Hydrolysis Of Ester Bond Research Articles

Selective deuteration for molecular insights into the digestion of medium chain triglycerides

Medium chain triglycerides (MCTs) are a unique form of dietary fat that have a wide range of health benefits. They are molecules with a glycerol backbone esterified with medium chain (6–12 carbon atoms) fatty acids on the two outer (sn-1 and sn-3) and the middle (sn-2) positions. During lipid digestion in the gastrointestinal tract, pancreatic lipase stereoselectively hydrolyses the ester bonds of these triglycerides on the sn-1 and sn-3 positions resulting in sn-2 monoglyceride and fatty acids as major products. However, the sn-2 monoglycerides are thermodynamically less stable than their sn-1/3 counterparts. Isomerization or fatty acid migration from the sn-2 monoglyceride to sn-1/3 monoglyceride may occur spontaneously and would lead to glycerol and fatty acid as final products. Here, tricaprin (C10) with selectively deuterated fatty acid chains was used for the first time to monitor chain migration and the stereoselectivity of the pancreatic lipase-catalyzed hydrolysis of ester bonds. The intermediate and final digestion products were studied using NMR and mass spectrometry under biologically relevant conditions. The hydrolysis of the sn-2 monocaprin to glycerol and capric acid did not occur within biologically relevant timescales and fatty acid migration occurs only in limited amounts as a result of the presence of undigested diglyceride species over long periods of time in the digestion medium. The slow kinetics for the exchange of the sn-2 fatty acid chain and the stereoselectivity of pancreatic lipase on MCTs is relevant for industrial processes that involve enzymatic interesterification and the production of high-value products such as specific structured triacylglycerols, confectionery fats and nutritional products.

Monitoring the Long-Term Degradation Behavior of Biomimetic Bioadhesive Using Wireless Magnetoelastic Sensor.

The degradation behavior of a tissue adhesive is critical to its ability to repair a wound while minimizing prolonged inflammatory response. Traditional degradation tests can be expensive to perform, as they require large numbers of samples. The potential for using magnetoelastic resonant sensors to track bioadhesive degradation behavior was investigated. Specifically, biomimetic poly (ethylene glycol)- (PEG-) based adhesive was coated onto magnetoelastic (ME) sensor strips. Adhesive-coated samples were submerged in solutions buffered at multiple pH levels (5.7, 7.4 and 10.0) at body temperature (37 °C) and the degradation behavior of the adhesive was tracked wirelessly by monitoring the changes in the resonant amplitude of the sensors for over 80 days. Adhesive incubated at pH 7.4 degraded over 75 days, which matched previously published data for bulk degradation behavior of the adhesive while utilizing significantly less material (∼10(3) times lower). Adhesive incubated at pH 10.0 degraded within 25 days while samples incubated at pH 5.7 did not completely degrade even after 80 days of incubation. As expected, the rate of degradation increased with increasing pH as the rate of ester bond hydrolysis is higher under basic conditions. As a result of requiring a significantly lower amount of samples compared to traditional methods, the ME sensing technology is highly attractive for fully characterizing the degradation behavior of tissue adhesives in a wide range of physiological conditions.

Tuning Cerium(IV)-Assisted Hydrolysis of Phosphatidylcholine Liposomes under Mildly Acidic and Neutral Conditions.

With the goal of designing a lysosomal phospholipase mimic, we optimized experimental variables to enhance Ce(IV) -assisted hydrolysis of phosphatidylcholine (PC) liposomes. Our best result was obtained with the chelating agent bis-tris propane (BTP). Similar to the hydrolytic enzyme, Ce(IV) -assisted hydrolysis of PC phosphate ester bonds was higher at lysosomal pH (∼4.8) compared to pH 7.2. In the presence of BTP, the average cleavage yield at ∼pH 4.8 and 37 °C was: 67±1 %, 5.7-fold higher than at ∼pH 7.2 and roughly equivalent to the percent of phospholipid found on the metal-accessible exo leaflet of small liposomes. No Ce(IV) precipitation was observed. When BTP was absent, there was significant turbidity, and the amount of cleavage at ∼pH 4.8 (69±1 %) was 2.1-fold higher than the yield obtained at ∼pH 7.2. Our results show that BTP generates homogenous solutions of Ce(IV) that hydrolyze phosphatidylcholine with enhanced selectivity for lysosomal pH.

A first continuous 4-aminoantipyrine (4-AAP)-based screening system for directed esterase evolution.

Esterases hydrolyze ester bonds with an often high stereoselectivity as well as regioselectivity and are therefore industrially employed in the synthesis of pharmaceuticals, in food processing, and in laundry detergents. Continuous screening systems based on p-nitrophenyl- (e.g., p-nitrophenyl acetate) or umbelliferyl-esters are commonly used in directed esterase evolution campaigns. Ongoing challenges in directed esterase evolution are screening formats which offer a broad substrate spectrum, especially for complex aromatic substrates. In this report, a novel continuous high throughput screening system for indirect monitoring of esterolytic activity was developed and validated by detection of phenols employing phenyl benzoate as substrate and p-nitrobenzyl esterase (pNBEBL from Bacillus licheniformis) as catalyst. The released phenol directly reacts with 4-aminoantipyrine yielding the red compound 1,5-dimethyl-4-(4-oxo-cyclohexa-2,5-dienylidenamino)-2-phenyl-1,2-dihydro-pyrazol-3-one. In this continuous B. licheniformis esterase activity detection system (cBLE-4AAP), the product formation is followed through an increase in absorbance at 509 nm. The cBLE-4AAP screening system was optimized in 96-well microtiter plate format in respect to standard deviation (5 %), linear detection range (15 to 250 μM), lower detection limit (15 μM), and pH (7.4 to 10.4). The cBLE-4AAP screening system was validated by screening a random epPCR pNBEBL mutagenesis library (2000 clones) for improved esterase activity at elevated temperatures. Finally, the variant T3 (Ser378Pro) was identified which nearly retains its specific activity at room temperature (WT 1036 U/mg and T3 929 U/mg) and shows compared to WT a 4.7-fold improved residual activity after thermal treatment (30 min incubation at 69.4 °C; WT 170 U/mg to T3 804 U/mg).

Kinetic Studies of Reactions of Hydroxyporphyrins on Silicate Surface

Construction of the monolayer film of semiconductive and redox-active porphyrins on the metal oxides such as silicate or titanates attracts interests for possible applications of the process in fabricating organic electronic devices, organic catalysts, and organic-inorganic hybrid materials. Porphyrins bearing linker functional groups such as hydroxy or bromo groups in the peripheral meso-phenyl groups were reacted with the surface silanol groups of silicate glass at 80 to 240 oC in a solid-solid reaction to obtain the monolayer film of porphyrin on the silicate glass. The rates of the reaction were determined by visible spectroscopic studies and they decreased in the order: primary alcohol > primary bromide ~ tertiary alcohol. In addition to the structures of the linker groups, melting points of porphyrins also affect the reactivity of the porphyrin. Porphyrins with long alkyl chains reacted faster than those without long alkyl chains, because the long alkyl groups would facilitate molecular motion to reach the transition state of the reaction. Hydrolysis of the porphyrin monolayer prepared from primary alcohol in 1 M aq. HCl at 50 oC proceeded in a similar rate to that prepared from tertiary alcohol. Base catalyzed hydrolysis in 1 M aq. NH3 at 30 oC of the porphyrin monolayer prepared from tertiary alcohol proceeded 20 times slower than that prepared from the primary alcohol. In the literature, it is well established that the hydrolysis of the silicate ester bond proceeds via the Si-O bond cleavage, since the silicon atom can form a penta-coodinated structure, and much more reactive than carbon atom toward a substitution reaction. Hydrolysis of the porphyrin monolayer prepared from the tertiary alcohol in H2 18O afforded 18O-labelled tertiary alcohol, indicating that there was a covalent bond between the porphyrin and silicate glass, and the C-O bond was cleaved in the acid catalyzed hydrolysis reaction of the tertiary alkyl silicate ester on the silicate glass.

Complete regression of breast tumour with a single dose of docetaxel-entrapped core-cross-linked polymeric micelles

Treatment with chemotherapy such as docetaxel (DTX) is associated with significant toxicity and tumour recurrence. In this study, we developed DTX-entrapped core-cross-linked polymeric micelles (DTX-CCL-PMs, 66 nm size) by covalently conjugating DTX to CCL-PMs via a hydrolysable ester bond. The covalent conjugation allowed for sustained release of DTX under physiological conditions in vitro. In vivo, DTX-CCL-PMs demonstrated superior therapeutic efficacy in mice bearing MDA-MB-231 tumour xenografts as compared to the marketed formulation of DTX (Taxotere®). Strikingly, a single intravenous injection of DTX-CCL-PMs enabled complete regression of both small (∼150 mm3) and established (∼550 mm3) tumours, leading to 100% survival of the animals. These remarkable antitumour effects of DTX-CCL-PMs are attributed to its enhanced tumour accumulation and anti-stromal activity. Furthermore, DTX-CCL-PMs exhibited superior tolerability in healthy rats as compared to Taxotere. These preclinical data strongly support clinical translation of this novel nanomedicinal product for the treatment of cancer.

Transesterification of PHA to oligomers covalently bonded with (bio)active compounds containing either carboxyl or hydroxyl functionalities.

This manuscript presents the synthesis and structural characterisation of novel biodegradable polymeric controlled-release systems of pesticides with potentially higher resistance to weather conditions in comparison to conventional forms of pesticides. Two methods for the preparation of pesticide-oligomer conjugates using the transesterification reaction were developed. The first method of obtaining conjugates, which consist of bioactive compounds with the carboxyl group and polyhydroxyalkanoates (PHAs) oligomers, is "one-pot" transesterification. In the second method, conjugates of bioactive compounds with hydroxyl group and polyhydroxyalkanoates oligomers were obtained in two-step method, through cyclic poly(3-hydroxybutyrate) oligomers. The obtained pesticide-PHA conjugates were comprehensively characterised using GPC, 1H NMR and mass spectrometry techniques. The structural characterisation of the obtained products at the molecular level with the aid of mass spectrometry confirmed that both of the synthetic strategies employed led to the formation of conjugates in which selected pesticides were covalently bonded to PHA oligomers via a hydrolysable ester bond.

On the pH Dependence of Class-1 RF-Dependent Termination of mRNA Translation

We have studied the pH dependence of the rate of termination of bacterial protein synthesis catalyzed by a class-1 release factor (RF1 or RF2). We used a classical quench-flow technique and a newly developed stopped-flow technique that relies on the use of fluorescently labeled peptides. We found the termination rate to increase with increasing pH and, eventually, to saturate at about 70s−1 with an apparent pKa value of about 7.6. From our data, we suggest that class-1 RF termination is rate limited by the chemistry of ester bond hydrolysis at low pH and by a stop-codon-dependent and pH-independent conformational change of RFs at high pH. We propose that RF-dependent termination depends on the participation of a hydroxide ion rather than a water molecule in the hydrolysis of the ester bond between the P-site tRNA and its peptide chain. We provide a simple explanation for why the rate of termination saturated at high pH in our experiments but not in those of others.

Radiopaque iodinated ethers of poly(vinyl iodobenzyl ether)s: Synthesis and evaluation for endovascular embolization

ABSTRACTLeachable‐free radiopaque iodinated polymers were designed as long‐lived embolization materials visible by X‐ray tomography. This is a definite improvement over liquid embolics incorporating either radiopaque inorganic particles or iodinated polymers having hydrolysable ester bonds. Grafting 4‐iodobenzyl or 2,3,5‐triiodobenzyl groups to poly(vinyl alcohol) (PVAL) yields iodobenzyl ethers of PVAL having iodine contents in the range 40–70 wt %. Their solubility in solvents accepted for medical devices (DMSO and NMP), viscosity of concentrated solutions, precipitation behavior, radiopacity, and stability with respect to sterilization and hydrolysis were assessed. The solvent NMP allows the preparation of concentrated solutions of suitable viscosity for their application as liquid embolics. Precipitation in water yields a cohesive mass of material that can plug vascular malformations. A rationale to the properties is given in terms of the Hansen contributions to the Hildebrand solubility parameters. Iodobenzyl ethers of PVA resist hydrolysis whereas their corresponding iodobenzoyl esters leach iodinated fragments. © 2014 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2015, 132, 41791.

Cyclic Swelling as a Phenomenon Inherent to Biodegradable Polyesters

The aim of this study is to evaluate and describe the phenomenon and mechanism of the spontaneous cyclic swelling and deswelling of linear and branched aliphatic polyesters in the aqueous medium. The fluctuation of gel volume in one or several cycles as an inherent property of biodegradable and bioerodible materials has not yet been described. We have observed the process at linear and branched polyesters of aliphatic α-hydroxy acids. The period of duration of cycles was in order of hours to days, as influenced by the size of the bodies ranging from 25 to 1000 mg, the temperature in the range of 7°C-42°C, ionic strength, and pH value. The results demonstrated that swelling is accompanied by hydrolysis of ester bonds with the development of small water-soluble osmotically active molecules. After reaching a higher degree of swelling, the obstruction effect of the gel decreases and the diffusion of soluble degradation products from the body to the environment prevails. A decrease in osmotic pressure inside the body and a decrease in the hydrophilic character of the gel matrix result in deswelling by a collapse of the structure, probably due to hydrophobic interactions of nonpolar polyester chains.

열, 염산 및 수산화나트륨 처리에 의한 Vectran®섬유의 특성 변화

Abstract: In this study, research was conducted on Vectran ® fibers (highly heat resistant, high strength, lightweightindustrial fibers) to determine their suitability for use in the development of hybrid wires and cables. Vectran fiberswere heat-treated to various temperatures and treated with HCl and NaOH solutions under various conditions. Theeffects of heat, HCl, and NaOH treatment on the creep behaviors, mechanical properties, and surface properties of Vec-tran fibers were examined. X-ray diffraction (XRD) analysis was used to investigate crystallinity changes; while Fou-rier transform infrared spectroscopy (FT-IR) and X-ray photoelectron spectroscopy (XPS) were used to analyzechemical structure changes resulting from degradation. Analysis showed that the mechanical properties and crystallin-ity of Vectran fibers changed significantly by treatment at temperatures greater than 250 o C. Although HCl treatmentsdid not cause significant changes, NaOH treatments resulted in considerable changes in the surface and mechanicalproperties and crystallinity. FT-IR and XPS analyses indicated that the degradation resulted from the hydrolysis of esterbonds in the fibers. Keywords: Vectran

Solution Speciation of the Dinuclear ZrIV‐Substituted Keggin Polyoxometalate [{α‐PW11O39Zr(μ‐OH)(H2O)}2]8– and Its Reactivity towards DNA‐Model Phosphodiester Hydrolysis

AbstractThe solution speciation of the ZrIV‐substituted Keggin polyoxometalate (Et2NH2)8[{α‐PW11O39Zr(μ‐OH)(H2O)}2]·7H2O (ZrK 2:2) was fully determined under different pD, temperature, and concentration conditions. Subsequently, phosphodiester bond hydrolysis of the DNA model substrate bis(4‐nitrophenyl) phosphate (BNPP) promoted by ZrK 2:2 was studied in detail. In the presence of ZrK 2:2, phosphoester bond hydrolysis in BNPP proceeded with a rate constant of kobs = (4.75 ± 0.25) × 10–6 s–1 at pD 6.4 and 60 °C, which represented a 320‐fold rate enhancement relative to the spontaneous hydrolysis of BNPP. The pD dependence of kobs exhibits a bell‐shaped profile, with the fastest rate observed at pD 6.4. An activation energy (Ea) of 60.16 kJ mol–1, enthalpy of activation (ΔH#) of 57.44 kJ mol–1, entropy of activation (ΔS#) of –173.16 J mol–1 K–1, and Gibbs activation energy (ΔG#) of 111.12 kJ mol–1 at 37 °C were calculated. The influence of the concentration of ZrK 2:2 on the reaction rate constant was studied in the concentration range 0.5 to 6.0 mM. The results showed that ZrK 2:2 is able to hydrolyze an excess amount of BNPP, thus demonstrating that ZrK 2:2 acts as a catalyst for phospho(di)ester bond hydrolysis. In addition, the influence of ionic strength and the inhibitor diphenyl phosphate on BNPP hydrolysis were examined.

Interactions of pharmacologically active snake venom sPLA2 with different cell lines

Secreted Phospholipases A2 (sPLA2s) represent a large family of structurally related enzymes, which target different tissues and organs and induce numerous pharmacological effects based on their catalytic specificity – hydrolysis of the sn-2 ester bond of glycerophospholipids. The neurotoxin vipoxin, isolated from the venom of Vipera ammodytes meriodionalis, is a heterodimeric postsynaptic ionic complex composed of two protein subunits – a basic and toxic His48 sPLA2 enzyme and an acidic, enzymatically inactive and non-toxic component. In this paper, for the first time, we demonstrate that vipoxin sPLA2 enzyme affects cell integrity and viability of four cell types and causes different cell responses. The most dramatic local tissue effects were observed with RPE-1 (retinal pigment epithelial) cells followed by A549 (adenocarcinomic human alveolar epithelial) cells and MDCK (Madin-Darby Canine Kidney epithelial) cells. Products of the enzymatic reaction, lysophospholipids and unsaturated free fatty acids, act as lipid mediators that can induce membrane damaging or can stimulate cell proliferation. Our preliminary results on the cytotoxic effect of vipoxin sPLA2 on A549 cells are promising in searching of its eventual anticancer potential.

Role of constitutive calcium-independent phospholipase A2 beta in hippocampo-prefrontal cortical long term potentiation and spatial working memory

Calcium independent phospholipase A2 (iPLA2) is an 85kDa protein that catalyzes the hydrolysis of the sn-2 acyl ester bond of glycerophospholipids to liberate free fatty acids and lysophospholipids. In this study, we determined the role of constitutive iPLA2β in long term potentiation (LTP) of the hippocampo-prefrontal cortical pathway in vivo. We also examined the effect of iPLA2β knockdown using the rewarded alternation in T-maze task, a test of spatial working memory which is dependent on this pathway. Intracortical injection of an inhibitor to iPLA2, bromoenol lactone (BEL) or antisense oligonucleotide to iPLA2β in the prefrontal cortex abolished induction of hippocampo-prefrontal cortical LTP. Moreover, iPLA2 inhibition and antisense knockdown resulted in increased errors in the rewarded alternation in T-maze task, indicating negative effects on spatial working memory. BEL or antisense injection did not produce DNA fragmentation in the cortex as demonstrated by TUNEL assay. Results confirm a role of constitutive iPLA2β in hippocampo-prefrontal cortical synaptic plasticity in vivo, and add to previous observations of a role of iPLA2 in hippocampal LTP in vitro, and long-term memory retrieval. They may be relevant in Alzheimer’s disease, and other neurodegenerative conditions that are associated with changes in iPLA2.

New Extremophilic Lipases and Esterases from Metagenomics

Lipolytic enzymes catalyze the hydrolysis of ester bonds in the presence of water. In media with low water content or in organic solvents, they can catalyze synthetic reactions such as esterification and transesterification. Lipases and esterases, in particular those from extremophilic origin, are robust enzymes, functional under the harsh conditions of industrial processes owing to their inherent thermostability and resistance towards organic solvents, which combined with their high chemo-, regio- and enantioselectivity make them very attractive biocatalysts for a variety of industrial applications. Likewise, enzymes from extremophile sources can provide additional features such as activity at extreme temperatures, extreme pH values or high salinity levels, which could be interesting for certain purposes. New lipases and esterases have traditionally been discovered by the isolation of microbial strains producing lipolytic activity. The Genome Projects Era allowed genome mining, exploiting homology with known lipases and esterases, to be used in the search for new enzymes. The Metagenomic Era meant a step forward in this field with the study of the metagenome, the pool of genomes in an environmental microbial community. Current molecular biology techniques make it possible to construct total environmental DNA libraries, including the genomes of unculturable organisms, opening a new window to a vast field of unknown enzymes with new and unique properties. Here, we review the latest advances and findings from research into new extremophilic lipases and esterases, using metagenomic approaches, and their potential industrial and biotechnological applications.

Identification of in vitro and in vivo metabolites of 12β-hydroxylveratroylzygadenine associated with neurotoxicity by using HPLC–MS/MS

Abstract Metabolism study was carried out on 12 β -hydroxylveratroylzygadenine (VOG) that is a cevine-type alkaloid existing in Veratrum nigrum L. and a neurotoxic component. In order to better understand the potential mechanism of neurotoxicity of VOG, this study measured VOG-induced DNA damage in the cerebellum and cerebral cortex of mice after 7 days repetitive oral dose by using single-cell gel electrophoresis (Comet assay). High performance liquid chromatography-tandem mass spectrometry (LC–MS/MS) was developed and applied to separate and identify in vitro and in vivo metabolites of VOG for investing the possible relationship of metabolism and neurotoxicity. In vitro experiment was carried out using rat liver microsomes, while the in vivo study was conducted on rats. The obtained results indicated that VOG might cause DNA damage in cerebellum and cerebral cortex of mice in a dose-dependent manner. Hydrolysis of ester bond and O -demethylation were proposed to be the main in vivo metabolic pathways of VOG, while the major in vitro metabolic pathways were proposed as methyl oxidation to aldehyde, dehydrogenation, hydrolysis of ester bond, hydrolysis of ester bond together with acetylation, and methoxylation. O -Demethylation reaction was likely to be associated with reactive oxygen species production, leading to the DNA damage.

Comparison of three tannases cloned from closely related lactobacillus species: L. Plantarum, L. Paraplantarum, and L. Pentosus

BackgroundTannase (tannin acyl hydrolase, EC 3.1.1.20) specifically catalyzes the hydrolysis of the galloyl ester bonds in hydrolyzable tannins to release gallic acid. The enzyme was found not only in fungal species but also many bacterial species including Lactobacillus plantarum, L. paraplantarum, and L. pentosus. Recently, we identified and expressed a tannase gene of L. plantarum, tanLpl, to show remarkable differences to characterized fungal tannases. However, little is known about genes responsible for tannase activities of L. paraplantarum and L. pentosus. We here identify the tannase genes (i.e. tanLpa and tanLpe) of the above lactobacilli species, and describe their molecular diversity among the strains as well as enzymological difference between species inclusive of L. plantarum.ResultsThe genes encoding tannase, designated tanLpa and tanLpe, were cloned from Lactobacillus paraplantarum NSO120 and Lactobacillus pentosus 21A-3, which shared 88% and 72% amino acid identity with TanLpl, cloned from Lactobacillus plantarum ATCC 14917T, respectively. These three enzymes could comprise a novel tannase subfamily of independent lineage, because no other tannases in the databases share significant sequence similarity with them. Each of tanLpl, tanLpa, and tanLpe was expressed in Bacillus subtilis RIK 1285 and recombinant enzymes were secreted and purified. The Km values of the enzymes on each galloyl ester were comparable; however, the kcat/Km values of TanLpa for EGCg, ECg, Cg, and GCg were markedly higher than those for TanLpl and TanLpe. Their enzymological properties were compared to reveal differences at least in substrate specificity.ConclusionTwo tannase genes responsible for tannase activities of L. paraplantarum and L. pentosus were identified and characterized. TanLpl, TanLpa and TanLpe forming a phylogenetic cluster in the known bacterial tannase genes and had a limited diversity in each other. Their enzymological properties were compared to reveal differences at least in substrate specificity. This is the first comparative study of closely related bacterial tannases.

Study of in vitro metabolism of m-nisoldipine in human liver microsomes and recombinant cytochrome P450 enzymes by liquid chromatography–mass spectrometry

This is a report about the investigation of the metabolic fate of m-nisoldipine in human liver microsomes and the recombinant cytochrome P450 enzymes by using LC–MS/MS. A sensitive and reliable LC–MS/MS method was developed to obtain a rapid and complete characterization of new metabolites and the metabolism pathways. The analytes were separated on a reversed phase C18 column with acetonitrile and 0.1% aqueous formic acid as the mobile phase. Tandem mass spectrometry with positive electrospray ionization was used to enable the structural characterization of the metabolites. A total of 10 metabolites were characterized with proposed structures in the incubation of human liver microsomes by comparing their retention times and spectral patterns with those of the parent drug. Dehydrogenation of the dihydropyridine core and reactions of side chains such as hydroxylation and hydrolysis of ester bonds were the major metabolic pathways. The specific cytochrome P450 (CYP) enzymes responsible for m-nisoldipine metabolites were identified using chemical inhibition and cDNA expressed CYP enzymes. The results indicated that CYP2C19 and CYP3A4 might play major roles in the metabolism of m-nisoldipine in human liver microsomes.

New La(III) Complex Immobilized on 3-Aminopropyl-Functionalized Silica as an Efficient and Reusable Catalyst for Hydrolysis of Phosphate Ester Bonds

Described herein is the synthesis, structure, and monoesterase and diesterase activities of a new mononuclear [La(III)(L(1))(NO3)2] (1) complex (H2L(1) = 2-bis[{(2-pyridylmethyl)-aminomethyl}-6-[N-(2-pyridylmethyl) aminomethyl)])-4-methyl-6-formylphenol) in the hydrolysis of 2,4-bis(dinitrophenyl)phosphate (2,4-BDNPP). When covalently linked to 3-aminopropyl-functionalized silica, 1 undergoes disproportionation to form a dinuclear species (APS-1), whose catalytic efficiency is increased when compared to the homogeneous reaction due to second coordination sphere effects which increase the substrate to complex association constant. The anchored catalyst APS-1 can be recovered and reused for subsequent hydrolysis reactions (five times) with only a slight loss in activity. In the presence of DNA, we suggest that 1 is also converted into the dinuclear active species as observed with APS-1, and both were shown to be efficient in DNA cleavage.

Biosynthesis, structural architecture and biotechnological potential of bacterial tannase: A molecular advancement

Tannin-rich materials are abundantly generated as wastes from several agroindustrial activities. Therefore, tannase is an interesting hydrolase, for bioconversion of tannin-rich materials into value added products by catalyzing the hydrolysis of ester and depside bonds and unlocked a new prospect in different industrial sectors like food, beverages, pharmaceuticals, etc. Microorganisms, particularly bacteria are one of the major sources of tannase. In the last decade, cloning and heterologous expression of novel tannase genes and structural study has gained momentum. In this article, we have emphasized critically on bacterial tannase that have gained worldwide research interest for their diverse properties. The present paper delineate the developments that have taken place in understanding the role of tannase action, microbial sources, various cultivation aspects, downstream processing, salient biochemical properties, structure and active sites, immobilization, efforts in cloning and overexpression and with special emphasis on recent molecular and biotechnological achievements.