Displaying publications 101 - 120 of 223 in total

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  1. Fulltext The Efficacy of Traditional Medicinal Plants in Modulating the Main Protease of SARS-CoV-2 and Cytokine Storm
    Choe J, Har Yong P, Xiang Ng Z
    Chem Biodivers, 2022 Nov;19(11):e202200655.
    PMID: 36125969 DOI: 10.1002/cbdv.202200655
    Selected traditional medicinal plants exhibit therapeutic effects in coronavirus disease (Covid-19) patients. This review aims to identify the phytochemicals from five traditional medicinal plants (Glycyrrhiza glabra, Nigella sativa, Curcuma longa, Tinospora cordifolia and Withania somnifera) with high potential in modulating the main protease (Mpro) activity and cytokine storm in Covid-19 infection. The Mpro binding affinity of 13 plant phytochemicals were in the following order: Withanoside II>withanoside IV>withaferin A>α-hederin>withanoside V>sitoindoside IX>glabridin>liquiritigenin, nigellidine>curcumin>glycyrrhizin>tinocordiside>berberine. Among these phytochemicals, glycyrrhizin, withaferin A, curcumin, nigellidine and cordifolioside A suppressed SARS-CoV-2 replication and showed stronger anti-inflammatory activities than standard Covid-19 drugs. Both preclinical and clinical evidences supported the development of plant bioactive compounds as Mpro inhibitors.
    Matched MeSH terms: Peptide Hydrolases
  2. Fulltext Protease-targeting peptide-functionalized porous silicon nanoparticles for cancer fluorescence imaging
    Kanathasan JS, Palanisamy UD, Radhakrishnan AK, Chakravarthi S, Thong TB, Swamy V
    Nanomedicine (Lond), 2022 Sep;17(21):1511-1528.
    PMID: 36382634 DOI: 10.2217/nnm-2022-0017
    Background: Porous silicon (pSi) nanoparticles (NPs) functionalized with suitable targeting ligands are now established cancer bioimaging agents and drug-delivery platforms. With growing interest in peptides as tumor-targeting ligands, much work has focused on the use of various peptides in combination with pSi NPs for cancer theranostics. Here, the authors investigated the targeting potential of pSi NPs functionalized with two types of peptide, a linear 10-mer peptide and its branched (Y-shaped) equivalent, that respond to legumain activity in tumor cells. Results: In vitro experiments established that the linear peptide-pSi NP conjugate had better aqueous stability under tumor conditions and higher binding efficiency (p  0.05) of linear peptide-conjugated pSi NPs in the tumor site within 4 h compared with nonconjugated pSi NPs. These results suggest that the linear peptide-pSi NP formulation is a nontoxic, stable and efficient fluorescence bioimaging agent and potential drug-delivery platform.
    Matched MeSH terms: Peptide Hydrolases
  3. Immobilization of cross-linked tannase enzyme on multiwalled carbon nanotubes and its catalytic behavior
    Ong CB, Annuar MSM
    Prep Biochem Biotechnol, 2018 Feb 07;48(2):181-187.
    PMID: 29341838 DOI: 10.1080/10826068.2018.1425707
    Immobilization of cross-linked tannase on pristine multiwalled carbon nanotubes (MWCNT) was successfully performed. Cross-linking of tannase molecules was made through glutaraldehyde. The immobilized tannase exhibited significantly improved pH, thermal, and recycling stability. The optimal pH for both free and immobilized tannase was observed at pH 5.0 with optimal operating temperature at 30°C. Moreover, immobilized enzyme retained greater biocatalytic activities upon 10 repeated uses compared to free enzyme in solution. Immobilization of tannase was accomplished by strong hydrophobic interaction most likely between hydrophobic amino acid moieties of the glutaraldehyde-cross-linked tannase to the MWCNT.
    Matched MeSH terms: Carboxylic Ester Hydrolases/chemistry*
  4. Fulltext Assessment of fragile histidine triad expression in ameloblastoma, odontogenic keratocyst and dentigerous cyst
    Haragannavar VC, Tegginamani AS, Raju S, Kudva S, Peter CD, Shruthi DK
    Indian J Pathol Microbiol, 2019 2 2;62(1):3-6.
    PMID: 30706851 DOI: 10.4103/IJPM.IJPM_403_18
    Background: FHIT (Fragile histidine triad) a member of tumor suppressor family, has been extensively studied in many solid tumors including head and neck squamous cell carcinoma. Among all head and neck cyst and tumors odontogenic lesions account approximately 3%-9%. The molecular pathogenesis of these lesions is less explored. Defects in cell cycle regulators and tumor suppressor genes could result in the development of odontogenic cyst and tumors. Hence, we aimed to determine the significant role of a tumor suppressor gene FHIT in most commonly occurring odontogenic lesions mainly ameloblastoma, odontogenic keratocyst and dentigerous cyst.

    Subjects and Methods: Immunohistochemical analysis of FHIT was done in ameloblastoma, odontogenic keratocyst, dentigerous cyst and dental follicle. Interpretation of the stained slides were done using standard scoring criteria by two pathologist. The results were subjected for statistical analysis.

    Results: Expression of FHIT varied among the groups, with highest negative expression in ameloblastoma 44.4% followed by odontogenic keratocyst 14% and 100%positive expression was seen in dentigerous cyst. The expression levels between the groups were statistically insignificant.

    Conclusion: The varied expression or negative expression of FHIT could be considered as an indicator for aggressive behavior and transformation of preneoplastic/cystic epithelium.

    Matched MeSH terms: Acid Anhydride Hydrolases/genetics*
  5. The mechanistic role of active site residues in non-stereo haloacid dehalogenase E (DehE)
    Zainal Abidin MH, Abd Halim KB, Huyop F, Tengku Abdul Hamid TH, Abdul Wahab R, Abdul Hamid AA
    J Mol Graph Model, 2019 07;90:219-225.
    PMID: 31103914 DOI: 10.1016/j.jmgm.2019.05.003
    Dehalogenase E (DehE) is a non-stereospecific enzyme produced by the soil bacterium, Rhizobium sp. RC1. Till now, the catalytic mechanism of DehE remains unclear although several literature concerning its structure and function are available. Since DehE is non-stereospecific, the enzyme was hypothesized to follow a 'direct attack mechanism' for the catalytic breakdown of a haloacid. For a molecular insight, the DehE modelled structure was docked in silico with the substrate 2-chloropropionic acid (2CP) in the active site. The ideal position of DehE residues that allowed a direct attack mechanism was then assessed via molecular dynamics (MD) simulation. It was revealed that the essential catalytic water was hydrogen bonded to the 'water-bearer', Asn114, at a relatively constant distance of ∼2.0 Å after 50 ns. The same water molecule was also closely sited to the catalytic Asp189 at an average distance of ∼2.0 Å, signifying the imperative role of the latter to initiate proton abstraction for water activation. This reaction was crucial to promote a direct attack on the α-carbon of 2CP to eject the halide ion. The water molecule was oriented favourably towards the α-carbon of 2CP at an angle of ∼75°, mirrored by the formation of stable enzyme-substrate orientations throughout the simulation. The data therefore substantiated that the degradation of a haloacid by DehE followed a 'direct attack mechanism'. Hence, this study offers valuable information into future advancements in the engineering of haloacid dehalogenases with improved activity and selectivity, as well as functionality in solvents other than water.
    Matched MeSH terms: Hydrolases/metabolism*
  6. Pathology and Host Immune Evasion During Human Leptospirosis: a Review
    Chin VK, Basir R, Nordin SA, Abdullah M, Sekawi Z
    Int Microbiol, 2020 May;23(2):127-136.
    PMID: 30875033 DOI: 10.1007/s10123-019-00067-3
    Human leptospirosis is considered as one of the most widespread and potentially fatal zoonotic diseases that causes high mortality and morbidity in the endemic regions of tropical and subtropical countries. The infection can arise from direct or indirect exposure of human through contaminated environment that contains leptospires or animal reservoirs that carry leptospires. The clinical manifestations during human leptospirosis ranges from asymptomatic, mild infections to severe and life-threatening complications involving multi-organ failures with kidneys, lungs and liver severely affected. Despite much efforts have been put in to unravel the pathogenesis during human leptospirosis, it remains obscure to which extent the host factors or the pathogen itself contribute towards the pathogenesis. Host innate immunity, especially, polymorphonuclear neutrophils and complement system are involved in the first line of defense during human leptospirosis. However, pathogenic Leptospira has acquired diverse evasion strategies to evade from host immunity and establish infection in infected hosts. Hence, in this review, we focus on organs pathology during human leptospiral infection and host evasion strategies employed by Leptospira. A profound understanding on leptospiral immunity and how Leptospira subvert the immune system may provide new insights on the development of therapeutic regimens against this species in future.
    Matched MeSH terms: Peptide Hydrolases/metabolism
  7. A porous-cross linked enzyme aggregates of maltogenic amylase from Bacillus lehensis G1: Robust biocatalyst with improved stability and substrate diffusion
    Nawawi NN, Hashim Z, Manas NHA, Azelee NIW, Illias RM
    Int J Biol Macromol, 2020 Apr 01;148:1222-1231.
    PMID: 31759025 DOI: 10.1016/j.ijbiomac.2019.10.101
    Enzymatic synthesis of maltooligosaccharides is hampered due to lack of stability of soluble enzyme. This limitation can be tackled by cross linked enzyme aggregates (CLEAs) immobilization approach. However, substrate diffusion is a major bottleneck in cross linking technology. Herein, CLEAs of maltogenic amylase from Bacillus lehensis G1 (Mag1) was developed with addition of porous agent (Mag1-p-CLEAs). Comparison of thermal, pH and kinetic analysis with CLEAs without porous agent (Mag1-CLEAs) and free Mag1 was performed. Mag1-p-CLEAs with porous structure prepared at 0.8% (w/v) of citrus pectin (porous agent), 0.25% (w/v) of chitosan (cross linker) and cross linked for 1.5 h yielded 91.20% activity. 80% of activity is retained after 30 min of incubation at 40 °C and showed longer half-life than free Mag1 and Mag1-CLEAs. Mag1-p-CLEAs also showed pH stability at acidic and alkaline pH. The 1.68-fold increase in Vmax value in comparison to Mag1-CLEAs showed that the presence of pores of Mag1-p-CLEAs enhanced the beta-cyclodextrin accessibility. The increase in high catalytic efficiency (Kcat/Km) value, 1.90-fold and 1.05-fold showed that it also has better catalytic efficiency than free Mag1 and Mag1-CLEAs, respectively. Mag1-p-CLEAs not only improved substrate diffusibility of CLEAs, but also leads to higher thermal and pH stability of Mag1.
    Matched MeSH terms: Glycoside Hydrolases/chemistry*
  8. Fulltext Effective refolding of a cysteine rich glycoside hydrolase family 19 recombinant chitinase from Streptomyces griseus by reverse dilution and affinity chromatography
    Oyeleye AO, Mohd Yusoff SF, Abd Rahim IN, Leow ATC, Saidi NB, Normi YM
    PLoS One, 2020;15(10):e0241074.
    PMID: 33091044 DOI: 10.1371/journal.pone.0241074
    Conventional refolding methods are associated with low yields due to misfolding and high aggregation rates or very dilute proteins. In this study, we describe the optimization of the conventional methods of reverse dilution and affinity chromatography for obtaining high yields of a cysteine rich recombinant glycoside hydrolase family 19 chitinase from Streptomyces griseus HUT6037 (SgChiC). SgChiC is a potential biocontrol agent and a reference enzyme in the study and development of chitinases for various applications. The overexpression of SgChiC was previously achieved by periplasmic localization from where it was extracted by osmotic shock and then purified by hydroxyapatite column chromatography. In the present study, the successful refolding and recovery of recombinant SgChiC (r-SgChiC) from inclusion bodies (IB) by reverse dilution and column chromatography methods is respectively described. Approximately 8 mg of r-SgChiC was obtained from each method with specific activities of 28 and 52 U/mg respectively. These yields are comparable to that obtained from a 1 L culture volume of the same protein isolated from the periplasmic space of E. coli BL21 (DE3) as described in previous studies. The higher yields obtained are attributed to the successful suppression of aggregation by a stepwise reduction of denaturant from high, to intermediate, and finally to low concentrations. These methods are straight forward, requiring the use of fewer refolding agents compared with previously described refolding methods. They can be applied to the refolding of other cysteine rich proteins expressed as inclusion bodies to obtain high yields of actively folded proteins. This is the first report on the recovery of actively folded SgChiC from inclusion bodies.
    Matched MeSH terms: Glycoside Hydrolases/chemistry*
  9. The applicability of using a protease extracted from cashew fruits (Anacardium occidentale), as possible meat tenderizer: An experimental design approach
    Ahmad MN, Shuhaimen MS, Normaya E, Omar MN, Iqbal A, Ku Bulat KH
    J Texture Stud, 2020 10;51(5):810-829.
    PMID: 32401337 DOI: 10.1111/jtxs.12529
    Meat tenderness is one of the most important organoleptic properties in determining consumer acceptance in meat product marketability. Therefore, an effective meat tenderization method is sought after by exploring plant-derived proteolytic enzymes as meat tenderizer. In this study, a novel protease from Cashew was identified as a new alternative halal meat tenderizer. The extraction of cashew protease was optimized using response surface methodology (R2 = 0.9803) by varying pH, CaCl2 concentration, mixing time, and mass. pH 6.34, 7.92 mM CaCl2 concentration, 5.51 min mixing time, and 19.24 g sample mass were the optimal extraction conditions. There was no significant difference (n = 3; p 
    Matched MeSH terms: Peptide Hydrolases/analysis*
  10. Insecticide toxicity, glutathione transferases and carboxylesterase activities in the larva of the Aedes mosquito
    Shamaan NA, Hamidah R, Jeffries J, Hashim AJ, Wan Ngah WZ
    Comp Biochem Physiol C Comp Pharmacol Toxicol, 1993 Jan;104(1):107-10.
    PMID: 8097444
    1. Toxicity evaluations of DDT, lindane, abate and carbaryl were carried out in the larvae of two wild Aedes aegypti strains from Kuala Lumpur and Klang. The Kuala Lumpur strain was more susceptible to the insecticides than the Klang strain. 2. The lethal toxicity time was also determined. The insecticides were found to take a longer time to exert their effect in the Klang strain as compared to the Kuala Lumpur strain. 3. Carboxylesterase activity was determined to be higher in the Kuala Lumpur strain, but glutathione transferase activities were higher in the Klang strain.
    Matched MeSH terms: Carboxylic Ester Hydrolases/metabolism*
  11. The activation of chick alkaline phosphatase by calmodulin
    Sivanaesan L, Kwan TK, Perumal R
    Biochem. Int., 1991 Oct;25(3):561-70.
    PMID: 1666829
    Calmodulin, an activator protein in most calcium-dependent processes, was isolated to apparent homogeneity from the femurs of 1-day old chicks using phenyl-Sepharose and high performance liquid chromatography. The purified calmodulin was found to produce a 6-fold increase in the activity of alkaline phosphatase isolated from the same source. A Ca2+ concentration of 10(-5) M was required for the activation. Purification of alkaline phosphatase involved acetone precipitation, DEAE-Sephacel and Sephadex G-200 column chromatography. The enzyme was purified to 540-fold and had a specific activity of 10.75 U/mg protein.
    Matched MeSH terms: Phosphoric Diester Hydrolases/metabolism
  12. Genetic markers in a Malaysian population: variants of uridine monophosphate kinase (UMPK), phosphoglycolate phosphatase (PGP) and pancreatic amylase (AMY2)
    Zarinah KH, Abdullah F, Tan SG
    Ann Hum Biol, 1984 11 1;11(6):533-6.
    PMID: 6084457
    Three genetic markers, red-cell UMPK, PGP and serum AMY2 were investigated in Malaysians of Malay, Chinese and Indian ancestries using starch-gel and agarose-gel electrophoresis. UMPK was found to be polymorphic in all three races. Variants were observed for PGP in Malays; in Indians it is a polymorphic marker whereas it is monomorphic in Chinese. AMY2 was polymorphic only in Indians. The UMPK1 frequencies in Malays, Chinese and Indians, respectively, are 0.851, 0.880 and 0.942. The PGP1 frequencies are 0.991, 1.000, 0.962, and the AMY1(2) frequencies are 1.000, 1.000 and 0.983.
    Matched MeSH terms: Phosphoric Monoester Hydrolases/genetics*
  13. 5'-Nucleotide phosphodiesterase isozyme-V in health, in cancer, and in viral hepatitis
    Lei-Injo LE, Tsou KC, Lo KW, Lopez CG, Balasegaram M, Ganesan S
    Cancer, 1980 Feb 15;45(4):795-8.
    PMID: 6244075
    An abnormal, fast-moving 5'-nucleotide phosphodiesterase isozyme was found in 90.0% of 20 Malaysian patients with primary hepatoma and in 23.5% of 391 Malaysian patients with various malignant diseases; it was also discovered in 42.9% of 14 Malaysian and American patients with clinically active hepatitis B infection; in 16.7% of 18 healthy American blood bank donors who were positive for hepatitis B surface antigen (HBsAg); in 13.9% of 287 healthy Malaysian blood bank donors, some positive for HBsAg; and in none of 160 healthy American donors who were negative for HBsAg. A correlation of this abnormal isozyme with hepatoma and with infectious hepatitis B is clearly evident.
    Matched MeSH terms: Phosphoric Diester Hydrolases/blood*
  14. Biochemical genetic markers in the Kadazans of Sabah, Malaysia
    Tan SG, Teng YS, Ganesan J, Lau KY, Lie-Injo LE
    Hum Genet, 1979 Jul 18;49(3):349-53.
    PMID: 289626
    Kadazans, the largest indigenous group in Sabah, northern Borneo, were surveyed for glyoxalase I, phosphoglucomutase I, red cell acid phosphatase, esterase D, adenosine deaminase, soluble glutamate pyruvate transaminase, soluble glutamate oxaloacetate transaminase, 6-phosphogluconate dehydrogenase, uridine monophosphate kinase, adenylate kinase, peptidase B and D, superoxide dismutase, C5, group specific component, haptoglobin and transferrin. Kadazans were found to be polymorphic for GLO I, PGM I, RCAP, esterase D, ADA, s-Gpt, 6PGD, UMPK, Gc, C5, haptoglobin and peptidase B. Rare variants were found for transferrin and peptidase D. No variant was found for s-Got, SOD and AK.
    Matched MeSH terms: Peptide Hydrolases/genetics
  15. Multi-template homology-based structural model of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1
    Adamu A, Shamsir MS, Wahab RA, Parvizpour S, Huyop F
    J Biomol Struct Dyn, 2017 Nov;35(15):3285-3296.
    PMID: 27800712 DOI: 10.1080/07391102.2016.1254115
    Dehalogenases are of high interest due to their potential applications in bioremediation and in synthesis of various industrial products. DehL is an L-2-haloacid dehalogenase (EC 3.8.1.2) that catalyses the cleavage of halide ion from L-2-halocarboxylic acid to produce D-2-hydroxycarboxylic acid. Although DehL utilises the same substrates as the other L-2-haloacid dehalogenases, its deduced amino acid sequence is substantially different (<25%) from those of the rest L-2-haloacid dehalogenases. To date, the 3D structure of DehL is not available. This limits the detailed understanding of the enzyme's reaction mechanism. The present work predicted the first homology-based model of DehL and defined its active site. The monomeric unit of the DehL constitutes α/β structure that is organised into two distinct structural domains: main and subdomains. Despite the sequence disparity between the DehL and other L-2-haloacid dehalogenases, its structural model share similar fold as the experimentally solved L-DEX and DehlB structures. The findings of the present work will play a crucial role in elucidating the molecular details of the DehL functional mechanism.
    Matched MeSH terms: Hydrolases/chemistry*
  16. Transcriptomic and Proteomic Analyses of Nepenthes ampullaria and Nepenthes rafflesiana Reveal Parental Molecular Expression in the Pitchers of Their Hybrid, Nepenthes × hookeriana
    Zulkapli MM, Ab Ghani NS, Ting TY, Aizat WM, Goh HH
    Front Plant Sci, 2020;11:625507.
    PMID: 33552113 DOI: 10.3389/fpls.2020.625507
    Nepenthes is a genus comprising carnivorous tropical pitcher plants that have evolved trapping organs at the tip of their leaves for nutrient acquisition from insect trapping. Recent studies have applied proteomics approaches to identify proteins in the pitcher fluids for better understanding the carnivory mechanism, but protein identification is hindered by limited species-specific transcriptomes for Nepenthes. In this study, the proteomics informed by transcriptomics (PIT) approach was utilized to identify and compare proteins in the pitcher fluids of Nepenthes ampullaria, Nepenthes rafflesiana, and their hybrid Nepenthes × hookeriana through PacBio isoform sequencing (Iso-Seq) and liquid chromatography-mass spectrometry (LC-MS) proteomic profiling. We generated full-length transcriptomes from all three species of 80,791 consensus isoforms with an average length of 1,692 bp as a reference for protein identification. The comparative analysis found that transcripts and proteins identified in the hybrid N. × hookeriana were more resembling N. rafflesiana, both of which are insectivorous compared with omnivorous N. ampullaria that can derive nutrients from leaf litters. Previously reported hydrolytic proteins were detected, including proteases, glucanases, chitinases, phosphatases, nucleases, peroxidases, lipid transfer protein, thaumatin-like protein, pathogenesis-related protein, and disease resistance proteins. Many new proteins with diverse predicted functions were also identified, such as amylase, invertase, catalase, kinases, ligases, synthases, esterases, transferases, transporters, and transcription factors. Despite the discovery of a few unique enzymes in N. ampullaria, we found no strong evidence of adaptive evolution to produce endogenous enzymes for the breakdown of leaf litter. A more complete picture of digestive fluid protein composition in this study provides important insights on the molecular physiology of pitchers and carnivory mechanism of Nepenthes species with distinct dietary habits.
    Matched MeSH terms: Peptide Hydrolases; Phosphoric Monoester Hydrolases
  17. Optimization of protease extraction from horse mango (Mangifera foetida Lour) kernels by a response surface methodology
    Ahmad MN, Liew SL, Yarmo MA, Said M
    Biosci Biotechnol Biochem, 2012;76(8):1438-44.
    PMID: 22878182
    Protease is one of the most important industrial enzymes with a multitude of applications in both food and non-food sectors. Although most commercial proteases are microbial proteases, the potential of non-conventional protease sources, especially plants, should not be overlooked. In this study, horse mango (Mangifera foetida Lour) fruit, known to produce latex with a blistering effect upon contact with human skin, was chosen as a source of protease, and the effect of the extraction process on its protease activity evaluated. The crude enzyme was extracted from the kernels and extraction was optimized by a response surface methodology (RSM) using a central composite rotatable design (CCRD). The variables studied were pH (x(1)), CaCl(2) (x(2)), Triton X-100 (x(3)), and 1,4-dithryeitol (x(4)). The results obtained indicate that the quadratic model is significant for all the variables tested. Based on the RSM model generated, optimal extraction conditions were obtained at pH 6.0, 8.16 mM CaCl(2), 5.0% Triton X-100, and 10.0 mM DTT, and the estimated response was 95.5% (w/w). Verification test results showed that the difference between the calculated and the experimental protease activity value was only 2%. Based on the t-value, the effects of the variables arranged in ascending order of strength were CaCl(2) < pH < DTT < Triton X-100.
    Matched MeSH terms: Peptide Hydrolases/isolation & purification*
  18. Potential of chicken by-products as sources of useful biological resources
    Lasekan A, Abu Bakar F, Hashim D
    Waste Manag, 2013 Mar;33(3):552-65.
    PMID: 22985619 DOI: 10.1016/j.wasman.2012.08.001
    By-products from different animal sources are currently being utilised for beneficial purposes. Chicken processing plants all over the world generate large amount of solid by-products in form of heads, legs, bones, viscera and feather. These wastes are often processed into livestock feed, fertilizers and pet foods or totally discarded. Inappropriate disposal of these wastes causes environmental pollution, diseases and loss of useful biological resources like protein, enzymes and lipids. Utilisation methods that make use of these biological components for producing value added products rather than the direct use of the actual waste material might be another viable option for dealing with these wastes. This line of thought has consequently led to researches on these wastes as sources of protein hydrolysates, enzymes and polyunsaturated fatty acids. Due to the multi-applications of protein hydrolysates in various branches of science and industry, and the large body of literature reporting the conversion of animal wastes to hydrolysates, a large section of this review was devoted to this subject. Thus, this review reports the known functional and bioactive properties of hydrolysates derived from chicken by-products as well their utilisation as source of peptone in microbiological media. Methods of producing these hydrolysates including their microbiological safety are discussed. Based on the few references available in the literature, the potential of some chicken by-product as sources of proteases and polyunsaturated fatty acids are pointed out along with some other future applications.
    Matched MeSH terms: Peptide Hydrolases/isolation & purification
  19. Fulltext Labrenzia sp. BM1: a quorum quenching bacterium that degrades N-acyl homoserine lactones via lactonase activity
    Ghani NA, Norizan SN, Chan XY, Yin WF, Chan KG
    Sensors (Basel), 2014;14(7):11760-9.
    PMID: 24995373 DOI: 10.3390/s140711760
    We report the degradation of quorum sensing N-acylhomoserine lactone molecules by a bacterium isolated from a Malaysian marine water sample. MALDI-TOF and phylogenetic analysis indicated this isolate BM1 clustered closely to Labrenzia sp. The quorum quenching activity of this isolate was confirmed by using a series of bioassays and rapid resolution liquid chromatography analysis. Labrenzia sp. degraded a wide range of N-acylhomoserine lactones namely N-(3-hexanoyl)-L-homoserine lactone (C6-HSL), N-(3-oxohexanoyl)-L-homoserine lactone (3-oxo-C6-HSL) and N-(3-hydroxyhexanoyl)-L-homoserine lactone (3-hydroxy-C6-HSL). Re-lactonisation bioassays confirmed Labrenzia sp. BM1 degraded these signalling molecules efficiently via lactonase activity. To the best of our knowledge, this is the first documentation of a Labrenzia sp. capable of degrading N-acylhomoserine lactones and confirmation of its lactonase-based mechanism of action.
    Matched MeSH terms: Carboxylic Ester Hydrolases/metabolism*
  20. Fulltext Rhodotorula mucilaginosa, a quorum quenching yeast exhibiting lactonase activity isolated from a tropical shoreline
    Ghani NA, Sulaiman J, Ismail Z, Chan XY, Yin WF, Chan KG
    Sensors (Basel), 2014;14(4):6463-73.
    PMID: 24721765 DOI: 10.3390/s140406463
    Two microbial isolates from a Malaysian shoreline were found to be capable of degrading N-acylhomoserine lactones. Both Matrix Assisted Laser Desorption Ionization-Time of Flight-Mass Spectrometry and 18S rDNA phylogenetic analyses confirmed that these isolates are Rhodotorula mucilaginosa. Quorum quenching activities were detected by a series of bioassays and rapid resolution liquid chromatography analysis. The isolates were able to degrade various quorum sensing molecules namely N-hexanoyl-L-homoserine lactone (C6-HSL), N-(3-oxo-hexanoyl)-L-homoserine lactone (3-oxo-C6-HSL) and N-(3-hydroxyhexanoyl)-L-homoserine lactone (3-hydroxy-C6-HSL). Using a relactonisation assay to verify the quorum quenching mechanism, it is confirmed that Rh. mucilaginosa degrades the quorum sensing molecules via lactonase activity. To the best of our knowledge, this is the first documentation of the fact that Rh. mucilaginosa has activity against a broad range of AHLs namely C6-HSL, 3-oxo-C6-HSL and 3-hydroxy-C6-HSL.
    Matched MeSH terms: Carboxylic Ester Hydrolases/metabolism*
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