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A biocatalyst is an enzyme that speeds up or slows down the rate at which a chemical reaction occurs and speeds up certain processes by 108 times. It is used as an anticancer agent because it targets drug activation inside the tumor microenvironment while limiting damage to healthy cells. Biocatalysts have been used for the synthesis of different heterocyclic compounds and is also used in the nano drug delivery systems. The use of nano-biocatalysts for tumor-targeted delivery not only aids in tumor invasion, angiogenesis, and mutagenesis, but also provides information on the expression and activity of many markers related to the microenvironment. Iosmapinol, moclobemide, cinepazide, lysine dioxygenase, epothilone, 1-homophenylalanine, and many more are only some of the anticancer medicines that have been synthesised using biocatalysts. In this review, we have highlighted the application of biocatalysts in cancer therapies as well as the use of biocatalysts in the synthesis of drugs and drug-delivery systems in the tumor microenvironment. [ABSTRACT FROM AUTHOR]

High-performance carbon dioxide (CO2)-capture technologies with low environmental impact are necessary to combat the current climate change crisis. Durable and versatile "drop-in-ready" textile structured packings with covalently immobilized carbonic anhydrase (CA) were created as efficient, easy to handle catalysts for CO2 absorption in benign solvents. The hydrophilic textile structure itself contributed high surface area and superior liquid transport properties to promote gas-liquid reactions that were further enhanced by the presence of CA, leading to excellent CO2 absorption efficiencies in lab-scale tests. Mechanistic investigations revealed that CO2 capture efficiency depended primarily on immobilized enzymes at or near the surface, whereas polymer entrapped enzymes were more protected from external stressors than those exposed at the surface, providing strategies to optimize performance and durability. Textile packing with covalently attached enzyme aggregates retained 100% of the initial 66.7% CO2 capture efficiency over 71-day longevity testing and retained 85% of the initial capture efficiency after 1-year of ambient dry storage. Subsequent stable performance in a 500 h continuous liquid flow scrubber test emphasized the material robustness. Biocatalytic textile packings performed well with different desirable solvents and across wide CO2 concentration ranges that are critical for CO2 capture from coal and natural gas-fired power plants, from natural gas and biogas for fuel upgrading, and directly from air. [ABSTRACT FROM AUTHOR]

The increasing global demand for petroleum oils has led to a significant increase in their cost and has led to the search for renewable alternative waste resources for biodiesel synthesis and production using novel environmentally sound and acceptable methods. In the current study, Kocuria flava lipase was immobilized on Fe3O4/cellulose nanocomposite; and used as a biocatalyst for the conversion of cooking oil wastes into biodiesel through the transesterification/esterification process. The characterization of Fe3O4/cellulose nanocomposite revealed several functional groups including carboxyl (C=O) and epoxy (C-O-C) groups that act as multipoint covalent binding sites between the lipase and the Fe3O4/cellulose nanocomposite and consequently increasing lipase immobility and stability. The immobilized lipase showed a high thermo-stability as it retained about 70% of its activity at 80 °C after 30 min. The kinetics of immobilized lipase revealed that the Km and Vmax values were 0.02 mM and 32.47 U/mg protein, respectively. Moreover, the immobilized lipase showed high stability and reusability for transesterification/esterification reactions for up to four cycles with a slight decline in the enzyme activity. Furthermore, the produced biodiesel characteristics were compatible with the standards, indicating that the biodiesel obtained is doable and may be utilized in our daily life as a diesel fuel. [ABSTRACT FROM AUTHOR]

Industries such as mining, cokemaking, (petro)chemical and electroplating produce effluents that contain free cyanide (fCN = HCN + CN−). Currently, fCN is mainly removed by (physico)chemical methods or by biotreatment with activated sludge. Cyanide hydratases (CynHs) (EC 4.2.1.66), which convert fCN to the much less toxic formamide, have been considered for a mild approach to wastewater decyanation. However, few data are available to evaluate the application potential of CynHs. In this study, we used a new CynH from Exidia glandulosa (protein KZV92691.1 designated NitEg by us), which was overproduced in Escherichia coli. The purified NitEg was highly active for fCN with 784 U/mg protein, kcat 927/s and kcat/KM 42/s/mM. It exhibited optimal activities at pH approximately 6–9 and 40–45 °C. It was quite stable in this pH range, and retained approximately 40% activity at 37 °C after 1 day. Silver and copper ions (1 mM) decreased its activity by 30–40%. The removal of 98–100% fCN was achieved for 0.6–100 mM fCN. Moreover, thiocyanate, sulfide, ammonia or phenol added in amounts typical of industrial effluents did not significantly reduce the fCN conversion, while electroplating effluents may need to be diluted due to high fCN and metal content. The ease of preparation of NitEg, its high specific activity, robustness and long shelf life make it a promising biocatalyst for the detoxification of fCN. [ABSTRACT FROM AUTHOR]

Eversa® Transform 2.0 lipase (ET2) is a recent lipase formulation derived from the Thermomyces lanuginosus lipase cultivated on Aspergillus oryzae and specially designed for biodiesel production. Since it has not been available for a long time, research on the efficiency of this enzyme in other applications remains unexplored. Moreover, even though it has been launched as a free enzyme, its immobilization may extend the scope of ET2 applications. This work explored ET2 immobilization on octadecyl methacrylate beads (IB-ADS-3) and proved the efficiency of the derivatives for esterification of glycerophosphocholine (GPC) with oleic acid in anhydrous systems. ET2 immobilized via interfacial activation on commercial hydrophobic support Immobead IB-ADS-3 showed maximum enzyme loading of 160 mg/g (enzyme/support) and great stability for GPC esterification under 30% butanone and solvent-free systems. For reusability, yields above 63% were achieved after six reaction cycles for GPC esterification. Considering the very high enzyme loading and the number of reuses achieved, these results suggest a potential application of this immobilized biocatalyst for esterification reactions in anhydrous media. This study is expected to encourage the exploration of other approaches for this enzyme, thereby opening up several new possibilities. [ABSTRACT FROM AUTHOR]

The market for industrial enzymes has witnessed constant growth, which is currently around 7% a year, projected to reach $10.5 billion in 2024. Lipases are hydrolase enzymes naturally responsible for triglyceride hydrolysis. They are the most expansively used industrial biocatalysts, with wide application in a broad range of industries. However, these biocatalytic processes are usually limited by the low stability of the enzyme, the half-life time, and the processes required to solve these problems are complex and lack application feasibility at the industrial scale. Emerging technologies create new materials for enzyme carriers and sophisticate the well-known immobilization principles to produce more robust, eco-friendlier, and cheaper biocatalysts. Therefore, this review discusses the trending studies and industrial applications of the materials and protocols for lipase immobilization, analyzing their advantages and disadvantages. Finally, it summarizes the current challenges and potential alternatives for lipases at the industrial level. [ABSTRACT FROM AUTHOR]

Glycolipids have become an ecofriendly alternative to chemically obtained surfactants, mainly for the cosmetic, pharmaceutical, and food industries. However, the sustainable production of these compounds is still challenging, because: (i) water is a recognized inhibitor, (ii) multiphases make the use of cosolvent reaction medium necessary, and (iii) there are difficulties in finding a source for both starting materials. This study used sugars and lipids from peach palm fruit shells or model compounds as substrates to synthesize glycolipids on five different renewable deep eutectic solvents (Re-DES) alone or with a cosolvent system. Substrate conversions up to 24.84% (so far, the highest reported for this reaction on DES), showing (1) the non-precipitation of glucose in the solvent, (2) emulsification and (3) low viscosity (e.g., more favorable mass transfer) as the main limiting factors for these heterogeneous enzymatic processes. The resulting conversion was reached using a cosolvent system Re-DES:DMSO:t-butanol that was robust enough to allow conversions in the range 19–25%, using either model compounds or sugar and fatty acid extracts, with free or immobilized enzymes. Finally, the characterization of the in-house synthesized glycolipids by surface tension demonstrated their potential as biosurfactants, for instance, as an alternative to alcohol ethoxylates, industrially produced using less sustainable methods. [ABSTRACT FROM AUTHOR]

The enantioselective synthesis of organic compounds is one of the great challenges in organic synthetic chemistry due to its importance for the acquisition of biologically active derivatives, e.g., pharmaceuticals, agrochemicals, and others. This is why biological systems are increasingly applied as tools for chiral compounds synthesis or modification. The use of whole cells of "wild-type" microorganisms is one possible approach, especially as some methods allow improving the conversion degrees and controlling the stereoselectivity of the reaction without the need to introduce changes at the genetic level. Simple manipulation of the culture conditions, the form of a biocatalyst, or the appropriate composition of the biotransformation medium makes it possible to obtain optically pure products in a cheap, safe, and environmentally friendly manner. This review contains selected examples of the influence of physicochemical factors on the stereochemistry of the biocatalytic preparation of enantiomerically pure compounds, which is undertaken through kinetically controlled separation of their racemic mixtures or reduction of prochiral ketones and has an effect on the final enantiomeric purity and enantioselectivity of the reaction. [ABSTRACT FROM AUTHOR]

Oleanolic acid (OA) is a pentacyclic triterpenoid widely found in plants and foods as an aglycone of triterpenoid saponins or as a free acid. OA exhibits beneficial activities for humans, including antitumor, antivirus, and hepatoprotection properties without apparent toxicity. The metabolites produced by the cytochrome P450 (P450) enzymes are critical for the evaluation of the efficacy and safety of drugs. In this study, the potential metabolites of OA were investigated by P450-catalyzed oxidation reactions. Among the various tested human P450s, only human CYP3A4 was active for the hydroxylation of OA. The major metabolite was characterized by a set of analyses using HPLC, LC–MS, and NMR. It was found to be 4-epi-hederagenenin, a chiral product, by regioselective hydroxylation of the methyl group at the C-23 position. These results indicated that CYP3A4 can hydroxylate an OA substrate to make 4-epi-hederagenenin. Possible drug–food interactions are discussed. [ABSTRACT FROM AUTHOR]

The role of oxygen in anodic biofilms is still a matter of debate. In this study, we tried to elucidate the structure and performance of an electrogenic biofilm that develops on air-exposed, carbon felt electrodes, commonly used in bioelectrochemical systems. By simultaneously recording the current density produced by the bioanode and dissolved oxygen concentration, both inside and in the vicinity of the biofilm, it was possible to demonstrate the influence of a protective aerobic layer present in the biofilm (mainly formed by Pseudomonas genus bacteria) that prevents electrogenic bacteria (such as Geobacter sp.) from hazardous exposure to oxygen during its normal operation. Once this protective barrier was deactivated for a long period of time, the catalytic capacity of the biofilm was severely affected. In addition, our results highlighted the importance of the material's porous structure for oxygen penetration in the electrode. [ABSTRACT FROM AUTHOR]

Rhododendrol (RD) is a naturally occurring phenolic compound found in many plants. Tyrosinase (Ty) converts RD to RD-catechol and subsequently RD-quinone via two-step oxidation reactions, after which RD-melanin forms spontaneously from RD-quinone. RD is cytotoxic in melanocytes and lung cancer cells, but not in keratinocytes and fibroblasts. However, the function of RD metabolites has not been possible to investigate due to the lack of available high purity metabolites. In this study, an enzymatic strategy for RD-catechol production was devised using engineered cytochrome P450 102A1 (CYP102A1) and Ty, and the product was analyzed using high-performance liquid chromatography (HPLC), LC-MS, and NMR spectroscopy. Engineered CYP102A1 regioselectively produced RD-catechol via hydroxylation at the ortho position of RD. Although RD-quinone was subsequently formed by two step oxidation in Ty catalyzed reactions, L-ascorbic acid (LAA) inhibited RD-quinone formation and contributed to regioselective production of RD-catechol. When LAA was present, the productivity of RD-catechol by Ty was 5.3-fold higher than that by engineered CYP102A1. These results indicate that engineered CYP102A1 and Ty can be used as effective biocatalysts to produce hydroxylated products, and Ty is a more cost-effective biocatalyst for industrial applications than engineered CYP102A1. [ABSTRACT FROM AUTHOR]

Biotechnological applications of cytochromes P450 show difficulties, such as low activity, thermal and/or solvent instability, narrow substrate specificity and redox partner dependence. In an attempt to overcome these limitations, an exploitation of novel thermophilic P450 enzymes from nature via uncultured approaches is desirable due to their great advantages that can resolve nearly all mentioned impediments. From the metagenomics library of the Binh Chau hot spring, an open reading frame (ORF) encoding a thermostable cytochrome P450—designated as P450-T3—which shared 66.6% amino acid sequence identity with CYP109C2 of Sorangium cellulosum So ce56 was selected for further identification and characterization. The ORF was synthesized artificially and heterologously expressed in Escherichia coli C43(DE3) using the pET17b system. The purified enzyme had a molecular weight of approximately 43 kDa. The melting temperature of the purified enzyme was 76.2 °C and its apparent half-life at 60 °C was 38.7 min. Redox partner screening revealed that P450-T3 was reduced well by the mammalian AdR-Adx4-108 and the yeast Arh1-Etp1 redox partners. Lauric acid, palmitic acid, embelin, retinoic acid (all-trans) and retinoic acid (13-cis) demonstrated binding to P450-T3. Interestingly, P450-T3 also bound and converted testosterone. Overall, P450-T3 might become a good candidate for biocatalytic applications on a larger scale. [ABSTRACT FROM AUTHOR]

Nowadays, biocatalysts have received much more attention in chemistry regarding their potential to enable high efficiency, high yield, and eco-friendly processes for a myriad of applications. Nature's vast repository of catalysts has inspired synthetic chemists. Furthermore, the revolutionary technologies in bioengineering have provided the fast discovery and evolution of enzymes that empower chemical synthesis. This article attempts to deliver a comprehensive overview of the last two decades of investigation into enzymatic reactions and highlights the effective performance progress of bio-enzymes exploited in organic synthesis. Based on the types of enzymatic reactions and enzyme commission (E.C.) numbers, the enzymes discussed in the article are classified into oxidoreductases, transferases, hydrolases, and lyases. These applications should provide us with some insight into enzyme design strategies and molecular mechanisms. [ABSTRACT FROM AUTHOR]

Genipin is a reagent isolated from the Gardenia jasminoides fruit extract, and whose low toxicity and good crosslinking properties have converted it into a reactive whose popularity is increasing by the day. These properties have made it widely used in many medical applications, mainly in the production of chitosan materials (crosslinked by this reactive), biological scaffolds for tissue engineering, and nanoparticles of chitosan and nanogels of proteins for controlled drug delivery, the genipin crosslinking being a key point to strengthen the stability of these materials. This review is focused on the mechanism of reaction of this reagent and its use in the design of biocatalysts, where genipin plays a double role, as a support activating agent and as inter- or intramolecular crosslinker. Its low toxicity makes this compound an ideal alterative to glutaraldehyde in these processes. Moreover, in some cases the features of the biocatalysts prepared using genipin surpassed those of the biocatalysts prepared using other standard crosslinkers, even disregarding toxicity. In this way, genipin is a very promising reagent in the design of biocatalysts. [ABSTRACT FROM AUTHOR]

In our previous study, Rhodotorula mucilaginosa (R. mucilaginosa) was selected via high throughput screening as a very active and selective whole-cell biocatalyst for the asymmetric reduction of ketones. In this study, the reduction of ketones to the desired chiral alcohols by immobilized cells of this strain was investigated. Characterization with Fourier-transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM) showed that whole R. mucilaginosa cells were successfully immobilized on support matrices composed of agar, calcium alginate, PVA-alginate and chitosan. The immobilized cells were applied to the enantioselective reduction of fourteen different aromatic ketones. Good to excellent results were achieved with R. mucilaginosa cells immobilized on agar and calcium alginate. The immobilized cells on the selected support matrix composed of agar exhibited a significant increase in pH tolerance at pH 3.5–9 and demonstrated highly improved thermal stability compared to free cells. The cells immobilized on agar retained 90% activity after 60 days storage at 4 °C and retained almost 100% activity after 6 reuse cycles. In addition, the immobilization procedures are very simple and cause minimal pollution. These results suggest that the application of immobilized R. mucilaginosa can be practical on an industrial scale to produce chiral alcohols. [ABSTRACT FROM AUTHOR]