activity of α-amylase immobilized on cloisite 30B was 2.39 ± 0.03, for α-amylase immobilized on activated cloisite 30B with epichlorohydrin was 1.96 ± 0.05 and for α-amylase immobilized on activated cloisite 30B with tosyl chloride was 2.17 ± 0.05 U mg−1. The optimum pH for the activity of free α-amylase was 7, but for α-amylase immobilized on cloisite 30B was 8, and for α-amylase immobilized on activated supports was 7.5. The immobilized enzymes had better thermal resistance and storage stability than free α-amylase, and they also showed excellent reusability.

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Topics: Immobilized enzyme (57%), Epichlorohydrin (51%)

1 Citations


Open accessJournal ArticleDOI: 10.1016/J.MSSP.2021.106310
Abstract: Metal-organic frameworks (MOFs) are crystalline microporous materials that show catalytic activity when used as hosts. Nanostructured materials supported by MOFs show increased catalytic activity and stability. Several steps or templates are vital in the synthesis of MOF composites. However, developing effective and simple MOF synthesis approaches remains challenging. In this study, a simple one-step reaction is described for preparing Nanosized Stannic (II) oxide particles in MOF composites, called nanosized SnO2/MOF-199 (HKUST-1). The SnO2/MOF-199 (30 wt%) exhibited the best degradation efficiency of metronidazole (MZ), SnO2/MOF-199 (5 wt%), SnO2/MOF-199 (10 wt%), SnO2/MOF-199 (20 wt%), and SnO2/MOF-199 (40 wt%). The photocatalyst used in this work is a novel nanocomposite-based compound. The nanocomposite was characterized using SEM, EDX, TEM, XRD, FT-IR, BET, and TG-DTG techniques. Also, PL and DRS analyses were used for the optical-property study of the photocatalyst. Afterward, the synthesized nanocomposite was used for metronidazole (MZ) degradation. The result showed that pH of the solution, irradiation time, time-CMZ interactions, and time-pH interactions remain highly significant in MZ degradation. The most suitable degradation extent was acquired at pH = 3, catalyst dosage = 2 g/L, MZ = 40 mg/L, and irradiation time of 240 min. Between type II-heterojunction and Z-scheme mechanisms, the second case showed the most significant role in MZ photodegradation.

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Topics: Nanocomposite (54%)

References
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89 results found


Open accessJournal ArticleDOI: 10.1016/J.BIOTECHADV.2015.03.006
Abstract: This work has been supported by grant CTQ2013-41507-R from Spanish MINECO, grant no.1102-489-25428 from COLCIENCIAS and Universidad Industrial de Santander (VIE-UIS Research Program) (Colombia) and CNPq grant 403505/2013-5 (Brazil). A. Berenguer-Murcia thanks the Spanish MINECO for a Ramon y Cajal fellowship (RyC-2009-03813).

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446 Citations


Open accessJournal ArticleDOI: 10.1021/BM400762H
16 Jul 2013-Biomacromolecules
Abstract: This work has been supported by Grant CTQ2009-07568 from Spanish Ministerio de Ciencia e Innovacion, Grant No.1102-489-25428 from COLCIENCIAS and Universidad Industrial de Santander (VIE-UIS Research Program) and CNPq and FAPERGS (Brazil). A.B.-M. thanks the Spanish Ministerio de Ciencia e Innovacion for a Ramon y Cajal fellowship (RyC-2009-03813).

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358 Citations


Journal ArticleDOI: 10.1016/0141-0229(86)90003-7
Volker Kasche1Institutions (1)
Abstract: Hydrolases can be used to catalyse the synthesis of condensation products such as β-lactam antibiotics, peptides, oligosaccharides and glycerides. In biotechnological processes, synthesis to achieve maximum yields may be carried out either as an equilibrium controlled or kinetically controlled reaction. Only in the later case is the yield of condensation product influenced by the properties of the enzyme that act as a transferase in this reaction. With the same amount of enzyme the maximum yield is also obtained much more rapidly than in the equilibrium controlled process. Hydrolases with high ratios of transferase to hydrolase activity are favourable for use. Recent results on the mechanisms of enzyme catalysed condensations allow a rational analysis of how yield controlling factors (pH, temperature, ionic strength, enzyme and substrate properties) may be changed to obtain optimum yields. This can be used to evaluate whether these biotechnological processes can compete with the chemical methods currently used for the synthesis of these products. It can also be used to plan rational protein engineering of the enzymes that in kinetically controlled synthesis of the condensation products may give yields that can compete favourably with the existing chemical processes to produce these compounds.

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Topics: Condensation reaction (53%), Yield (chemistry) (52%), Substrate (chemistry) (52%) ... read more

306 Citations


Journal ArticleDOI: 10.1016/S0168-1656(00)00432-6
Abstract: The effects of important reaction parameters for enhancing isoamyl acetate formation through lipase-catalyzed esterification of isoamyl alcohol were investigated in this study Increase in substrate (acid) concentration led to decrease in conversions A critical enzyme concentration of 3 g l(-1) was detected for a substrate concentration of 006 M (each of alcohol and acid) Solvents with partition coefficient higher than 1000 (log P>30) supported enzyme activity to give high conversions Acetic acid at higher concentrations could not be esterified easily probably owing to its role in lowering the microaqueous pH of the enzyme Extraneous water/buffer addition decreased the isoamyl acetate yields slightly ( approximately 10%) at 0005-001% v/v of the reaction mixture and drastically (>40%) at above 001% v/v Buffer saturation of the organic solvent employed improved esterification (upto two-fold), particularly at moderately higher substrate concentrations (>018 M) Employing acetic anhydride instead of acetic acid resulted in a two-fold increase in the yields (at 025 M substrate) Use of excess nucleophile (alcohol) concentration by increasing the alcohol/acid molar ratio resulted in higher conversions in shorter duration (upto eight-fold even at 15 M acetic acid) Yields above 80% were achieved with substrate concentrations as high as 15 M and more than 150 g l(-1) isoamyl acetate concentrations were obtained employing a relatively low enzyme concentration of 10 g l(-1) The operational stability of lipase was also observed to be reasonably high enabling ten reuses of the biocatalyst

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Topics: Isoamyl acetate (71%), Isoamyl alcohol (60%), Acetic acid (59%) ... read more

228 Citations


Open accessJournal ArticleDOI: 10.1016/J.MCAT.2019.110607
Abstract: The use of immobilized enzymes is now a routine process for the manufacture of many industrial products in the pharmaceutical, chemical and food industry. Some enzymes, such as lipases, are naturally robust and efficient, can be used for the production of many different molecules and have a wide range of industrial applications thanks to their broad selectivity. As an example, lipase from Candida antarctica (CalB) has been used by BASF to produce chiral compounds, such as the herbicide Dimethenamide-P, which was previously made chemically. The use of the immobilized enzyme has provided significant advantages over a chemical process, such as the possibility to use equimolar concentration of substrates, obtain an enantiomeric excess > 99%, use relatively low temperatures ( 1 ]. Some more specific enzymes, like transaminases, have required protein engineering to become suitable for applications in production of APIs (Active Pharmaceutical Ingredients) in conditions which are extreme for a wild type enzyme. The process developed by Merck for sitagliptin manufacture is a good example of challenging enzyme engineering applied to API manufacture. The previous process of sitagliptin involved hydrogenation of enamine at high pressure using a rhodium-based chiral catalyst. By developing an engineered transaminase, the enzymatic process was able to convert 200 g/l of prositagliptin in the final product, with e.e. >99.5% and using an immobilized enzyme in the presence of DMSO as a cosolvent [ 2 ]. For all enzymes, the possibility to be immobilized and used in a heterogeneous form brings important industrial and environmental advantages, such as simplified downstream processing or continuous process operations. Here, we present a series of large-scale applications of immobilized enzymes with benefits for the food, chemical, pharmaceutical, cosmetics and medical device industries, some of which have been scarcely reported on previously. In general, all enzymatic reactions can benefit from the immobilization, however, the final choice to use them in immobilized form depends on the economic evaluation of costs associated with their use versus benefits obtained in the process. It can be concluded that the benefits are rather significant, since the use of immobilized enzymes in industry is increasing.

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196 Citations