Displaying publications 1 - 20 of 181 in total

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  1. Fluorescence studies of selected 2-alkylaminopyrimidines
    Abdullah Z, Tahir NM, Abas MR, Aiyub Z, Low BK
    Molecules, 2004 Jun 30;9(7):520-6.
    PMID: 18007451
    The reactions of 2-chloropyrimidine with methylamine, ethylamine and piperidine gave the corresponding 2-N-methylamino-, 2-N-ethylamino- and 2N- piperidinopyrimidines, respectively. The fluorescence properties of these alkylamino derivatives in chloroform, ethyl acetate, carbon tetrachloride, acetone, ether, ethanol and methanol were studied. All the alkylamino derivatives showed the highest fluorescence intensity in polar protic solvents; thus 2-N-methylaminopyrimidine (highest fluorescence intensity at 377 nm when excited at 282 nm) and 2-N-ethylaminopyrimidine (highest fluorescence intensity at 375 nm, when excited at 286 nm) showed the highest fluorescence in methanol. In ethanol, 2-N-piperidinopyrimidine showed a fluorescence peak at 403 nm when excited at 360 nm and in chloroform it fluoresced at 392 nm when excited at 356 nm.
    Matched MeSH terms: Solvents/chemistry
  2. Structure and dynamics of Candida rugosa lipase: the role of organic solvent
    Tejo BA, Salleh AB, Pleiss J
    J Mol Model, 2004 Dec;10(5-6):358-66.
    PMID: 15597204
    The effect of organic solvent on the structure and dynamics of proteins was investigated by multiple molecular dynamics simulations (1 ns each) of Candida rugosa lipase in water and in carbon tetrachloride. The choice of solvent had only a minor structural effect. For both solvents the open and the closed conformation of the lipase were near to their experimental X-ray structures (C(alpha) rms deviation 1-1.3 A). However, the solvents had a highly specific effect on the flexibility of solvent-exposed side chains: polar side chains were more flexible in water, but less flexible in organic solvent. In contrast, hydrophobic residues were more flexible in organic solvent, but less flexible in water. As a major effect solvent changed the dynamics of the lid, a mobile element involved in activation of the lipase, which fluctuated as a rigid body about its average position. While in water the deviations were about 1.6 A, organic solvent reduced flexibility to 0.9 A. This increase rigidity was caused by two salt bridges (Lys85-Asp284, Lys75-Asp79) and a stable hydrogen bond (Lys75-Asn 292) in organic solvent. Thus, organic solvents stabilize the lid but render the side chains in the hydrophobic substrate-binding site more mobile. [figure: see text]. Superimposition of open (black, PDB entry 1CRL) and closed (gray, PDB entry 1TRH) conformers of C. rugosa lipase. The mobile lid is indicated.
    Matched MeSH terms: Solvents/chemistry*
  3. Physical factors affecting the production of organic solvent-tolerant protease by Pseudomonas aeruginosa strain K
    Rahman RN, Geok LP, Basri M, Salleh AB
    Bioresour Technol, 2005 Mar;96(4):429-36.
    PMID: 15491823
    The physical factors affecting the production of an organic solvent-tolerant protease from Pseudomonas aeruginosa strain K was investigated. Growth and protease production were detected from 37 to 45 degrees C with 37 degrees C being the optimum temperature for P. aeruginosa. Maximum enzyme activity was achieved at static conditions with 4.0% (v/v) inoculum. Shifting the culture from stationary to shaking condition decreased the protease production (6.0-10.0% v/v). Extracellular organic solvent-tolerant protease was detected over a broad pH range from 6.0 to 9.0. However, the highest yield of protease was observed at pH 7.0. Neutral media increased the protease production compared to acidic or alkaline media.
    Matched MeSH terms: Solvents/chemistry*
  4. Solvent accessibility in native and isolated domain environments: general features and implications to interface predictability
    Raih MF, Ahmad S, Zheng R, Mohamed R
    Biophys Chem, 2005 Apr 1;114(1):63-9.
    PMID: 15792862
    A non-redundant database of 4536 structural domains, comprising more than 790,000 residues, has been used for the calculation of their solvent accessibility in the native protein environment and then in the isolated domain environment. Nearly 140,000 (18%) residues showed a change in accessible surface area in the above two conditions. General features of this change under these two circumstances have been pointed out. Propensities of these interfacing amino acid residues have been calculated and their variation for different secondary structure types has been analyzed. Actual amount of surface area lost by different secondary structures is higher in the case of helix and strands compared to coil and other conformations. Overall change in surface area in hydrophobic and uncharged residues is higher than that in charged residues. An attempt has been made to know the predictability of interface residues from sequence environments. This analysis and prediction results have significant implications towards determining interacting residues in proteins and for the prediction of protein-protein, protein-ligand, protein-DNA and similar interactions.
    Matched MeSH terms: Solvents/chemistry*
  5. High-yield purification of an organic solvent-tolerant lipase from Pseudomonas sp. strain S5
    Rahman RN, Baharum SN, Basri M, Salleh AB
    Anal Biochem, 2005 Jun 15;341(2):267-74.
    PMID: 15907872
    An organic solvent-tolerant S5 lipase was purified by affinity chromatography and anion exchange chromatography. The molecular mass of the lipase was estimated to be 60 kDa with 387 purification fold. The optimal temperature and pH were 45 degrees C and 9.0, respectively. The purified lipase was stable at 45 degrees C and pH 6-9. It exhibited the highest stability in the presence of various organic solvents such as n-dodecane, 1-pentanol, and toluene. Ca2+ and Mg2+ stimulated lipase activity, whereas EDTA had no effect on its activity. The S5 lipase exhibited the highest activity in the presence of palm oil as a natural oil and triolein as a synthetic triglyceride. It showed random positional specificity on the thin-layer chromatography.
    Matched MeSH terms: Solvents/chemistry
  6. A novel organic solvent tolerant lipase from Bacillus sphaericus 205y: extracellular expression of a novel OST-lipase gene
    Sulong MR, Abdul Rahman RN, Salleh AB, Basri M
    Protein Expr Purif, 2006 Oct;49(2):190-5.
    PMID: 16769222
    An organic solvent tolerant (OST) lipase gene from Bacillus sphaericus 205y was successfully expressed extracellularly. The expressed lipase was purified using two steps purification; ultrafiltration and hydrophobic interaction chromatography (HIC) to 8-fold purity and 32% recovery. The purified 205y lipase revealed homogeneity on denaturing gel electrophoresis and the molecular mass was at approximately 30 kDa. The optimum pH for the purified 205y lipase was 7.0-8.0 and its stability showed a broad range of pH value between pH 5.0 to 13.0 at 37 degrees C. The purified 205y lipase exhibited an optimum temperature of 55 degrees C. The activity of the purified lipase was stimulated in the presence of Ca2+ and Mg2+. Ethylenediaminetetraacetic acid (EDTA) has no effect on its activity; however inhibition was observed with phenylmethane sulfonoyl fluoride (PMSF) a serine hydrolase inhibitor. Organic solvents such as dimethylsulfoxide (DMSO), methanol, p-xylene and n-decane enhanced the activity. Studies on the effect of oil showed that the lipase was most active in the presence of tricaprin (C10). The lipase exhibited 1,3 positional specificity.
    Matched MeSH terms: Solvents/chemistry
  7. A new organic solvent tolerant protease from Bacillus pumilus 115b
    Rahman RN, Mahamad S, Salleh AB, Basri M
    J Ind Microbiol Biotechnol, 2007 Jul;34(7):509-17.
    PMID: 17492323
    Five out of the nine benzene-toulene-ethylbenzene-xylene (BTEX) tolerant bacteria that demonstrated high protease activity on skim milk agar were isolated. Among them, isolate 115b identified as Bacillus pumilus exhibited the highest protease production. The protease produced was stable in 25% (v/v) benzene and toluene and it was activated 1.7 and 2.5- fold by n-dodecane and n-tetradecane, respectively. The gene encoding the organic solvent tolerant protease was cloned and its nucleotide sequence determined. Sequence analysis revealed an open reading frame (ORF) of 1,149 bp that encoded a polypeptide of 383 amino acid residues. The polypeptide composed of 29 residues of signal peptide, a propeptide of 79 residues and a mature protein of 275 amino acids with a calculated molecular mass of 27,846 Da. This is the only report available to date on organic solvent tolerant protease from B. pumilus.
    Matched MeSH terms: Solvents/chemistry*
  8. Biophenols from agro-industrial wastes
    Jamal P, Alam MZ, Suhani F
    Med J Malaysia, 2008 Jul;63 Suppl A:107-8.
    PMID: 19025008
    Large quantities of agro-based liquid wastes are produced every year and their disposal is often a problem for industries. In light of that, in this study prudent effort was done to screen the agro-industrial wastes - pineapple waste (PAW) and palm oil mill effluent (POME) for valuable biophenols product. Three different solvents; ethanol, acetone and distilled water were screened in order to enhance the process. All experiments were performed using fixed process conditions of solid to solvent ratio, temperatures, time and agitation speed. Effectiveness of extraction process to produce biophenol was based on high amount with more activity. POME was selected as potential source with biophenol content of 125.42 mg/L GAE.
    Matched MeSH terms: Solvents/chemistry
  9. Regio- and stereoselective biomimetic synthesis of oligostilbenoid dimers from resveratrol analogues: influence of the solvent, oxidant, and substitution
    Velu SS, Buniyamin I, Ching LK, Feroz F, Noorbatcha I, Gee LC, et al.
    Chemistry, 2008;14(36):11376-84.
    PMID: 19003831 DOI: 10.1002/chem.200801575
    Oligostilbenoids are polyphenols that are widely distributed in nature with multifaceted biological activities. To achieve biomimetic synthesis of unnatural derivatives, we subjected three resveratrol analogues to oligomerization by means of one-electron oxidants. Upon varying the metal oxidant (AgOAc, CuBr(2), FeCl(3)6 H(2)O, FeCl(3)6 H(2)O/NaI, PbO(2), VOF(3)), the solvent (over the whole range of polarities), and the oxygenated substitution pattern of the starting material, stilbenoid oligomers with totally different carbon skeletons were obtained. Here we propose to explain the determinism of the type of skeleton produced with the aid of hard and soft acid/base concepts in conjunction with the solvating properties of the solvents and the preferred alignment by the effect of pi stacking.
    Matched MeSH terms: Solvents/chemistry*
  10. A glycerol-free process to produce biodiesel by supercritical methyl acetate technology: an optimization study via Response Surface Methodology
    Tan KT, Lee KT, Mohamed AR
    Bioresour Technol, 2010 Feb;101(3):965-9.
    PMID: 19773156 DOI: 10.1016/j.biortech.2009.09.004
    In this study, fatty acid methyl esters (FAME) have been successfully produced from transesterification reaction between triglycerides and methyl acetate, instead of alcohol. In this non-catalytic supercritical methyl acetate (SCMA) technology, triacetin which is a valuable biodiesel additive is produced as side product rather than glycerol, which has lower commercial value. Besides, the properties of the biodiesel (FAME and triacetin) were found to be superior compared to those produced from conventional catalytic reactions (FAME only). In this study, the effects of various important parameters on the yield of biodiesel were optimized by utilizing Response Surface Methodology (RSM) analysis. The mathematical model developed was found to be adequate and statistically accurate to predict the optimum yield of biodiesel. The optimum conditions were found to be 399 degrees C for reaction temperature, 30 mol/mol of methyl acetate to oil molar ratio and reaction time of 59 min to achieve 97.6% biodiesel yield.
    Matched MeSH terms: Solvents/chemistry
  11. Molten globule-triggered inactivation of a thermostable and solvent stable lipase in hydrophilic solvents
    Hamid TH, Rahman RN, Salleh AB, Basri M
    Protein J, 2010 May;29(4):290-7.
    PMID: 20509044 DOI: 10.1007/s10930-010-9251-7
    The use of lipase in hydrophilic solvent is usually hampered by inactivation. The solvent stability of a recombinant solvent stable lipase isolated from thermostable Bacillus sp. strain 42 (Lip 42), in DMSO and methanol were studied at different solvent-water compositions. The enzymatic activities were retained in up to 45% v/v solvent compositions. The near-UV CD spectra indicated that tertiary structures were perturbed at 60% v/v and above. Far-UV CD in methanol indicated the secondary structure in Lip 42 was retained throughout all solvent compositions. Fluorescence studies indicated formations of molten globules in solvent compositions of 60% v/v and above. The enzyme was able to retain its secondary structures in the presence of methanol; however, there was a general reduction in beta-sheet and an increase in alpha-helix contents. The H-bonding arrangements triggered in methanol and DMSO, respectively, caused different forms of tertiary structure perturbations on Lip 42, despite both showing partial denaturation with molten globule formations.
    Matched MeSH terms: Solvents/chemistry
  12. Determination of partition coefficient and analysis of nitrophenols by three-phase liquid-phase microextraction coupled with capillary electrophoresis
    Sanagi MM, Miskam M, Wan Ibrahim WA, Hermawan D, Aboul-Enein HY
    J Sep Sci, 2010 Jul;33(14):2131-9.
    PMID: 20549667 DOI: 10.1002/jssc.201000172
    A three-phase hollow fiber liquid-phase microextraction method coupled with CE was developed and used for the determination of partition coefficients and analysis of selected nitrophenols in water samples. The selected nitrophenols were extracted from 14 mL of aqueous solution (donor solution) with the pH adjusted to pH 3 into an organic phase (1-octanol) immobilized in the pores of the hollow fiber and finally backextracted into 40.0 microL of the acceptor phase (NaOH) at pH 12.0 located inside the lumen of the hollow fiber. The extractions were carried out under the following optimum conditions: donor solution, 0.05 M H(3)PO(4), pH 3.0; organic solvent, 1-octanol; acceptor solution, 40 microL of 0.1 M NaOH, pH 12.0; agitation rate, 1050 rpm; extraction time, 15 min. Under optimized conditions, the calibration curves for the analytes were linear in the range of 0.05-0.30 mg/L with r(2)>0.9900 and LODs were in the range of 0.01-0.04 mg/L with RSDs of 1.25-2.32%. Excellent enrichment factors of up to 398-folds were obtained. It was found that the partition coefficient (K(a/d)) values were high for 2-nitrophenol, 3-nitrophenol, 4-nitrophenol, 2,4-dinitrophenol and 2,6-dinitrophenol and that the individual partition coefficients (K(org/d) and K(a/org)) promoted efficient simultaneous extraction from the donor through the organic phase and further into the acceptor phase. The developed method was successfully applied for the analysis of water samples.
    Matched MeSH terms: Solvents/chemistry
  13. Organic-solvent stability of elastase strain K overexpressed in an Escherichia-Pseudomonas expression system
    Wong CF, Salleh AB, Basri M, Abd Rahman RN
    Biotechnol Appl Biochem, 2010 Sep;57(1):1-7.
    PMID: 20726840 DOI: 10.1042/BA20100224
    The structural gene of elastase strain K (elastase from Pseudomonas aeruginosa strain K), namely HindIII1500PstI, was successfully sequenced to contain 1497 bp. The amino acid sequence, deduced from the nucleotide sequence, revealed that the mature elastase consists of 301 amino acids, with a molecular mass of 33.1 kDa, and contains a conserved motif HEXXH, zinc ligands and residues involved in the catalysis of elastase strain K. The structural gene was successfully cloned to a shuttle vector, pUCP19, and transformed into Escherichia coli strains TOP10, KRX, JM109 and Tuner™ pLacI as well as P. aeruginosa strains PA01 (A.T.C.C. 47085) and S5, with detection of significant protein expression. Overexpression was detected from transformants KRX/pUCP19/HindIII1500PstI of E. coli and PA01/pUCP19/HindIII1500PstI of P. aeruginosa, with increases in elastolytic activity to 13.83- and 5.04-fold respectively relative to their controls. In addition, recombinant elastase strain K showed considerable stability towards numerous organic solvents such as methanol, ethanol, acetone, toluene, undecan-1-ol and n-dodecane, which typically pose a detrimental effect on enzymes; our finding provides further information to support the potential application of the enzyme in synthetic industries, particularly peptide synthesis.
    Matched MeSH terms: Solvents/chemistry
  14. Extraction of Cu(II) from aqueous solutions by vegetable oil-based organic solvents
    Chang SH, Teng TT, Ismail N
    J Hazard Mater, 2010 Sep 15;181(1-3):868-72.
    PMID: 20638965 DOI: 10.1016/j.jhazmat.2010.05.093
    Various types of vegetable oil-based organic solvents (VOS), i.e. vegetable oils (corn, canola, sunflower and soybean oils) with and without extractants (di-2-ethylhexylphosphoric acid (D2EHPA) and tributylphosphate (TBP)), were investigated into their potentiality as greener substitutes for the conventional petroleum-based organic solvents to extract Cu(II) from aqueous solutions. The pH-extraction isotherms of Cu(II) using various vegetable oils loaded with both D2EHPA and TBP were investigated and the percentage extraction (%E) of Cu(II) achieved by different types of VOS was determined. Vegetable oils without extractants and those loaded with TBP alone showed a poor extractability for Cu(II). Vegetable oils loaded with both D2EHPA and TBP were found to be the most effective VOS for Cu(II) extraction and, thus, are potential greener substitutes for the conventional petroleum-based organic solvents.
    Matched MeSH terms: Solvents/chemistry*
  15. Sub/supercritical liquefaction of oil palm fruit press fiber for the production of bio-oil: effect of solvents
    Mazaheri H, Lee KT, Bhatia S, Mohamed AR
    Bioresour Technol, 2010 Oct;101(19):7641-7.
    PMID: 20510608 DOI: 10.1016/j.biortech.2010.04.072
    Thermal decomposition of oil palm fruit press fiber (FPF) with sub/supercritical methanol, ethanol, acetone, and 1,4-dioxane treatments were investigated using a high-pressure autoclave reactor. When FPF was decomposed with methanol, ethanol, and acetone from 483 to 603 K, the highest degree of conversion obtained were 81.5%, 77.8%, and 67.9% while the highest liquid product yield (LP) obtained were 38.0%, 36.9%, and 38.5%, respectively. For the case of 1,4-dioxane, the conversion of FPF increased from 18.30% to 80.00%, while LP yield increased dramatically from 13.30% to 50.90% (consisting of 42.3% bio-oil compounds) when the reaction temperature was increased from 483 to 563 K. However, the conversion of FPF and LP yield decreased to 69.60% and 24.10%, respectively, when the temperature was further increased to 603 K. Comparison between all the solvents, subcritical 1,4-dioxane treatment was found very effective in the degradation of FPF to produce bio-oil component.
    Matched MeSH terms: Solvents/chemistry*
  16. Fulltext Expression of an organic solvent stable lipase from Staphylococcus epidermidis AT2
    Rahman RN, Kamarudin NH, Yunus J, Salleh AB, Basri M
    Int J Mol Sci, 2010;11(9):3195-208.
    PMID: 20957088 DOI: 10.3390/ijms11093195
    An organic solvent tolerant lipase gene from Staphylococcus epidermidis AT2 was successfully cloned and expressed with pTrcHis2 in E. coli TOP10. Sequence analysis revealed an open reading frame (ORF) of 1,933 bp in length which coded for a polypeptide of 643 amino acid residues. The polypeptide comprised of a signal peptide (37 amino acids), pro-peptide and a mature protein of 390 amino acids. Expression of AT2 lipase resulted in an 18-fold increase in activity, upon the induction of 0.6 mM IPTG after a 10 h incubation period. Interestingly, this lipase was stable in various organic solvents (25% (v/v), mainly toluene, octanol, p-xylene and n-hexane). Literature shows that most of the organic solvent stable bacterial lipases were produced by Pseudomonas sp. and Bacillus sp., but very few from Staphylococcus sp. This lipase demonstrates great potential to be employed in various industrial applications.
    Matched MeSH terms: Solvents/chemistry
  17. Anticancer activity of 3-O-acylated betulinic acid derivatives obtained by enzymatic synthesis
    Ahmad FB, Ghaffari Moghaddam M, Basri M, Abdul Rahman MB
    Biosci Biotechnol Biochem, 2010;74(5):1025-9.
    PMID: 20460723
    An easy and efficient strategy to prepare betulinic acid esters with various anhydrides was used by the enzymatic synthesis method. It involves lipase-catalyzed acylation of betulinic acid with anhydrides as acylating agents in organic solvent. Lipase from Candida antarctica immobilized on an acrylic resin (Novozym 435) was employed as a biocatalyst. Several 3-O-acyl-betulinic acid derivatives were successfully obtained by this procedure. The anticancer activity of betulinic acid and its 3-O-acylated derivatives were then evaluated in vitro against human lung carcinoma (A549) and human ovarian (CAOV3) cancer cell lines. 3-O-glutaryl-betulinic acid, 3-O-acetyl-betulinic acid, and 3-O-succinyl-betulinic acid showed IC(50)<10 microg/ml against A549 cancer cell line tested and showed better cytotoxicity than betulinic acid. In an ovarian cancer cell line, all betulinic acid derivatives prepared showed weaker cytotoxicity than betulinic acid.
    Matched MeSH terms: Solvents/chemistry
  18. Comparative studies of products obtained from solvolysis liquefaction of oil palm empty fruit bunch fibres using different solvents
    Fan SP, Zakaria S, Chia CH, Jamaluddin F, Nabihah S, Liew TK, et al.
    Bioresour Technol, 2011 Feb;102(3):3521-6.
    PMID: 21123058 DOI: 10.1016/j.biortech.2010.11.046
    Solvolysis of oil palm empty fruit bunches (EFB) fibres using different solvents (acetone, ethylene glycol (EG), ethanol, water and toluene) were carried out using an autoclave at 275°C for 60 min. The solvent efficiency in term of conversion yield was found to be: EG>water>ethanol>acetone>toluene. The liquid products and residue obtained were analyzed using Fourier transform infrared spectroscopy (FTIR) and gas chromatography/mass selectivity. The obtained results showed that the chemical properties of the oil product were significantly affected by the type of solvent used for the solvolysis process. The higher heating value (HHV) of oil products obtained using ethanol is ∼29.42 MJ/kg, which is the highest among the oil products produced using different solvents. Water, ethanol and toluene yield major phenolic compounds. While EG favors the formation of alcohol compounds and acetone yields ketone and aldehyde compounds.
    Matched MeSH terms: Solvents/chemistry*
  19. Fulltext Crystallization and preliminary X-ray crystallographic analysis of a thermostable organic solvent-tolerant lipase from Bacillus sp. strain 42
    Khusaini MS, Rahman RN, Mohamad Ali MS, Leow TC, Basri M, Salleh AB
    Acta Crystallogr Sect F Struct Biol Cryst Commun, 2011 Mar 01;67(Pt 3):401-3.
    PMID: 21393852 DOI: 10.1107/S1744309111002028
    An organic solvent-tolerant lipase from Bacillus sp. strain 42 was crystallized using the capillary-tube method. The purpose of studying this enzyme was in order to better understand its folding and to characterize its properties in organic solvents. By initially solving its structure in the native state, further studies on protein-solvent interactions could be performed. X-ray data were collected at 2.0 Å resolution using an in-house diffractometer. The estimated crystal dimensions were 0.09×0.19×0.08 mm. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=117.41, b=80.85, c=99.44 Å, β=96.40°.
    Matched MeSH terms: Solvents/chemistry*
  20. Fulltext Gas chromatography-mass spectrometry analysis of various organic extracts of Merremia borneensis from Sabah
    Hossain MA, Shah MD, Sakari M
    Asian Pac J Trop Med, 2011 Aug;4(8):637-41.
    PMID: 21914542 DOI: 10.1016/S1995-7645(11)60162-4
    OBJECTIVE: To analyse the chemical composition of different extracts of Merremia borneensis (M. borneensis) by gas chromatography-mass spectrometry (GC-MS).

    METHODS: The dried leaves powder was extracted with methanol at room temperature by using Soxhlet extractor. Methanol crude extracts of M. borneensis were extrastel with hexane, chloroform, ethyl acetate and butanol.

    RESULTS: Qualitative analyses of various organic crude extracts showed that majority of these are flavonoids, terpeniods, alkaloids and glycosides. Most of the identified compounds by GC-MS are biologically important. Further the M. borneensis leaf possesses certain characteristics that can be ascribed to cultivation on a domestic plantation.

    CONCLUSIONS: The suitable extracts for respective compounds can be chosen on the basis of above GC-MS analysis. All the major compounds from different extracts are biologically active molecules. Thus the identification of a good number of compounds from various extracts M. borneensis might have some ecological significance.

    Matched MeSH terms: Solvents/chemistry
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