Displaying publications 1 - 20 of 40 in total

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  1. Productivity of laccase in solid substrate fermentation of selected agro-residues by Pycnoporus sanguineus
    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
  2. Microbial biodegradation of recalcitrant synthetic dyes from textile-enriched wastewater by Fusarium oxysporum
    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
  3. Draft genome sequence of the basidiomycetous fungus Tinctoporellus epimiltinus strain RS1
    Subramaniam R, Siddiquee S, Aguol KA, Hoque MZ, Kumar SV
    Data Brief, 2019 Apr;23:103796.
    PMID: 31372442 DOI: 10.1016/j.dib.2019.103796
    Members of the genus Tinctoporellus, which belong to the wood-degrading basidiomycetes, possess the ability to synthesize an array of industrially potent enzymes and metabolites. Here, we present the draft genome sequence of the species Tinctoporellus epimiltinus strain RS1, which is the first to represent its genus. The genome was sequenced using Illumina's 2 × 150 bp paired-end Nextera protocol. The draft genome assembly was 46.2 Mb in size consisting of 13,791 protein coding genes. Identification of carbohydrate active enzymes and laccases from the data may be useful in order to harness the metabolic potentials of the fungi. The data can be accessed at ENA under the accession number FTLJ00000000.
    Matched MeSH terms: Laccase
  4. Microbial degradation of low-density polyethylene, polyethylene terephthalate, and polystyrene by novel isolates from plastic-polluted environment
    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
  5. Fulltext Decolourisation Capabilities of Ligninolytic Enzymes Produced by Marasmius cladophyllus UMAS MS8 on Remazol Brilliant Blue R and Other Azo Dyes
    Sing NN, Husaini A, Zulkharnain A, Roslan HA
    Biomed Res Int, 2017;2017:1325754.
    PMID: 28168194 DOI: 10.1155/2017/1325754
    Marasmius cladophyllus was examined for its ability to degradatively decolourise the recalcitrant dye Remazol Brilliant Blue R (RBBR) and screened for the production of ligninolytic enzymes using specific substrates. Monitoring dye decolourisation by the decrease in absorbance ratio of A592/A500 shows that the decolourisation of RBBR dye was associated with the dye degradation. Marasmius cladophyllus produces laccase and lignin peroxidase in glucose minimal liquid medium containing RBBR. Both enzyme activities were increased, with laccase activity recorded 70 times higher reaching up to 390 U L-1 on day 12. Further in vitro RBBR dye decolourisation using the culture medium shows that laccase activity was correlated with the dye decolourisation. Fresh RBBR dye continuously supplemented into the decolourised culture medium was further decolourised much faster in the subsequent round of the RBBR dye decolourisation. In vitro dye decolourisation using the crude laccase not only decolourised 76% of RBBR dye in just 19 hours but also decolourised 54% of Orange G and 33% of Congo red at the same period of time without the use of any exogenous mediator. This rapid dye decolourisation ability of the enzymes produced by M. cladophyllus thus suggested its possible application in the bioremediation of dye containing wastewater.
    Matched MeSH terms: Laccase/metabolism*
  6. Fulltext Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes
    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
  7. Modeling of growth and laccase production by Pycnoporus sanguineus
    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*
  8. Fulltext Enzymatic and genetic characterization of lignin depolymerization by Streptomyces sp. S6 isolated from a tropical environment
    Riyadi FA, Tahir AA, Yusof N, Sabri NSA, Noor MJMM, Akhir FNMD, et al.
    Sci Rep, 2020 05 08;10(1):7813.
    PMID: 32385385 DOI: 10.1038/s41598-020-64817-4
    The conversion of lignocellulosic biomass into bioethanol or biochemical products requires a crucial pretreatment process to breakdown the recalcitrant lignin structure. This research focuses on the isolation and characterization of a lignin-degrading bacterial strain from a decaying oil palm empty fruit bunch (OPEFB). The isolated strain, identified as Streptomyces sp. S6, grew in a minimal medium with Kraft lignin (KL) as the sole carbon source. Several known ligninolytic enzyme assays were performed, and lignin peroxidase (LiP), laccase (Lac), dye-decolorizing peroxidase (DyP) and aryl-alcohol oxidase (AAO) activities were detected. A 55.3% reduction in the molecular weight (Mw) of KL was observed after 7 days of incubation with Streptomyces sp. S6 based on gel-permeation chromatography (GPC). Gas chromatography-mass spectrometry (GC-MS) also successfully highlighted the production of lignin-derived aromatic compounds, such as 3-methyl-butanoic acid, guaiacol derivatives, and 4,6-dimethyl-dodecane, after treatment of KL with strain S6. Finally, draft genome analysis of Streptomyces sp. S6 also revealed the presence of strong lignin degradation machinery and identified various candidate genes responsible for lignin depolymerization, as well as for the mineralization of the lower molecular weight compounds, confirming the lignin degradation capability of the bacterial strain.
    Matched MeSH terms: Laccase/genetics
  9. Thermokinetic comparison of trypan blue decolorization by free laccase and fungal biomass
    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*
  10. Fulltext Insight into plant cell wall degradation and pathogenesis of Ganoderma boninense via comparative genome analysis
    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
  11. Recovery of laccase from processed Hericium erinaceus (Bull.:Fr) Pers. fruiting bodies in aqueous two-phase system
    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
  12. Potential uses of spent mushroom substrate and its associated lignocellulosic enzymes
    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
  13. Characterization of white rot fungi from wood decayed for lignin degradation
    Nurul-Aliyaa YA, Awang NA, Mohd MH
    Lett Appl Microbiol, 2023 Oct 04;76(10).
    PMID: 37777838 DOI: 10.1093/lambio/ovad118
    The present study was conducted to isolate and identify white rot fungi (WRF) from wood decayed and to determine their ability to produce lignin-modifying enzymes (LMEs), specifically laccase (Lac), lignin peroxidase (LiP), and manganese peroxidase (MnP), on solid and liquid media supplemented with synthetic dyes namely 2,2'-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), azure B, and phenol red. A total of 23 isolates of WRF were isolated from decayed wood and identified as eight different species namely Phanerochaete australis, Perenniporia tephropora, Lentinus squarrosulus, Ganoderma australe, Trametes polyzona, Lentinus sajor-caju, Gymnopilus dilepis, and Fomitopsis palustris based on morphological characteristics, DNA sequences of the internal transcribed spacer (ITS) region, and phylogenetic inference. The fungal isolates can be divided into four groups based on the type of LMEs produced, namely A (Lac-LiP-MnP) with 16 isolates, B (Lac-MnP) (three isolates), C (Lac) (three isolates), and D (MnP) (one isolate). This study highlights P. australis (BJ38) as the best producer of Lac and LiP, while L. squarrosulus (IPS72) is the best producer of MnP. The present study is the first reported P. australis as an efficient lignin degrader by demonstrating the highest activity of two important LMEs.
    Matched MeSH terms: Laccase/genetics; Laccase/metabolism
  14. Myco-Remediation of Xenobiotic Organic Compounds for a Sustainable Environment: A Critical Review
    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
  15. Oxidative enzymes from newly local strain Aspergillus iizukae EAN605 using pumpkin peels as a production substrate: Optimized production, characterization, application and techno-economic analysis
    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
  16. Fulltext A Review on the Biotechnological Applications of the Operational Group Bacillus amyloliquefaciens
    Ngalimat MS, Yahaya RSR, Baharudin MMA, Yaminudin SM, Karim M, Ahmad SA, et al.
    Microorganisms, 2021 Mar 17;9(3).
    PMID: 33802666 DOI: 10.3390/microorganisms9030614
    Bacteria under the operational group Bacillus amyloliquefaciens (OGBa) are all Gram-positive, endospore-forming, and rod-shaped. Taxonomically, the OGBa belongs to the Bacillus subtilis species complex, family Bacillaceae, class Bacilli, and phylum Firmicutes. To date, the OGBa comprises four bacterial species: Bacillus amyloliquefaciens, Bacillus siamensis, Bacillus velezensis and Bacillus nakamurai. They are widely distributed in various niches including soil, plants, food, and water. A resurgence in genome mining has caused an increased focus on the biotechnological applications of bacterial species belonging to the OGBa. The members of OGBa are known as plant growth-promoting bacteria (PGPB) due to their abilities to fix nitrogen, solubilize phosphate, and produce siderophore and phytohormones, as well as antimicrobial compounds. Moreover, they are also reported to produce various enzymes including α-amylase, protease, lipase, cellulase, xylanase, pectinase, aminotransferase, barnase, peroxidase, and laccase. Antimicrobial compounds that able to inhibit the growth of pathogens including non-ribosomal peptides and polyketides are also produced by these bacteria. Within the OGBa, various B. velezensis strains are promising for use as probiotics for animals and fishes. Genome mining has revealed the potential applications of members of OGBa for removing organophosphorus (OPs) pesticides. Thus, this review focused on the applicability of members of OGBa as plant growth promoters, biocontrol agents, probiotics, bioremediation agents, as well as producers of commercial enzymes and antibiotics. Here, the bioformulations and commercial products available based on these bacteria are also highlighted. This review will better facilitate understandings of members of OGBa and their biotechnological applications.
    Matched MeSH terms: Laccase
  17. Decolorization of palm oil mill effluent using growing cultures of Curvularia clavata
    Neoh CH, Lam CY, Lim CK, Yahya A, Ibrahim Z
    Environ Sci Pollut Res Int, 2014 Mar;21(6):4397-408.
    PMID: 24327114 DOI: 10.1007/s11356-013-2350-1
    Agricultural wastewater that produces color are of environmental and health concern as colored effluent can produce toxic and carcinogenic by-products. From this study, batch culture optimization using response surface methods indicated that the fungus isolated from the pineapple solid waste, Curvularia clavata was able to decolorize sterile palm oil mill effluent (POME) which is mainly associated with polyphenol and lignin. Results showed successful decolorization of POME up to 80 % (initial ADMI [American Dye Manufacturing Index] of 3,793) with 54 % contributed by biosorption and 46 % by biodegradation after 5 days of treatment. Analysis using HPLC and GC-MS showed the degradation of color causing compound such as 3-methoxyphenyl isothiocynate and the production of new metabolites. Ecotoxicity test indicated that the decolorized effluent is safe for discharge. To determine the longevity of the fungus for a prolonged decolorization period, sequential batch decolorization studies were carried out. The results showed that lignin peroxidase and laccase were the main ligninolytic enzymes involved in the degradation of color. Carboxymethyl cellulase (CMCase) and xylanase activities were also detected suggesting possible roles of the enzymes in promoting growth of the fungus which consequently contributed to improved decolorization of POME. In conclusion, the ability of C. clavata in treating color of POME indicated that C. clavata is of potential use for decolorization and degradation of agricultural wastewater containing polyphenolic compounds.
    Matched MeSH terms: Laccase/metabolism
  18. Comprehensive studies on optimization of ligno-hemicellulolytic enzymes by indigenous white rot hymenomycetes under solid-state cultivation using agro-industrial wastes
    Naidu Y, Siddiqui Y, Idris AS
    J Environ Manage, 2020 Apr 01;259:110056.
    PMID: 31929034 DOI: 10.1016/j.jenvman.2019.110056
    The disposal of oil palm biomass is a huge challenge in Malaysian oil palm plantations. The aim of this study was to develop efficient solid-state cultivated (SSC) ligno-hemicellulolytic bio-degrader formulations of indigenous white-rot hymenomycetes (Trametes lactinea FBW and Pycnoporus sanguineus FBR) utilizing oil palm empty fruit bunches (EFB), rubber wood sawdust (SD) and vermiculite (V) either alone or in combination as substrates. Based on significant laccase (849.40 U mg-1 protein), xylanase (42.26 U g-1 protein) and amylase (157.49 U g-1 protein) production, SD+V (T5) and V (T3) were the optimum substrates for SSC of T. lactinea FBW. Whereas, utilizing EFB (T1) substrate for SSC of P. sanguineus FBR enhanced the production of MnP (42.51 U mg-1 protein), LiP (103.20 U mg-1 protein) and CMCase (34.39 U g-1 protein), enzymes. Apparently, this is the first study reporting on the protein profiles by T. lactinea FBW, producing two isoforms of un-purified laccase (~55 and 70 kDa) and MnP (~40 and 60 kDa) and a CMCase band (~60 kDa) during SSC on SD+V (T5) substrate. Interestingly, this is also the first report to document a single isoform of un-purified laccase (~50 kDa), MnP (~45 kDa), CMCase (~60 kDa) and xylanase (~55 kDa) by P. sanguineus FBR during SSC on empty fruit bunches substrate. The computed Principal Component Analysis (PCA) Biplot analysis elucidated the relationship between the solid substrate compositions, the hymenomycete strain, ligno-hemicellulolytic enzyme profiles, and cultivation time. Therefore, it is suggested to use PCA as a tool for multivariate analysis method for comprehensive selection and optimization of ligno-hemicellulolytic enzyme cocktails by the indigenous white rot hymenomycetes. These non-toxic (acute oral toxicity) formulations are safe to be used in field applications to efficiently degrade oil palm trunks and root mass that had been felled, chipped or pulverized under zero burning waste management program. This study could also serve as an alternative method for efficient utilization of agro-industrial waste as substrates for the development of cost-effective bio-degraders formulations for agro-waste management.
    Matched MeSH terms: Laccase
  19. Laccase enzymes: purification, structure to catalysis and tailoring
    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*
  20. The catalytic activity enhancement and biodegradation potential of free laccase and novel sol-gel laccase in non-conventional solvents
    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*
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