Displaying publications 1 - 20 of 42 in total

Abstract:
Sort:
  1. Chan KG, Chong TM, Adrian TG, Kher HL, Hong KW, Grandclément C, et al.
    Genome Announc, 2015;3(6).
    PMID: 26659682 DOI: 10.1128/genomeA.01442-15
    Stenotrophomonas maltophilia ZBG7B was isolated from vineyard soil of Zellenberg, France. Here, we present the draft genome sequence of this bacterial strain, which has facilitated the prediction of function for several genes encoding biotechnologically important enzymes, such as xylosidase, xylanase, laccase, and chitinase.
    Matched MeSH terms: Laccase
  2. Sayyed RZ, Bhamare HM, Sapna, Marraiki N, Elgorban AM, Syed A, et al.
    PLoS One, 2020;15(6):e0229968.
    PMID: 32497077 DOI: 10.1371/journal.pone.0229968
    Although laccase has been recognized as a wonder molecule and green enzyme, the use of low yielding fungal strains, poor production, purification, and low enzyme kinetics have hampered its large-scale application. Thus,this study aims to select high yielding fungal strains and optimize the production, purification, and kinetics of laccase of Aspergillus sp. HB_RZ4. The results obtained indicated that Aspergillus sp. HB_RZ4 produced a significantly large amount of laccase under meso-acidophilic shaking conditions in a medium containing glucose and yeast extract. A 25 μM CuSO4 was observed to enhance the enzyme yield. The enzyme was best purified on a Sephadex G-100 column. The purified enzyme resembled laccase of A. flavus. The kinetics of the purified enzyme revealed high substrate specificity and good velocity of reaction,using ABTS as a substrate. The enzyme was observed to be stable over various pH values and temperatures. The peptide structure of the purified enzyme was found to resemble laccase of A. kawachii IFO 4308. The fungus was observed to decolorize various dyes independent of the requirement of a laccase mediator system.Aspergillus sp. HB_RZ4 was observed to be a potent natural producer of laccase, and it decolorized the dyes even in the absence of a laccase mediator system. Thus, it can be used for bioremediation of effluent that contains non-textile dyes.
    Matched MeSH terms: Laccase/antagonists & inhibitors; Laccase/metabolism*; Laccase/chemistry
  3. Razak NN, Annuar MS
    Appl Biochem Biotechnol, 2014 Mar;172(6):2932-44.
    PMID: 24464534 DOI: 10.1007/s12010-014-0731-7
    Free laccase and fungal biomass from white-rot fungi were compared in the thermokinetics study of the laccase-catalyzed decolorization of an azo dye, i.e., Trypan Blue. The decolorization in both systems followed a first-order kinetics. The apparent first-order rate constant, k1', value increases with temperature. Apparent activation energy of decolorization was similar for both systems at ∼ 22 kJ mol(-1), while energy for laccase inactivation was 18 kJ mol(-1). Although both systems were endothermic, fungal biomass showed higher enthalpy, entropy, and Gibbs free energy changes for the decolorization compared to free laccase. On the other hand, free laccase showed reaction spontaneity over a wider range of temperature (ΔT = 40 K) as opposed to fungal biomass (ΔT = 15 K). Comparison of entropy change (ΔS) values indicated metabolism of the dye by the biomass.
    Matched MeSH terms: Laccase/chemistry*
  4. Karimi S, Abdulkhani A, Karimi A, Ghazali AH, Ahmadun FL
    Environ Technol, 2010 Apr 1;31(4):347-56.
    PMID: 20450108 DOI: 10.1080/09593330903473861
    The efficiency of advanced oxidation processes (AOPs), enzymatic treatment and combined enzymatic/AOP sequences for the colour remediation of soda and chemimechanical pulp and paper mill effluent was investigated. The results indicated that under all circumstances, the AOP using ultraviolet irradiation (photo-Fenton) was more efficient in the degradation of effluent components in comparison with the dark reaction. It was found that both versatile peroxidase (VP) from Bjerkandera adusta and laccase from Trametes versicolor, as pure enzymes, decolorize the deep brown effluent to a clear light-yellow solution. In addition, it was found that in the laccase treatment, the decolorization rates of both effluents were enhanced in the presence of 2, 2'-azinobis (3-ethylbenzthiazoline-6-sulfonate), while in the case of VP, Mn(+2) decreased the efficiency of the decolorization treatment. The concomitant use of enzymes and AOPs imposes a considerable effect on the colour remediation of effluent samples.
    Matched MeSH terms: Laccase/metabolism; Laccase/chemistry*
  5. Mohidem NA, Mat HB
    Bioresour Technol, 2012 Jun;114:472-7.
    PMID: 22464060 DOI: 10.1016/j.biortech.2012.02.138
    The catalytic activity of free laccase and a novel sol-gel laccase (SOLAC) in ionic liquids and organic solvents was demonstrated by using 2,6-dimethoxyphenol (2,6-DMP) as a substrate. The enhancement of the catalytic activity of the SOLAC was observed and compared to the free laccase in both media. The oxidative biodegradation of o-chlorophenol as a model of phenolic environmental pollutants in organic media shows that the degradation was observed only when using water pre-saturated organic solvents or reverse micelle system. The SOLAC gave higher biodegradation rate in either aqueous or organic solvents, in which the optimum temperature was observed at 40 °C for the reverse micelle system as a reaction medium. All results demonstrated the potential use of the SOLAC for biodegradation of phenolic environmental pollutants in non-conventional media.
    Matched MeSH terms: Laccase/isolation & purification*; Laccase/chemistry*
  6. Rajagopalu D, Show PL, Tan YS, Muniandy S, Sabaratnam V, Ling TC
    J Biosci Bioeng, 2016 Sep;122(3):301-6.
    PMID: 26922478 DOI: 10.1016/j.jbiosc.2016.01.016
    The feasible use of aqueous two-phase systems (ATPSs) to establish a viable protocol for the recovery of laccase from processed Hericium erinaceus (Bull.:Fr.) Pers. fruiting bodies was evaluated. Cold-stored (4.00±1.00°C) H. erinaceus recorded the highest laccase activities of 2.02±0.04 U/mL among all the processed techniques. The evaluation was carried out in twenty-five ATPSs, which composed of polyethylene glycol (PEG) with various molecular weights and potassium phosphate salt solution to purify the protein from H. erinaceus. Optimum recovery condition was observed in the ATPS which contained 17% (w/w) PEG with a molecular weight of 8000 and 12.2% (w/w) potassium phosphate solution, at a volume ratio (VR) of 1.0. The use of ATPS resulted in one-single primary recovery stage process that produced an overall yield of 99% with a purification factor of 8.03±0.46. The molecular mass of laccases purified from the bottom phase was in the range of 55-66 kDa. The purity of the partitioned laccase was confirmed with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
    Matched MeSH terms: Laccase/biosynthesis*; Laccase/isolation & purification*; Laccase/chemistry
  7. Vikineswary S, Abdullah N, Renuvathani M, Sekaran M, Pandey A, Jones EB
    Bioresour Technol, 2006 Jan;97(1):171-7.
    PMID: 15967661
    A comparative study on solid substrate fermentation (SSF) of sago 'hampas', oil palm frond parenchyma tissue (OPFPt) and rubberwood sawdust with Pycnoporus sanguineus for laccase production was carried out. Optimal mycelial growth of Pyc. sanguineus was observed on all the substrates studied over a 21 days time-course fermentation. Laccase productivity was highest during degradation of sago 'hampas' and OPFPt and a range from 7.5 to 7.6 U/g substrate on the 11th day of fermentation compared to degradation of rubberwood sawdust with a maximum laccase productivity of 5.7 U/g substrate on day 11 of SSF. Further optimization of laccase production was done by varying the inoculum age, density and nitrogen supplementation. SSF of OPFPt by Pyc. sanguineus gave maximum productivity of laccase of 46.5 U/g substrate on day 6 of fermentation with a 30% (w/w) of 4 weeks old inoculum and 0.92% nitrogen in the form of urea supplemented in the substrate. The extraction of laccase was also optimized in this study. Recovery of laccase was fourfold higher at 30.6 U/g substrate on day 10 of SSF using unadjusted tap water at pH 8.0 as extraction medium at 25+/-2 degrees C compared to laccase recovery of 7.46 U/g substrate using sodium acetate buffer at pH 4.8 at 4 degrees C. Further optimization showed that laccase recovery was increased by 50% with a value of 46.5 U/g substrate on day 10 of SSF when the extraction medium was tap water adjusted to pH 5.0 at 25+/-2 degrees C.
    Matched MeSH terms: Laccase/biosynthesis*; Laccase/isolation & purification
  8. Phan CW, Sabaratnam V
    Appl Microbiol Biotechnol, 2012 Nov;96(4):863-73.
    PMID: 23053096 DOI: 10.1007/s00253-012-4446-9
    Mushroom industries generate a virtually in-exhaustible supply of a co-product called spent mushroom substrate (SMS). This is the unutilised substrate and the mushroom mycelium left after harvesting of mushrooms. As the mushroom industry is steadily growing, the volume of SMS generated annually is increasing. In recent years, the mushroom industry has faced challenges in storing and disposing the SMS. The obvious solution is to explore new applications of SMS. There has been considerable discussion recently about the potentials of using SMS for production of value-added products. One of them is production of lignocellulosic enzymes such as laccase, xylanase, lignin peroxidase, cellulase and hemicellulase. This paper reviews scientific research and practical applications of SMS as a readily available and cheap source of enzymes for bioremediation, animal feed and energy feedstock.
    Matched MeSH terms: Laccase/metabolism
  9. Noman E, Al-Gheethi AA, Talip BA, Mohamed R, Kassim AH
    J Hazard Mater, 2020 03 15;386:121954.
    PMID: 31884363 DOI: 10.1016/j.jhazmat.2019.121954
    The present study deals with optimizing, producing, characterizing, application and techno- economic analysis of oxidative enzymes [Laccase (Lac), manganese peroxidase (MnP), and lignin peroxidase (LiP)] from Aspergillus iizukae EAN605 in submerged fermentation process using pumpkin peels as a production substrate. The best operating parameters for producing Lac, MnP and LiP (6.15, 2.58 and 127.99 U mg-1 respectively) were recorded with 20 g 100 mL-1 of substrate, 4.6 mL 100 mL-1 of inoculum size at pH 5.5 after 10 days. The crude enzyme exhibited high stability at pH (3-9) and temperatures (20-60 °C). Km (Michaelis-Menten) of Lac, MnP and LiP crude enzyme was 2.25, 1.79 and 0.72 mM respectively. The decolourization of Remazol Brilliant Blue R by the crude enzyme was 84.84 %. The techno-economic analysis was assessed for a production unit with an annual operating time for enzymatic production and application is 7920 h/year and 100 m3 of the capacity. The process would produce 27,000 cm3 of crude enzyme with a price of USD 0.107 per cm3 compared to USD 1 per cm3 of the current commercial enzyme. The findings indicated that pumpkin peels have potential as a production substrate for oxidative enzymes from A. iizukae EAN605 and is economically feasible.
    Matched MeSH terms: Laccase
  10. Mohd Syukri MS, A Rahman R, Mohamad Z, Md Illias R, Nik Mahmood NA, Jaafar NR
    Int J Biol Macromol, 2021 Jan 01;166:876-883.
    PMID: 33144251 DOI: 10.1016/j.ijbiomac.2020.10.244
    Enzyme immobilization has been known to be one of the methods to improve the stability and reusability of enzyme. In this study, a strategy to optimize laccase immobilization on polyethylene terephthalate grafted with maleic anhydride electrospun nanofiber mat (PET-g-MAH ENM) was developed. The development involves the screening and optimization processes of the crucial factors that influence the immobilization yield such as enzyme concentration, pH values, covalent bonding (CV) time, CV temperature, crosslinking (CL) time, CL temperature and glutaraldehyde concentration using two-level factorial design and Box-Behnken design (BBD), respectively. It was found that laccase concentration, pH values and glutaraldehyde concentration play important role in enhancing the immobilization yield of laccase on PET-g-MAH ENM in the screening process. Subsequently, the optimization result showed at 0.28 mg/ml laccase concentration, pH 3 and 0.45% (v/v) glutaraldehyde concentrations gave the highest immobilization yield at 87.64% which was 81.2% increment from the immobilization yield before optimization. Under the optimum condition, the immobilized laccase was able to oxidize 2, 2-azino-bis 3-ethylbenzothiazoline-6- sulfonic acid (ABTS) in a broad range of pH (pH 3-6) and temperature (20- 70 °C). Meanwhile, the kinetic parameters for Km and Vmax were 1.331 mM and 0.041 mM/min, respectively. It was concluded that the optimization of immobilized laccase on PET-g-MAH ENM enhance the performance of this biocatalyst.
    Matched MeSH terms: Laccase/metabolism; Laccase/chemistry*
  11. Noman E, Al-Gheethi A, Mohamed RMSR, Talip BA
    Top Curr Chem (Cham), 2019 May 27;377(3):17.
    PMID: 31134390 DOI: 10.1007/s41061-019-0241-8
    In this article, the utilization of fungi for the degradation of xenobiotic organic compounds (XOCs) from different wastewater and aqueous solutions has been reviewed. The myco-remediation (myco-enzymes, myco-degradation, and myco-sorption) process is widely used to remove XOCs, which are not easily biodegradable. The removal of XOCs from textile wastewaters through chemical and physical processes has been addressed by many researchers. Currently, the application of oxidative enzymes [manganese peroxidase (MnP), lignin peroxidase (LiP), and laccase] and myco-adsorption is becoming more common for the removal of XOCs from wastewater. Although the advanced oxidation process (AOPs) is a preferred technology for removing XOCs, its use is restricted due to its relatively high cost, which led to research studies on non-traditional and low-cost technology. The current review aimed to organize the scattered available information on the potential of myco-remediation for XOC removal. Moreover, the utilization of agricultural wastes as a production substrate for oxidative enzymes has been reported by many authors. Agricultural waste materials are highly inducible for oxidative enzyme production by fungi and are cost-effective in comparison to commercial substances. It is evident from the literature survey of 80 recently published papers that myco-enzymes have demonstrated outstanding XOC removal capabilities. Fungal laccase enzyme is the first step to degrade the lignin and then to get the carbon source form the cellulose by cellulose enzyme.
    Matched MeSH terms: Laccase
  12. Saat MN, Annuar MS, Alias Z, Chuan LT, Chisti Y
    Bioprocess Biosyst Eng, 2014 May;37(5):765-75.
    PMID: 24005762 DOI: 10.1007/s00449-013-1046-8
    Production of extracellular laccase by the white-rot fungus Pycnoporus sanguineus was examined in batch submerged cultures in shake flasks, baffled shake flasks and a stirred tank bioreactor. The biomass growth in the various culture systems closely followed a logistic growth model. The production of laccase followed a Luedeking-Piret model. A modified Luedeking-Piret model incorporating logistic growth effectively described the consumption of glucose. Biomass productivity, enzyme productivity and substrate consumption were enhanced in baffled shake flasks relative to the cases for the conventional shake flasks. This was associated with improved oxygen transfer in the presence of the baffles. The best results were obtained in the stirred tank bioreactor. At 28 °C, pH 4.5, an agitation speed of 600 rpm and a dissolved oxygen concentration of ~25 % of air saturation, the laccase productivity in the bioreactor exceeded 19 U L(-1 )days(-1), or 1.5-fold better than the best case for the baffled shake flask. The final concentration of the enzyme was about 325 U L(-1).
    Matched MeSH terms: Laccase/biosynthesis*
  13. Singh P, Lau CSS, Siah SY, Chua KO, Ting ASY
    Arch Microbiol, 2024 Mar 22;206(4):188.
    PMID: 38519709 DOI: 10.1007/s00203-024-03895-8
    Biodegradation is an eco-friendly measure to address plastic pollution. This study screened four bacterial isolates that were capable of degrading recalcitrant polymers, i.e., low-density polyethylene, polyethylene terephthalate, and polystyrene. The unique bacterial isolates were obtained from plastic polluted environment. Dermacoccus sp. MR5 (accession no. OP592184) and Corynebacterium sp. MR10 (accession no. OP536169) from Malaysian mangroves and Bacillus sp. BS5 (accession no. OP536168) and Priestia sp. TL1 (accession no. OP536170) from a sanitary landfill. The four isolates showed a gradual increase in the microbial count and the production of laccase and esterase enzymes after 4 weeks of incubation with the polymers (independent experiment set). Bacillus sp. BS5 produced the highest laccase 15.35 ± 0.19 U/mL and showed the highest weight loss i.e., 4.84 ± 0.6% for PS. Fourier transform infrared spectroscopy analysis confirmed the formation of carbonyl and hydroxyl groups as a result of oxidation reactions by enzymes. Liquid chromatography-mass spectrometry analysis showed the oxidation of the polymers to small molecules (alcohol, ethers, and acids) assimilated by the microbes during the degradation. Field emission scanning electron microscopy showed bacterial colonization, biofilm formation, and surface erosion on the polymer surface. The result provided significant insight into enzyme activities and the potential of isolates to target more than one type of polymer for degradation.
    Matched MeSH terms: Laccase
  14. Thoa LTK, Thao TTP, Nguyen-Thi ML, Chung ND, Ooi CW, Park SM, et al.
    Chemosphere, 2023 Jun;325:138392.
    PMID: 36921772 DOI: 10.1016/j.chemosphere.2023.138392
    The present study reported the improvement of biological treatment for the removal of recalcitrant dyes including aniline blue, reactive black 5, orange II, and crystal violet in contaminated water. The biodegradation efficiency of Fusarium oxysporum was significantly enhanced by the addition of mediators and by adjusting the biomass density and nutrient composition. A supplementation of 1% glucose in culture medium improved the biodegradation efficiency of aniline blue, reactive black 5, orange II, and crystal violet by 2.24, 1.51, 4.46, and 2.1 folds, respectively. Meanwhile, the addition of mediators to culture medium significantly increased the percentages of total removal for aniline blue, reactive black 5, orange II, and crystal violet, reaching 86.07%, 68.29%, 76.35%, and 95.3%, respectively. Interestingly, the fungal culture supplemented with 1% remazol brilliant blue R boosted the biodegradation up to 97.06%, 89.86%, 91.38%, and 86.67% for aniline blue, reactive black 5, orange II, and crystal violet, respectively. Under optimal culture conditions, the fungal culture could degrade these synthetic dyes concentration up to 104 mg/L. The present study demonstrated that different recalcitrant dye types can be efficiently degraded using microorganism such as F. oxysporum.
    Matched MeSH terms: Laccase/metabolism
  15. Lazim ZM, Hadibarata T
    Braz J Microbiol, 2016 Jul-Sep;47(3):610-6.
    PMID: 27287336 DOI: 10.1016/j.bjm.2016.04.015
    This study aimed to investigate the impact of nonionic surfactants on the efficacy of fluorine degradation by Polyporus sp. S133 in a liquid culture. Fluorene was observed to be degraded in its entirety by Polyporus sp. S133 subsequent to a 23-day incubation period. The fastest cell growth rate was observed in the initial 7 days in the culture that was supplemented with Tween 80. The degradation process was primarily modulated by the activity of two ligninolytic enzymes, laccase and MnP. The highest laccase activity was stimulated by the addition of Tween 80 (2443U/L) followed by mixed surfactant (1766U/L) and Brij 35 (1655U/L). UV-vis spectroscopy, TLC analysis and mass spectrum analysis of samples subsequent to the degradation process in the culture medium confirmed the biotransformation of fluorene. Two metabolites, 9-fluorenol (λmax 270, tR 8.0min and m/z 254) and protocatechuic acid (λmax 260, tR 11.3min and m/z 370), were identified in the treated medium.
    Matched MeSH terms: Laccase
  16. Moin SF, Omar MN
    Protein Pept Lett, 2014;21(8):707-13.
    PMID: 23855667
    Laccases belong to the multicopper binding protein family that catalysis the reduction of oxygen molecule to produce water. These enzymes are glycosylated proteins and have been isolated and purified from fungi, bacteria, plant, insects and lichens. The variety of commercial and industrial application of laccases has attracted much attention towards the research addressing different aspects of the protein characterization, production and fit for purpose molecule. Here we briefly discuss the purification, catalytic mechanism in light of available understanding of structure-function relationship and the tailoring side of the protein, which has been the subject of recent research. Purification strategy of laccases is a method of choice and is facilitated by increased production of the enzyme. The structure-function relationship has given insights to unfold the catalytic mechanism. Site directed mutagenesis and other modification at C-terminal end or surrounding environment of copper centres have shown promising results to fit for purpose aspect, with a lot remains to be explored in glycosylation status and its alteration.
    Matched MeSH terms: Laccase/genetics; Laccase/isolation & purification; Laccase/metabolism*; Laccase/chemistry*
  17. Ramzi AB, Che Me ML, Ruslan US, Baharum SN, Nor Muhammad NA
    PeerJ, 2019;7:e8065.
    PMID: 31879570 DOI: 10.7717/peerj.8065
    Background: G. boninense is a hemibiotrophic fungus that infects oil palms (Elaeis guineensis Jacq.) causing basal stem rot (BSR) disease and consequent massive economic losses to the oil palm industry. The pathogenicity of this white-rot fungus has been associated with cell wall degrading enzymes (CWDEs) released during saprophytic and necrotrophic stage of infection of the oil palm host. However, there is a lack of information available on the essentiality of CWDEs in wood-decaying process and pathogenesis of this oil palm pathogen especially at molecular and genome levels.

    Methods: In this study, comparative genome analysis was carried out using the G. boninense NJ3 genome to identify and characterize carbohydrate-active enzyme (CAZymes) including CWDE in the fungal genome. Augustus pipeline was employed for gene identification in G. boninense NJ3 and the produced protein sequences were analyzed via dbCAN pipeline and PhiBase 4.5 database annotation for CAZymes and plant-host interaction (PHI) gene analysis, respectively. Comparison of CAZymes from G. boninense NJ3 was made against G. lucidum, a well-studied model Ganoderma sp. and five selected pathogenic fungi for CAZymes characterization. Functional annotation of PHI genes was carried out using Web Gene Ontology Annotation Plot (WEGO) and was used for selecting candidate PHI genes related to cell wall degradation of G. boninense NJ3.

    Results: G. boninense was enriched with CAZymes and CWDEs in a similar fashion to G. lucidum that corroborate with the lignocellulolytic abilities of both closely-related fungal strains. The role of polysaccharide and cell wall degrading enzymes in the hemibiotrophic mode of infection of G. boninense was investigated by analyzing the fungal CAZymes with necrotrophic Armillaria solidipes, A. mellea, biotrophic Ustilago maydis, Melampsora larici-populina and hemibiotrophic Moniliophthora perniciosa. Profiles of the selected pathogenic fungi demonstrated that necrotizing pathogens including G. boninense NJ3 exhibited an extensive set of CAZymes as compared to the more CAZymes-limited biotrophic pathogens. Following PHI analysis, several candidate genes including polygalacturonase, endo β-1,3-xylanase, β-glucanase and laccase were identified as potential CWDEs that contribute to the plant host interaction and pathogenesis.

    Discussion: This study employed bioinformatics tools for providing a greater understanding of the biological mechanisms underlying the production of CAZymes in G. boninense NJ3. Identification and profiling of the fungal polysaccharide- and lignocellulosic-degrading enzymes would further facilitate in elucidating the infection mechanisms through the production of CWDEs by G. boninense. Identification of CAZymes and CWDE-related PHI genes in G. boninense would serve as the basis for functional studies of genes associated with the fungal virulence and pathogenicity using systems biology and genetic engineering approaches.

    Matched MeSH terms: Laccase
  18. Gou Z, Ma NL, Zhang W, Lei Z, Su Y, Sun C, et al.
    Environ Res, 2020 09;188:109829.
    PMID: 32798948 DOI: 10.1016/j.envres.2020.109829
    Intensive studies have been performed on the improvement of bioethanol production by transformation of lignocellulose biomass. In this study, the digestibility of corn stover was dramatically improved by using laccase immobilized on Cu2+ modified recyclable magnetite nanoparticles, Fe3O4-NH2. After digestion, the laccase was efficiently separated from slurry. The degradation rate of lignin reached 40.76%, and the subsequent cellulose conversion rate 38.37% for 72 h at 35 °C with cellulase at 50 U g-1 of corn stover. Compared to those of free and inactivated mode, the immobilized laccase pre-treatment increased subsequent cellulose conversion rates by 23.98% and 23.34%, respectively. Moreover, the reusability of immobilized laccase activity remained 50% after 6 cycles. The storage and thermal stability of the fixed laccase enhanced by 70% and 24.1% compared to those of free laccase at 65 °C, pH 4.5, respectively. At pH 10.5, it exhibited 16.3% more activities than its free mode at 35 °C. Our study provides a new avenue for improving the production of bioethanol with immobilized laccase for delignification using corn stover as the starting material.
    Matched MeSH terms: Laccase
  19. Begum SZ, Nizam NSM, Muhamad A, Saiman MI, Crouse KA, Abdul Rahman MB
    PLoS One, 2020;15(11):e0238147.
    PMID: 33147237 DOI: 10.1371/journal.pone.0238147
    Laccases, oxidative copper-enzymes found in fungi and bacteria were used as the basis in the design of nona- and tetrapeptides. Laccases are known to be excellent catalysts for the degradation of phenolic xenobiotic waste. However, since solvent extraction of laccases is environmentally-unfriendly and yields obtained are low, they are less preferred compared to synthetic catalysts. The histidine rich peptides were designed based on the active site of laccase extracted from Trametes versicolor through RCSB Protein Data Bank, LOMETS and PyMol software. The peptides were synthesized using Fmoc-solid phase peptide synthesis (SPPS) with 30-40% yield. These peptides were purified and characterized using LC-MS (purities >75%), FTIR and NMR spectroscopy. Synthesized copper(II)-peptides were crystallized and then analyzed spectroscopically. Their structures were elucidated using 1D and 2D NMR. Standards (o,m,p-cresol, 2,4-dichlorophenol) catalysed using laccase from Trametes versicolor (0.66 U/mg) were screened under different temperatures and stirring rate conditions. After optimizing the degradation of the standards with the best reaction conditions reported herein, medications with phenolic and aromatic structures such as ibuprofen, paracetamol (acetaminophen), salbutamol, erythromycin and insulin were screened using laccase (positive control), apo-peptides and copper-peptides. Their activities evaluated using GC-MS, were compared with those of peptide and copper-peptide catalysts. The tetrapeptide was found to have the higher degradation activity towards salbutamol (96.8%) compared with laccase at 42.8%. Ibuprofen (35.1%), salbutamol (52.9%) and erythromycin (49.7%) were reported to have the highest degradation activities using Cu-tetrapeptide as catalyst when compared with the other medications. Consequently, o-cresol (84%) was oxidized by Tp-Cu while the apo-peptides failed to oxidize the cresols. Copper(II)-peptides were observed to have higher catalytic activity compared to their parent peptides and the enzyme laccase for xenobiotic degradation.
    Matched MeSH terms: Laccase/chemistry*
  20. Masran R, Zanirun Z, Bahrin EK, Ibrahim MF, Lai Yee P, Abd-Aziz S
    Appl Microbiol Biotechnol, 2016 Jun;100(12):5231-46.
    PMID: 27115758 DOI: 10.1007/s00253-016-7545-1
    Abundant lignocellulosic biomass from various industries provides a great potential feedstock for the production of value-added products such as biofuel, animal feed, and paper pulping. However, low yield of sugar obtained from lignocellulosic hydrolysate is usually due to the presence of lignin that acts as a protective barrier for cellulose and thus restricts the accessibility of the enzyme to work on the cellulosic component. This review focuses on the significance of biological pretreatment specifically using ligninolytic enzymes as an alternative method apart from the conventional physical and chemical pretreatment. Different modes of biological pretreatment are discussed in this paper which is based on (i) fungal pretreatment where fungi mycelia colonise and directly attack the substrate by releasing ligninolytic enzymes and (ii) enzymatic pretreatment using ligninolytic enzymes to counter the drawbacks of fungal pretreatment. This review also discusses the important factors of biological pretreatment using ligninolytic enzymes such as nature of the lignocellulosic biomass, pH, temperature, presence of mediator, oxygen, and surfactant during the biodelignification process.
    Matched MeSH terms: Laccase/metabolism
Filters
Contact Us

Please provide feedback to Administrator (afdal@afpm.org.my)

External Links