Displaying publications 1 - 20 of 55 in total

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  1. Ekeoma BC, Ekeoma LN, Yusuf M, Haruna A, Ikeogu CK, Merican ZMA, et al.
    J Biotechnol, 2023 Jun 10;369:14-34.
    PMID: 37172936 DOI: 10.1016/j.jbiotec.2023.05.003
    The issue of environmental pollution has been worsened by the emergence of new contaminants whose morphology is yet to be fully understood . Several techniques have been adopted to mitigate the pollution effects of these emerging contaminants, and bioremediation involving plants, microbes, or enzymes has stood out as a cost-effective and eco-friendly approach. Enzyme-mediated bioremediation is a very promising technology as it exhibits better pollutant degradation activity and generates less waste. However, this technology is subject to challenges like temperature, pH, and storage stability, in addition to recycling difficulty as it is arduous to isolate them from the reaction media. To address these challenges, the immobilization of enzymes has been successfully applied to ameliorate the activity, stability, and reusability of enzymes. Although this has significantly increased the uses of enzymes over a wide range of environmental conditions and facilitated the use of smaller bioreactors thereby saving cost, it still comes with additional costs for carriers and immobilization. Additionally, the existing immobilization methods have their individual limitations. This review provides state-of-the-art information to readers focusing on bioremediation using enzymes. Different parameters such as: the sustainability of biocatalysts, the ecotoxicological evaluation of transformation contaminants, and enzyme groups used were reviewed. The efficacy of free and immobilized enzymes, materials and methods for immobilization, bioreactors used, challenges to large-scale implementation, and future research needs were thoroughly discussed.
    Matched MeSH terms: Biocatalysis
  2. Sharma T, Xia C, Sharma A, Raizada P, Singh P, Sharma S, et al.
    Bioengineered, 2022 Apr;13(4):10518-10539.
    PMID: 35443858 DOI: 10.1080/21655979.2022.2062526
    Enzymes of commercial importance, such as lipase, amylase, laccase, phytase, carbonic anhydrase, pectinase, maltase, glucose oxidase etc., show multifunctional features and have been extensively used in several fields including fine chemicals, environmental, pharmaceutical, cosmetics, energy, food industry, agriculture and nutraceutical etc. The deployment of biocatalyst in harsh industrial conditions has some limitations, such as poor stability. These drawbacks can be overcome by immobilizing the enzyme in order to boost the operational stability, catalytic activity along with facilitating the reuse of biocatalyst. Nowadays, functionalized polymers and composites have gained increasing attention as an innovative material for immobilizing the industrially important enzyme. The different types of polymeric materials and composites are pectin, agarose, cellulose, nanofibers, gelatin, and chitosan. The functionalization of these materials enhances the loading capacity of the enzyme by providing more functional groups to the polymeric material and hence enhancing the enzyme immobilization efficiency. However, appropriate coordination among the functionalized polymeric materials and enzymes of interest plays an important role in producing emerging biocatalysts with improved properties. The optimal coordination at a biological, physical, and chemical level is requisite to develop an industrial biocatalyst. Bio-catalysis has become vital aspect in pharmaceutical and chemical industries for synthesis of value-added chemicals. The present review describes the current advances in enzyme immobilization on functionalized polymers and composites. Furthermore, the applications of immobilized enzymes in various sectors including bioremediation, biosensor and biodiesel are also discussed.
    Matched MeSH terms: Biocatalysis
  3. Hau EH, Teh SS, Yeo SK, Mah SH
    J Sci Food Agric, 2022 Jan 15;102(1):233-240.
    PMID: 34081335 DOI: 10.1002/jsfa.11350
    BACKGROUND: The oil palm tree produces 90% of wastes and the limited usage of these wastes causes a major disposal problem in the mills. Nevertheless, these by-products have a large amount of nutritional components. Thus, the present study aimed to determine the physicochemical and functional properties of protein hydrolysates (PH) from oil palm leaves (OPL) extracted using different concentrations of Alcalase (0-10%) at 2 h of hydrolysis time.

    RESULTS: Fourier transform infrared spectral analyses showed that the enzymatic hydrolysis altered functional groups of OPL where a secondary amine was present in the PH. Changes were also observed in the thermal stability where the enthalpy heat obtained for PH (933.93-1142.57 J g-1 ) was much lower than OPL (7854.11 J g-1 ). The results showed that the PH extracted by 8% Alcalase exhibited absolute zeta potential, as well as a high emulsifying activity index (70.64 m2  g-1 of protein) and emulsion stability index (60.58 min). Furthermore, this PH showed higher solubility (96.32%) and emulsifying properties compared to other PHs. It is also comparable with commercial plant proteins, indicating that 8% Alcalase is an optimum concentration for hydrolysis.

    CONCLUSION: In summary, the physicochemical and functional properties of PH extracted from OPL showed good functional properties, suggesting that it can be used as an alternative plant protein in food industries. © 2021 Society of Chemical Industry.

    Matched MeSH terms: Biocatalysis
  4. Bilal M, Lam SS, Iqbal HMN
    Environ Pollut, 2022 Jan 15;293:118582.
    PMID: 34856243 DOI: 10.1016/j.envpol.2021.118582
    The discharge of an alarming number of recalcitrant pollutants from various industrial activities presents a serious threat to environmental sustainability and ecological integrity. Bioremediation has gained immense interest around the world due to its environmentally friendly and cost-effective nature. In contrast to physical and chemical methods, the use of microbial enzymes, particularly immobilized biocatalysts, has been demonstrated as a versatile approach for the sustainable mitigation of environmental pollution. Considerable attention is now devoted to developing novel enzyme engineering approaches and state-of-the-art bioreactor design for ameliorating the overall bio-catalysis and biodegradation performance of enzymes. This review discusses the contemporary and state of the art technical and scientific progress regarding applying oxidoreductase enzyme-based biocatalytic systems to remediate a vast number of pharmaceutically active compounds from water and wastewater bodies. A comprehensive insight into enzyme immobilization, the role of mediators, bioreactors designing, and transformation products of pharmaceuticals and their associated toxicity is provided. Additional studies are necessary to elucidate enzymatic degradation mechanisms, monitor the toxicity levels of the resulting degraded metabolites and optimize the entire bio-treatment strategy for technical and economical affordability.
    Matched MeSH terms: Biocatalysis
  5. Johan UUM, Rahman RNZRA, Kamarudin NHA, Ali MSM
    Colloids Surf B Biointerfaces, 2021 Sep;205:111882.
    PMID: 34087776 DOI: 10.1016/j.colsurfb.2021.111882
    Carboxylesterases (CEs) are members of prominent esterase, and as their name imply, they catalyze the cleavage of ester linkages. By far, a considerable number of novel CEs have been identified to investigate their exquisite physiological and biochemical properties. They are abundant enzymes in nature, widely distributed in relatively broad temperature range and in various sources; both macroorganisms and microorganisms. Given the importance of these enzymes in broad industries, interest in the study of their mechanisms and structural-based engineering are greatly increasing. This review presents the current state of knowledge and understanding about the structure and functions of this ester-metabolizing enzyme, primarily from bacterial sources. In addition, the potential biotechnological applications of bacterial CEs are also encompassed. This review will be useful in understanding the molecular basis and structural protein of bacterial CEs that are significant for the advancement of enzymology field in industries.
    Matched MeSH terms: Biocatalysis
  6. Jacob AG, Wahab RA, Mahat NA
    Enzyme Microb Technol, 2021 Aug;148:109807.
    PMID: 34116744 DOI: 10.1016/j.enzmictec.2021.109807
    Oil palm leaves (OPL) silica (SiO2) can replace the energy-intensive, commercially produced SiO2. Moreover, the agronomically sourced biogenic SiO2 is more biocompatible and cost-effective enzyme support, which properties could be improved by the addition of magnetite (Fe3O4) and graphene oxide (GO) to yield better ternary support to immobilize enzymes, i.e., Candida rugosa lipase (CRL). This study aimed to optimize the Candida rugosa lipase (CRL immobilization onto the ternary OPL-silica-magnetite (Fe3O4)-GO (SiO2/Fe3O4/GO) support, for use as biocatalyst for ethyl valerate (EV) production. Notably, this is the first study detailing the CRL/SiO2/Fe3O4/GO biocatalyst preparation for rapid and high yield production of ethyl valerate (EV). AFM and FESEM micrographs revealed globules of CRL covalently bound to GL-A-SiO2/Fe3O4/GO; similar to Raman and UV-spectroscopy results. FTIR spectra revealed amide bonds at 3478 cm-1 and 1640 cm-1 from covalent interactions between CRL and GL-A-SiO2/Fe3O4/GO. Optimum immobilization conditions were 4% (v/v) glutaraldehyde, 8 mg/mL CRL, at 16 h stirring in 150 mM NaCl at 30 °C, offering 24.78 ± 0.26 mg/g protein (specific activity = 65.24 ± 0.88 U/g). The CRL/SiO2/Fe3O4/GO yielded 77.43 ± 1.04 % of EV compared to free CRL (48.75 ± 0.70 %), verifying the suitability of SiO2/Fe3O4/GO to hyperactivate and stabilize CRL for satisfactory EV production.
    Matched MeSH terms: Biocatalysis
  7. Rafiqul ISM, Mimi Sakinah AM, Zularisam AW
    Prep Biochem Biotechnol, 2021;51(10):1060-1070.
    PMID: 33724897 DOI: 10.1080/10826068.2021.1897840
    Enzymatic production of bioxylitol from lignocellulosic biomass (LCB) provides a promising alternative to both chemical and fermentative routes. This study aimed to assess the impacts of catalytic variables on bioxylitol production from wood sawdust using xylose reductase (XR) enzyme and to optimize the bioprocess. Enzyme-based xylitol production was carried out in batch cultivation under various experimental conditions to obtain maximum xylitol yield and productivity. The response surface methodology (RSM) was followed to fine-tune the most significant variables such as reaction time, temperature, and pH, which influence the synthesis of bioxylitol from sawdust hydrolysate and to optimize them. The optimum time, temperature, and pH became were 12.25 h, 35 °C, and 6.5, respectively, with initial xylose 18.8 g/L, NADPH 2.83 g/L, XR 0.027 U/mg, and agitation 100 rpm. The maximum xylitol production was attained at 16.28 g/L with a yield and productivity of 86.6% (w/w) and 1.33 g/L·h, respectively. Optimization of catalytic parameters using sequential strategies resulted in 1.55-fold improvement in overall xylitol production. This study explores a novel strategy for using sawdust hemicellulose in bioxylitol production by enzyme technology.
    Matched MeSH terms: Biocatalysis
  8. Onoja E, Wahab RA
    Appl Biochem Biotechnol, 2020 Oct;192(2):585-599.
    PMID: 32495234 DOI: 10.1007/s12010-020-03348-0
    Strategies to immobilize the individual enzymes are crucial for enhancing catalytic applicability and require a controlled immobilization process. Herein, protocol for immobilizing Candida rugosa lipase (CRL) onto modified magnetic silica derived from oil palm leaves ash (OPLA) was optimized for the effects of concentration of CRL, immobilization time, and temperature, monitored by titrimetric and spectrometric methods. XRD and TGA-DTG spectrometric observations indicated that OPLA-silica was well coated over magnetite (SiO2-MNPs) and CRLs were uniformly bound by covalent bonds to SiO2-MNPs (CRL/Gl-A-SiO2-MNPs). The optimized immobilization protocol showed that in the preparation of CRL/Gl-A-SiO2-MNPs, CRL with 68.3 mg/g protein loading and 74.6 U/g specific activity was achieved using 5 mg/mL of CRL, with an immobilization time of 12 h at 25 °C. The present work also demonstrated that acid-pretreated OPLA is a potential source of renewable silica, envisioning its applicability for practical use in enzymatic catalysis on solid support.
    Matched MeSH terms: Biocatalysis
  9. Ling JWA, Chang LS, Babji AS, Lim SJ
    J Sci Food Agric, 2020 Oct;100(13):4714-4722.
    PMID: 32468613 DOI: 10.1002/jsfa.10530
    BACKGROUND: Processing of edible bird's nest (EBN) requires extensive washing to remove impurities and produces huge amounts of EBN co-products, which contain mainly feathers with glycoproteins attached, which are usually discarded. This study was conducted to recover the valuable EBN glycoproteins from the waste material. Enzymatic hydrolysis was applied to recover EBN glycopeptides from EBN co-products (EBNcoP ) and processed cleaned EBN (EBNclean ) was used as control, which were then freeze-dried into EBN hydrolysates (EBNhcoP and EBNhclean , respectively).

    RESULTS: The recovery yield for EBNhclean and EBNhcoP were 89.09 ± 0.01% and 47.64 ± 0.26%, respectively, indicating nearly 50% of glycopeptide can be recovered from the waste material. Meanwhile, N-acetylneuraminic acid, a major acid sugar in EBN glycoproteins, of EBNhcoP increased by 229% from 58.6 ± 3.9 to 192.9 ± 3.1 g kg-1 , indicating the enzymatic hydrolysis removed impurities and thus enhanced the N-acetylneuraminic acid content. Total soluble protein was more than 330 g kg-1 for all the samples. Colour parameter showed that hydrolysate samples have greater L* (lightness) values. Chroma result indicates the intensity of all the samples were low (

    Matched MeSH terms: Biocatalysis
  10. Wang S, Lee WJ, Wang Y, Tan CP, Lai OM, Wang Y
    J Agric Food Chem, 2020 Aug 05;68(31):8391-8403.
    PMID: 32511921 DOI: 10.1021/acs.jafc.0c01346
    Medium-chain diacylglycerol (MCD), medium-long-chain diacylglycerol (MLCD), and long-chain diacylglycerol (LCD) were prepared through enzymatic esterification using different conditions at temperatures of 55-70 °C and reaction times of 1.5-5 h and in the presence of 5-6% Novozym 435. Subsequently, purification was performed using three different techniques, namely, molecular distillation (MD), deodorization (DO), and silica gel column chromatography (SGCC). Variations in terms of the physicochemical and thermodynamic properties, crystallization properties, and kinetics of the diacylglycerols (DAGs) before and after purification were determined. Irrespective of the DAG chain lengths, SGCC was able to produce samples with high DAG purity (96-99 wt %), followed by MD (58-79 wt %) and DO (39-59 wt %). A higher 1,3-DAG/1,2-DAG ratio was recorded for all samples, with the highest ratio recorded for SGCC purified samples. Regardless of the purification techniques used, the solid fat content (SFC) profiles of crude samples with steep curves were altered post-purification, showing a gradual increment in SFC along with increasing temperature. Modification of the Avrami constant and coefficient suggested the modification of the crystal growth mechanism post-purification. Crystallization and melting temperatures of products with a higher DAG purity were shifted to a higher temperature region. Variations were also reflected in terms of the crystal polymorphism, whereby the α and β' crystals transitioned into the more stable β form in purified samples accompanied by modification in the microstructures and crystal sizes. However, there was insignificant change in the morphology of MLCD crystal after purification, except for the decrease in crystal sizes. In conclusion, synthesis of MCD, MLCD, and LCD comprising different DAG purities had distinctive SFC profiles, thermodynamic properties, crystallization kinetics, and crystal morphologies, which can be further incorporated into the preparation of a variety of fat products to obtain end products with desired characteristics.
    Matched MeSH terms: Biocatalysis
  11. Saat MN, Mohamad Annuar MS
    Biotechnol Appl Biochem, 2020 May;67(3):354-365.
    PMID: 31746015 DOI: 10.1002/bab.1859
    One-pot synthesis of sugar-functionalized oligomeric caprolactone was carried out by lipase-catalyzed esterification of ε-caprolactone (ECL) with methyl-d-glucopyranoside (MGP) followed by the elongation of functionalized oligomer chain. Functionalization was performed in a custom-fabricated glass reactor equipped with Rushton turbine impeller and controlled temperature at 60 °C using tert-butanol as reaction medium. The overall reaction steps include MGP esterification of ECL monomer and its subsequent elongation by free 6-hydroxyhexanoate monomer units. A ping-pong bi-bi mechanism without ternary complex was proposed for esterification of ECL and MGP with apparent values of kinetic constant, namely maximal velocity (Vmax ), Michaelis constant for MGP (KmMGP ), and Michaelis constant for ECL (KmECL ) at 3.848 × 10-3  M H-1 , 8.189 × 10-2  M, and 6.050 M, respectively. Chain propagation step of MGP-functionalized ECL oligomer exhibits the properties of living polymerization mechanism. Linear relationship between conversion (%) and number average molecular weight, Mn (g mol-1 ), of functionalized oligomer was observed. Synthesized functionalized oligomer showed narrow range of molecular weight from 1,400 to 1,600 g mol-1 with more than 90% conversion achieved. Structural analysis confirmed the presence of covalent bond between the hydroxyl group in MGP with carboxyl end group of ECL oligomer.
    Matched MeSH terms: Biocatalysis
  12. Sivapragasam M, Moniruzzaman M, Goto M
    Biotechnol J, 2020 Apr;15(4):e1900073.
    PMID: 31864234 DOI: 10.1002/biot.201900073
    Ionic liquids (ILs), a class of materials with unique physicochemical properties, have been used extensively in the fields of chemical engineering, biotechnology, material sciences, pharmaceutics, and many others. Because ILs are very polar by nature, they can migrate into the environment with the possibility of inclusion in the food chain and bioaccumulation in living organisms. However, the chemical natures of ILs are not quintessentially biocompatible. Therefore, the practical uses of ILs must be preceded by suitable toxicological assessments. Among different methods, the use of microorganisms to evaluate IL toxicity provides many advantages including short generation time, rapid growth, and environmental and industrial relevance. This article reviews the recent research progress on the toxicological properties of ILs toward microorganisms and highlights the computational prediction of various toxicity models.
    Matched MeSH terms: Biocatalysis
  13. Morsy SAGZ, Ahmad Tajudin A, Ali MSM, Shariff FM
    Front Microbiol, 2020;11:572309.
    PMID: 33101245 DOI: 10.3389/fmicb.2020.572309
    The world today is in a quest for new means of environmental remediation as the methods currently used are not sufficient to halt the damage. Mostly, a global direction is headed toward a shift from traditional chemical-based methods to a more ecofriendly alternative. In this context, biocatalysis is seen as a cost-effective, energy saving, and clean alternative. It is meant to catalyze degradation of recalcitrant chemicals in an easy, rapid, green, and sustainable manner. One already established application of biocatalysis is the removal of dyes from natural water bodies using enzymes, notably oxidoreductases like laccases, due to their wide range of substrate specificity. In order to boost their catalytic activity, various methods of enhancements have been pursued including immobilization of the enzyme on different support materials. Aside from increased catalysis, immobilized laccases have the advantages of higher stability, better durability against harsh environment conditions, longer half-lives, resistance against protease enzymes, and the ability to be recovered for reuse. This review briefly outlines the current methods used for detoxification and decolorization of dye effluents stressing on the importance of laccases as a revolutionary biocatalytic solution to this environmental problem. This work highlights the significance of laccase immobilization and also points out some of the challenges and opportunities of this technology.
    Matched MeSH terms: Biocatalysis
  14. Elias N, Wahab RA, Chandren S, Abdul Razak FI, Jamalis J
    Enzyme Microb Technol, 2019 Nov;130:109367.
    PMID: 31421729 DOI: 10.1016/j.enzmictec.2019.109367
    Currently, the chemically-assisted esterification to manufacture butyl butyrate employs corrosive homogeneous acid catalyst and liberates enormous quantities of hazardous by-products which complicate downstream treatment processes. This study aimed to identify the optimized esterification conditions, and the kinetic aspects of the enzyme-assisted synthesis of butyl butyrate using immobilized Candida rugosa lipase activated by chitosan-reinforced nanocellulose derived from raw oil palm leaves (CRL/CS-NC). The best process variables that gave the maximum conversion degree of butyl butyrate by CRL/CS-NC (90.2%) in just 3 h, as compared to free CRL (62.9%) are as follows: 50 °C, 1:2 M ratio of acid/alcohol, stirring rate of 200 rpm and a 3 mg/mL enzyme load. The enzymatic esterification followed the ping pong bi-bi mechanism with substrate inhibition, revealing a ˜1.1-fold higher Ki for CRL/CS-NC (55.55 mM) over free CRL (50.68 mM). This indicated that CRL/CS-NC was less inhibited by the substrates. Butanol was preferred over butyric acid as reflected by the higher apparent Michaelis-Menten constant of CRL/CS-NC for butanol (137 mM) than butyric acid (142.7 mM). Thus, the kinetics data conclusively showed that CRL/CS-NC (Vmax 0.48 mM min-1, Keff 0.07 min-1 mM-1) was catalytically more efficient than free CRL (Vmax 0.35 mM min-1, Keff 0.06 min-1 mM-1).
    Matched MeSH terms: Biocatalysis
  15. Fong MJB, Loy ACM, Chin BLF, Lam MK, Yusup S, Jawad ZA
    Bioresour Technol, 2019 Oct;289:121689.
    PMID: 31252316 DOI: 10.1016/j.biortech.2019.121689
    In the present study, catalytic pyrolysis of Chlorella vulgaris biomass was conducted to analyse the kinetic and thermodynamic performances through thermogravimetric approach. HZSM-5 zeolite, limestone (LS), bifunctional HZSM-5/LS were used as catalysts and the experiments were heated from 50 to 900 °C at heating rates of 10-100 °C/min. Iso-conversional model-free methods such as Flynn-Wall-Ozawa (FWO), Kissinger-Akahira-Sunose (KAS), Starink's, and Vyazovkin (V) were employed to evaluate the kinetic parameters meanwhile the thermodynamic parameters were determined by using FWO and KAS methods. The calculated EA values of non-catalytic and catalytic pyrolysis of HZSM-5 zeolite, LS, and bifunctional HZSM-5/LS were determined to be in the range of 156.16-158.10 kJ/mol, 145.26-147.84 kJ/mol, 138.81-142.06 kJ/mol, and 133.26 kJ/mol respectively. The results have shown that catalytic pyrolysis with the presence of bifunctional HZSM-5/LS resulted to a lower average EA and ΔH compared to HZSM-5, and LS which indicated less energy requirement in the process.
    Matched MeSH terms: Biocatalysis
  16. Monajemi H, Md Zain S, Ishida T, Wan Abdullah WAT
    Biochem. Cell Biol., 2019 08;97(4):497-503.
    PMID: 30444637 DOI: 10.1139/bcb-2018-0220
    The search for the mechanism of ribosomal peptide bond formation is still ongoing. Even though the actual mechanism of peptide bod formation is still unknown, the dominance of proton transfer in this reaction is known for certain. Therefore, it is vital to take the quantum mechanical effects on proton transfer reaction into consideration; the effects of which were neglected in all previous studies. In this study, we have taken such effects into consideration using a semi-classical approach to the overall reaction mechanism. The M06-2X density functional with the 6-31++G(d,p) basis set was used to calculate the energies of the critical points on the potential energy surface of the reaction mechanism, which are then used in transition state theory to calculate the classical reaction rate. The tunnelling contribution is then added to the classical part by calculating the transmission permeability and tunnelling constant of the reaction barrier, using the numerical integration over the Boltzmann distribution for the symmetrical Eckart potential. The results of this study, which accounts for quantum effects, indicates that the A2451 ribosomal residue induces proton tunnelling in a stepwise peptide bond formation.
    Matched MeSH terms: Biocatalysis*
  17. Wong YM, Show PL, Wu TY, Leong HY, Ibrahim S, Juan JC
    J Biosci Bioeng, 2019 Feb;127(2):150-159.
    PMID: 30224189 DOI: 10.1016/j.jbiosc.2018.07.012
    Bio-hydrogen production from wastewater using sludge as inoculum is a sustainable approach for energy production. This study investigated the influence of initial pH and temperature on bio-hydrogen production from dairy wastewater using pretreated landfill leachate sludge (LLS) as an inoculum. The maximum yield of 113.2 ± 2.9 mmol H2/g chemical oxygen demand (COD) (12.8 ± 0.3 mmol H2/g carbohydrates) was obtained at initial pH 6 and 37 °C. The main products of volatile fatty acids were acetate and butyrate with the ratio of acetate:butyrate was 0.4. At optimum condition, Gibb's free energy was estimated at -40 kJ/mol, whereas the activation enthalpy and entropy were 65 kJ/mol and 0.128 kJ/mol/l, respectively. These thermodynamic quantities suggest that bio-hydrogen production from dairy wastewater using pretreated LLS as inoculum was effective and efficient. In addition, genomic and bioinformatics analyses were performed in this study.
    Matched MeSH terms: Biocatalysis
  18. Ng YL, Olivos-García A, Lim TK, Noordin R, Lin Q, Othman N
    Am J Trop Med Hyg, 2018 12;99(6):1518-1529.
    PMID: 30298805 DOI: 10.4269/ajtmh.18-0415
    Entamoeba histolytica is a protozoan parasite that causes amebiasis and poses a significant health risk for populations in endemic areas. The molecular mechanisms involved in the pathogenesis and regulation of the parasite are not well characterized. We aimed to identify and quantify the differentially abundant membrane proteins by comparing the membrane proteins of virulent and avirulent variants of E. histolytica HM-1:IMSS, and to investigate the potential associations among the differentially abundant membrane proteins. We performed quantitative proteomics analysis using isobaric tags for relative and absolute quantitation labeling, in combination with two mass spectrometry instruments, that is, nano-liquid chromatography (nanoLC)-matrix-assisted laser desorption/ionization-mass spectrometry/mass spectrometry and nanoLC-electrospray ionization tandem mass spectrometry. Overall, 37 membrane proteins were found to be differentially abundant, whereby 19 and 18 membrane proteins of the virulent variant of E. histolytica increased and decreased in abundance, respectively. Proteins that were differentially abundant include Rho family GTPase, calreticulin, a 70-kDa heat shock protein, and hypothetical proteins. Analysis by Protein ANalysis THrough Evolutionary Relationships database revealed that the differentially abundant membrane proteins were mainly involved in catalytic activities (29.7%) and metabolic processes (32.4%). Differentially abundant membrane proteins that were found to be involved mainly in the catalytic activities and the metabolic processes were highlighted together with their putative roles in relation to the virulence. Further investigations should be performed to elucidate the roles of these proteins in E. histolytica pathogenesis.
    Matched MeSH terms: Biocatalysis
  19. Pakalapati H, Arumugasamy SK, Jewaratnam J, Wong YJ, Khalid M
    Biopolymers, 2018 Dec;109(12):e23240.
    PMID: 30489632 DOI: 10.1002/bip.23240
    A statistical approach with D-optimal design was used to optimize the process parameters for polycaprolactone (PCL) synthesis. The variables selected were temperature (50°C-110°C), time (1-7 h), mixing speed (50-500 rpm) and monomer/solvent ratio (1:1-1:6). Molecular weight was chosen as response and was determined using matrix-assisted laser desorption/ionization time of flight (MALDI TOF). Using the D-optimal method in design of experiments, the interactions between parameters and responses were analysed and validated. The results show a good agreement with a minimum error between the actual and predicted values.
    Matched MeSH terms: Biocatalysis
  20. Liang H, Qin X, Tan CP, Li D, Wang Y
    J Agric Food Chem, 2018 Nov 21;66(46):12361-12367.
    PMID: 30394748 DOI: 10.1021/acs.jafc.8b04804
    Docosahexaenoyl and eicosapentaenoyl ethanolamides (DHEA and EPEA) have physiological functions, including immunomodulation, brain development, and anti-inflammation, but their efficient production is still unresolved. In this study, choline-chloride-based natural deep eutectic solvents are used as media to improve the production of DHEA and EPEA. The water content showed a key effect on the reactant conversion. Adding water to choline chloride-glucose (CG, molar ratio of 5:2) led to a significant increase (13.03% for EPEA and 27.95% for DHEA) in the yields after 1 h. The high yields of EPEA (96.84%) and DHEA (90.06%) were obtained under the optimized conditions [fish oil ethyl esters/ethanolamine molar ratio of 1:2, temperature of 60 °C, 1 h, enzyme loading of 2195 units, and CG containing 8.50% water of 43.30% (w/w, relative to total reactants)]. The products could be easily separated using centrifugation. In summary, the research has the potential to produce fatty acyl ethanolamides.
    Matched MeSH terms: Biocatalysis
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