Displaying publications 21 - 40 of 61 in total

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  1. Fulltext Novel NAD+-Farnesal Dehydrogenase from Polygonum minus Leaves. Purification and Characterization of Enzyme in Juvenile Hormone III Biosynthetic Pathway in Plant
    Seman-Kamarulzaman AF, Mohamed-Hussein ZA, Ng CL, Hassan M
    PLoS One, 2016;11(8):e0161707.
    PMID: 27560927 DOI: 10.1371/journal.pone.0161707
    Juvenile Hormone III is of great concern due to negative effects on major developmental and reproductive maturation in insect pests. Thus, the elucidation of enzymes involved JH III biosynthetic pathway has become increasing important in recent years. One of the enzymes in the JH III biosynthetic pathway that remains to be isolated and characterized is farnesal dehydrogenase, an enzyme responsible to catalyze the oxidation of farnesal into farnesoic acid. A novel NAD+-farnesal dehydrogenase of Polygonum minus was purified (315-fold) to apparent homogeneity in five chromatographic steps. The purification procedures included Gigacap S-Toyopearl 650M, Gigacap Q-Toyopearl 650M, and AF-Blue Toyopearl 650ML, followed by TSK Gel G3000SW chromatographies. The enzyme, with isoelectric point of 6.6 is a monomeric enzyme with a molecular mass of 70 kDa. The enzyme was relatively active at 40°C, but was rapidly inactivated above 45°C. The optimal temperature and pH of the enzyme were found to be 35°C and 9.5, respectively. The enzyme activity was inhibited by sulfhydryl agent, chelating agent, and metal ion. The enzyme was highly specific for farnesal and NAD+. Other terpene aldehydes such as trans- cinnamaldehyde, citral and α- methyl cinnamaldehyde were also oxidized but in lower activity. The Km values for farnesal, citral, trans- cinnamaldehyde, α- methyl cinnamaldehyde and NAD+ were 0.13, 0.69, 0.86, 1.28 and 0.31 mM, respectively. The putative P. minus farnesal dehydrogenase that's highly specific towards farnesal but not to aliphatic aldehydes substrates suggested that the enzyme is significantly different from other aldehyde dehydrogenases that have been reported. The MALDI-TOF/TOF-MS/MS spectrometry further identified two peptides that share similarity to those of previously reported aldehyde dehydrogenases. In conclusion, the P. minus farnesal dehydrogenase may represent a novel plant farnesal dehydrogenase that exhibits distinctive substrate specificity towards farnesal. Thus, it was suggested that this novel enzyme may be functioning specifically to oxidize farnesal in the later steps of JH III pathway. This report provides a basic understanding for recombinant production of this particular enzyme. Other strategies such as adding His-tag to the protein makes easy the purification of the protein which is completely different to the native protein. Complete sequence, structure and functional analysis of the enzyme will be important for developing insect-resistant crop plants by deployment of transgenic plant.
    Matched MeSH terms: Plant Proteins/chemistry*
  2. Synthesis, Antioxidant and In-Silico Studies of Potent Urease Inhibitors: N-(4-{[(4-Methoxyphenethyl)-(substituted)amino]sulfonyl}phenyl)acetamides
    Abbasi MA, Raza H, Rehman AU, Siddiqui SZ, Nazir M, Mumtaz A, et al.
    Drug Res (Stuttg), 2019 Feb;69(2):111-120.
    PMID: 30086567 DOI: 10.1055/a-0654-5074
    In this study, a new series of sulfonamides derivatives was synthesized and their inhibitory effects on DPPH and jack bean urease were evaluated. The in silico studies were also applied to ascertain the interactions of these molecules with active site of the enzyme. Synthesis was initiated by the nucleophilic substitution reaction of 2-(4-methoxyphenyl)-1-ethanamine (1: ) with 4-(acetylamino)benzenesulfonyl chloride (2): in aqueous sodium carbonate at pH 9. Precipitates collected were washed and dried to obtain the parent molecule, N-(4-{[(4-methoxyphenethyl)amino]sulfonyl}phenyl)acetamide (3): . Then, this parent was reacted with different alkyl/aralkyl halides, (4A-M: ), using dimethylformamide (DMF) as solvent and LiH as an activator to produce a series of new N-(4-{[(4-methoxyphenethyl)-(substituted)amino]sulfonyl}phenyl)acetamides (5A-M: ). All the synthesized compounds were characterized by IR, EI-MS, 1H-NMR, 13C-NMR and CHN analysis data. All of the synthesized compounds showed higher urease inhibitory activity than the standard thiourea. The compound 5 F: exhibited very excellent enzyme inhibitory activity with IC50 value of 0.0171±0.0070 µM relative to standard thiourea having IC50 value of 4.7455±0.0546 µM. Molecular docking studies suggested that ligands have good binding energy values and bind within the active region of taget protein. Chemo-informatics properties were evaluated by computational approaches and it was found that synthesized compounds mostly obeyed the Lipinski' rule.
    Matched MeSH terms: Plant Proteins/chemistry
  3. Sequence analysis and gene expression of putative oil palm chitinase and chitinase-like proteins in response to colonization of Ganoderma boninense and Trichoderma harzianum
    Yeoh KA, Othman A, Meon S, Abdullah F, Ho CL
    Mol Biol Rep, 2013 Jan;40(1):147-58.
    PMID: 23065213 DOI: 10.1007/s11033-012-2043-8
    Chitinases are glycosyl hydrolases that cleave the β-1,4-glycosidic linkages between N-acetylglucosamine residues in chitin which is a major component of fungal cell wall. Plant chitinases hydrolyze fungal chitin to chitin oligosaccharides that serve as elicitors of plant defense system against fungal pathogens. However, plants synthesize many chitinase isozymes and some of them are not pathogenesis-related. In this study, three full-length cDNA sequences encoding a putative chitinase (EgChit3-1) and two chitinase-like proteins (EgChit1-1 and EgChit5-1) have been cloned from oil palm (Elaeis guineensis) by polymerase chain reaction (PCR). The abundance of these transcripts in the roots and leaves of oil palm seedlings treated with Ganoderma boninense (a fungal pathogen) or Trichoderma harzianum (an avirulent symbiont), and a combination of both fungi at 3, 6 and 12 weeks post infection were profiled by real time quantitative reverse-transcription (qRT)-PCR. Our findings showed that the gene expression of EgChit3-1 increased significantly in the roots of oil palm seedlings treated with either G. boninense or T. harzianum and a combination of both; whereas the gene expression of EgChit1-1 in the treated roots of oil palm seedlings was not significantly higher compared to those of the untreated oil palm roots. The gene expression of EgChit5-1 was only higher in the roots of oil palm seedlings treated with T. harzianum compared to those of the untreated oil palm roots. In addition, the gene expression of EgChit1-1 and EgChit3-1 showed a significantly higher gene expression in the leaf samples of oil palm seedlings treated with either G. boninense or T. harzianum.
    Matched MeSH terms: Plant Proteins/chemistry
  4. Serine-rich protein is a novel positive regulator for silicon accumulation in mangrove
    Sahebi M, Hanafi MM, Siti Nor Akmar A, Rafii MY, Azizi P, Idris AS
    Gene, 2015 Feb 10;556(2):170-81.
    PMID: 25479011 DOI: 10.1016/j.gene.2014.11.055
    Silicon (Si) plays an important role in reducing plant susceptibility against a variety of different biotic and abiotic stresses; and also has an important regulatory role in soil to avoid heavy metal toxicity and providing suitable growing conditions for plants. A full-length cDNAs of 696bp of serine-rich protein was cloned from mangrove plant (Rhizophora apiculata) by amplification of cDNA ends from an expressed sequence tag homologous to groundnut (Arachis hypogaea), submitted to NCBI (KF211374). This serine-rich protein gene encodes a deduced protein of 223 amino acids. The transcript titre of the serine-rich protein was found to be strongly enriched in roots compared with the leaves of two month old mangrove plants and expression level of this serine-rich protein was found to be strongly induced when the mangrove seedlings were exposed to SiO2. Expression of the serine-rich protein transgenic was detected in transgenic Arabidopsis thaliana, where the amount of serine increased from 1.02 to 37.8mg/g. The same trend was also seen in Si content in the roots (14.3%) and leaves (7.4%) of the transgenic A. thaliana compared to the wild-type plants under Si treatment. The biological results demonstrated that the accumulation of the serine amino acid in the vegetative tissues of the transgenic plants enhanced their ability to absorb and accumulate more Si in the roots and leaves and suggests that the serine-rich protein gene has potential for use in genetic engineering of different stress tolerance characteristics.
    Matched MeSH terms: Plant Proteins/chemistry
  5. Iron-Binding Capacity of Defatted Rice Bran Hydrolysate and Bioavailability of Iron in Caco-2 Cells
    Foong LC, Imam MU, Ismail M
    J Agric Food Chem, 2015 Oct 21;63(41):9029-36.
    PMID: 26435326 DOI: 10.1021/acs.jafc.5b03420
    The present study was aimed at utilizing defatted rice bran (DRB) protein as an iron-binding peptide to enhance iron uptake in humans. DRB samples were treated with Alcalase and Flavourzyme, and the total extractable peptides were determined. Furthermore, the iron-binding capacities of the DRB protein hydrolysates were determined, whereas iron bioavailability studies were conducted using an in vitro digestion and absorption model (Caco-2 cells). The results showed that the DRB protein hydrolysates produced by combined Alcalase and Flavourzyme hydrolysis had the best iron-binding capacity (83%) after 90 min of hydrolysis. The optimal hydrolysis time to produce the best iron-uptake in Caco-2 cells was found to be 180 min. The results suggested that DRB protein hydrolysates have potent iron-binding capacities and may enhance the bioavailability of iron, hence their suitability for use as iron-fortified supplements.
    Matched MeSH terms: Plant Proteins/chemistry
  6. Fulltext Etlingera elatior-Mediated Synthesis of Gold Nanoparticles and Their Application as Electrochemical Current Enhancer
    Azri FA, Selamat J, Sukor R, Yusof NA, Ahmad Raston NH, Nordin N, et al.
    Molecules, 2019 Aug 29;24(17).
    PMID: 31470528 DOI: 10.3390/molecules24173141
    This work presents a simple green synthesis of gold nanoparticles (AuNPs) by using an aqueous extract of Etlingera elatior (torch ginger). The metabolites present in E. elatior, including sugars, proteins, polyphenols, and flavonoids, were known to play important roles in reducing metal ions and supporting the subsequent stability of nanoparticles. The present work aimed to investigate the ability of the E. elatior extract to synthesise AuNPs via the reduction of gold (III) chloride hydrate and characterise the properties of the nanoparticles produced. The antioxidant properties of the E. elatior extract were evaluated by analysing the total phenolic and total flavonoid contents. To ascertain the formation of AuNPs, the synthesised particles were characterised using the ultraviolet-visible (UV-Vis) spectroscopy, Fourier transform infrared (FTIR) spectroscopy, high-resolution transmission electron microscopy (HRTEM), energy-dispersive X-ray (EDX) microscopy, and dynamic light scattering (DLS) measurement. The properties of the green synthesised AuNPs were shown to be comparable to the AuNPs produced using a conventional reducing agent, sodium citrate. The UV-Vis measured the surface plasmon resonance of the AuNPs, and a band centered at 529 nm was obtained. The FTIR results proved that the extract contained the O-H functional group that is responsible for capping the nanoparticles. The HRTEM images showed that the green synthesized AuNPs were of various shapes and the average of the nanoparticles' hydrodynamic diameter was 31.5 ± 0.5 nm. Meanwhile, the zeta potential of -32.0 ± 0.4 mV indicates the high stability and negative charge of the AuNPs. We further successfully demonstrated that using the green synthesised AuNPs as the nanocomposite to modify the working surface of screen-printed carbon electrode (SPCE/Cs/AuNPs) enhanced the rate of electron transfer and provided a sensitive platform for the detection of Cu(II) ions.
    Matched MeSH terms: Plant Proteins/chemistry
  7. Optimization of Protein Extraction and Two-Dimensional Electrophoresis Protocols for Oil Palm Leaf
    Daim LD, Ooi TE, Yusof HM, Majid NA, Karsani SA
    Protein J, 2015 Aug;34(4):304-12.
    PMID: 26263918 DOI: 10.1007/s10930-015-9626-x
    Oil palm (Elaeis guineensis) is an important economic crop cultivated for its nutritional palm oil. A significant amount of effort has been undertaken to understand oil palm growth and physiology at the molecular level, particularly in genomics and transcriptomics. Recently, proteomics studies have begun to garner interest. However, this effort is impeded by technical challenges. Plant sample preparation for proteomics analysis is plagued with technical challenges due to the presence of polysaccharides, secondary metabolites and other interfering compounds. Although protein extraction methods for plant tissues exist, none work universally on all sample types. Therefore, this study aims to compare and optimize different protein extraction protocols for use with two-dimensional gel electrophoresis of young and mature leaves from the oil palm. Four protein extraction methods were evaluated: phenol-guanidine isothiocyanate, trichloroacetic acid-acetone precipitation, sucrose and trichloroacetic acid-acetone-phenol. Of these four protocols, the trichloroacetic acid-acetone-phenol method was found to give the highest resolution and most reproducible gel. The results from this study can be used in sample preparations of oil palm tissue for proteomics work.
    Matched MeSH terms: Plant Proteins/chemistry*
  8. Fulltext Curculin exhibits sweet-tasting and taste-modifying activities through its distinct molecular surfaces
    Kurimoto E, Suzuki M, Amemiya E, Yamaguchi Y, Nirasawa S, Shimba N, et al.
    J Biol Chem, 2007 Nov 16;282(46):33252-33256.
    PMID: 17895249 DOI: 10.1074/jbc.C700174200
    Curculin isolated from Curculigo latifolia, a plant grown in Malaysia, has an intriguing property of modifying sour taste into sweet taste. In addition to this taste-modifying activity, curculin itself elicits a sweet taste. Although these activities have been attributed to the heterodimeric isoform and not homodimers of curculin, the underlying mechanisms for the dual action of this protein have been largely unknown. To identify critical sites for these activities, we performed a mutational and structural study of recombinant curculin. Based on the comparison of crystal structures of curculin homo- and heterodimers, a series of mutants was designed and subjected to tasting assays. Mapping of amino acid residues on the three-dimensional structure according to their mutational effects revealed that the curculin heterodimer exhibits sweet-tasting and taste-modifying activities through its partially overlapping but distinct molecular surfaces. These findings suggest that the two activities of the curculin heterodimer are expressed through its two different modes of interactions with the T1R2-T1R3 heterodimeric sweet taste receptor.
    Matched MeSH terms: Plant Proteins/chemistry*
  9. Proteomic analysis of heat treated bitter gourd (Momordica charantia L. var. Hong Kong Green) using 2D-DIGE
    Ng ZX, Chua KH, Kuppusamy UR
    Food Chem, 2014 Apr 1;148:155-61.
    PMID: 24262540 DOI: 10.1016/j.foodchem.2013.10.025
    This study aimed to investigate the changes in the proteome of bitter gourd prior to and after subjecting to boiling and microwaving. A comparative analysis of the proteome profiles of raw and thermally treated bitter gourds was performed using 2D-DIGE. The protein content and number of protein spots in raw sample was higher when compared to the cooked samples. Qualitative analysis revealed that 103 (boiled sample) and 110 (microwaved sample) protein spots were up regulated whereas 120 (boiled sample) and 107 (microwaved sample) protein spots were down regulated. Ten protein spots with the highest significant fold change in the cooked samples were involved in carbohydrate/energy metabolisms and stress responses. Small heat shock proteins, superoxide dismutase, quinone oxidoreductase, UDP-glucose pyrophosphorylase and phosphoglycerate kinase play a role in heat-stress-mediated protection of bitter gourd. This study suggests that appropriate heat treatment (cooking methods) can lead to induction of selected proteins in bitter gourd.
    Matched MeSH terms: Plant Proteins/chemistry*
  10. Agrowaste-based nanofibers as a probiotic encapsulant: fabrication and characterization
    Fung WY, Yuen KH, Liong MT
    J Agric Food Chem, 2011 Aug 10;59(15):8140-7.
    PMID: 21711050 DOI: 10.1021/jf2009342
    This study explored the potential of soluble dietary fiber (SDF) from agrowastes, okara (soybean solid waste), oil palm trunk (OPT), and oil palm frond (OPF) obtained via alkali treatment, in the nanoencapsulation of Lactobacillus acidophilus . SDF solutions were amended with 8% poly(vinyl alcohol) to produce nanofibers using electrospinning technology. The spinning solution made from okara had a higher pH value at 5.39 ± 0.01 and a higher viscosity at 578.00 ± 11.02 mPa·s (P < 0.05), which resulted in finer fibers. FTIR spectra of nanofibers showed the presence of hemicellulose material in the SDF. Thermal behavior of nanofibers suggested possible thermal protection of probiotics in heat-processed foods. L. acidophilus was incorporated into the spinning solution to produce nanofiber-encapsulated probiotic, measuring 229-703 nm, visible under fluorescence microscopy. Viability studies showed good bacterial survivability of 78.6-90% under electrospinning conditions and retained viability at refrigeration temperature during the 21 day storage study.
    Matched MeSH terms: Plant Proteins/chemistry*
  11. Chemical and physicochemical characterization of agrowaste fibrous materials and residues
    Kuan YH, Liong MT
    J Agric Food Chem, 2008 Oct 8;56(19):9252-7.
    PMID: 18788708 DOI: 10.1021/jf802011j
    The objective of this study was to evaluate the chemical, physicochemical, and functional properties of agrowastes derived from okara ( Glycine max), corn cob ( Zea mays sp.), wheat straw ( Triticum sp.), and rice husk ( Oryza sativa) for potential applications in foods. The fibrous materials (FM) were treated with alkali to yield fibrous residues (FR). Rice husk contained the highest ash content (FM, 8.56%; FR, 9.04%) and lowest lightness in color (FM, 67.63; FR, 63.46), possibly due to the abundance of mineral constituents. Corn cob contained the highest amount of soluble dietary fiber (SDF), whereas okara had the highest total dietary fiber (TDF). The high dietary fiber fractions of corn cob and okara also contributed to the highest water- and oil-holding capacities, emulsifying activities, and emulsion stabilities for both FM and FR samples. These results indicate that these agrowastes could be utilized as functional ingredients in foods.
    Matched MeSH terms: Plant Proteins/chemistry
  12. Physicochemical and functional properties of Alcalase-extracted protein hydrolysate from oil palm leaves
    Hau EH, Teh SS, Yeo SK, Mah SH
    J Sci Food Agric, 2022 Jan 15;102(1):233-240.
    PMID: 34081335 DOI: 10.1002/jsfa.11350
    BACKGROUND: The oil palm tree produces 90% of wastes and the limited usage of these wastes causes a major disposal problem in the mills. Nevertheless, these by-products have a large amount of nutritional components. Thus, the present study aimed to determine the physicochemical and functional properties of protein hydrolysates (PH) from oil palm leaves (OPL) extracted using different concentrations of Alcalase (0-10%) at 2 h of hydrolysis time.

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

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

    Matched MeSH terms: Plant Proteins/chemistry*
  13. Optimized preparation and characterization of CLEA-lipase from cocoa pod husk
    Khanahmadi S, Yusof F, Amid A, Mahmod SS, Mahat MK
    J Biotechnol, 2015 May 20;202:153-61.
    PMID: 25481099 DOI: 10.1016/j.jbiotec.2014.11.015
    Cross-linked enzyme aggregate (CLEA) is easily prepared from crude enzyme and has many advantages to the environment and it is considered as an economic method in the context of industrial biocatalysis compared to free enzyme. In this work, a highly active and stable CLEA-lipase from cocoa pod husk (CPH) which is a by-product after removal of cocoa beans, were assayed for their hydrolytic activity and characterized under the optimum condition successfully. Face centered central composite design (FCCCD) under response surface methodology (RSM) was used to get the optimal conditions of the three significant factors (concentration of ammonium sulfate, concentration of glutaraldehyde and concentration of additive) to achieve higher enzyme activity of CLEA. From 20 runs, the highest activity recorded was around 9.407U (83% recovered activity) under the condition of using 20% saturated ammonium sulfate, 60mM glutaraldehyde as cross-linker and 0.17mM bovine serum albumin as feeder. Moreover, the optimal reaction temperature and pH value in enzymatic reaction for both crude enzyme and immobilized were found to be 45°C at pH 8 and 60°C at pH 8.2, respectively. A systematic study of the stability of CLEA and crude enzyme was taken with regards to temperature (25-60°C) and pH (5-10) value and in both factors, CLEA-lipase showed more stability than free lipase. The Km value of CLEA was higher compared to free enzyme (0.55mM vs. 0.08mM). The CLEA retained more than 60% of the initial activity after six cycles of reuse compared to free enzyme. The high stability and recyclability of CLEA-lipase from CPH make it efficient for different industrial applications.
    Matched MeSH terms: Plant Proteins/chemistry
  14. Molecular analysis of Hsp70 mechanisms in plants and their function in response to stress
    Usman MG, Rafii MY, Martini MY, Yusuff OA, Ismail MR, Miah G
    Biotechnol Genet Eng Rev, 2017 Apr;33(1):26-39.
    PMID: 28649918 DOI: 10.1080/02648725.2017.1340546
    Studying the strategies of improving abiotic stress tolerance is quite imperative and research under this field will increase our understanding of response mechanisms to abiotic stress such as heat. The Hsp70 is an essential regulator of protein having the tendency to maintain internal cell stability like proper folding protein and breakdown of unfolded proteins. Hsp70 holds together protein substrates to help in movement, regulation, and prevent aggregation under physical and or chemical pressure. However, this review reports the molecular mechanism of heat shock protein 70 kDa (Hsp70) action and its structural and functional analysis, research progress on the interaction of Hsp70 with other proteins and their interaction mechanisms as well as the involvement of Hsp70 in abiotic stress responses as an adaptive defense mechanism.
    Matched MeSH terms: Plant Proteins/chemistry
  15. Fulltext Effect of different purification techniques on the characteristics of heteropolysaccharide-protein biopolymer from durian (Durio zibethinus) seed
    Amid BT, Mirhosseini H
    Molecules, 2012 Sep 10;17(9):10875-92.
    PMID: 22964503 DOI: 10.3390/molecules170910875
    Natural biopolymers from plant sources contain many impurities (e.g., fat, protein, fiber, natural pigment and endogenous enzymes), therefore, an efficient purification process is recommended to minimize these impurities and consequently improve the functional properties of the biopolymer. The main objective of the present study was to investigate the effect of different purification techniques on the yield, protein content, solubility, water- and oil-holding capacity of a heteropolysaccharide-protein biopolymer obtained from durian seed. Four different purification methods using different chemicals and solvents (i.e., A (isopropanol and ethanol), B (isopropanol and acetone), C (saturated barium hydroxide), and D (Fehling solution)] to liberate the purified biopolymer from its crude form were compared. In most cases, the purification process significantly (p < 0.05) improved the physicochemical properties of heteropolysaccharide-protein biopolymer from durian fruit seed. The present work showed that the precipitation using isopropanol and acetone (Method B) resulted in the highest purification yield among all the tested purification techniques. The precipitation using saturated barium hydroxide (Method C) led to induce the highest solubility and relatively high capacity of water absorption. The current study reveals that the precipitation using Fehling solution (Method D) most efficiently eliminates the protein fraction, thus providing more pure biopolymer suitable for biological applications.
    Matched MeSH terms: Plant Proteins/chemistry*
  16. Shear flow behaviour and emulsion-stabilizing effect of natural polysaccharide-protein gum in aqueous system and oil/water (O/W) emulsion
    Amid BT, Mirhosseini H
    Colloids Surf B Biointerfaces, 2013 Mar 1;103:430-40.
    PMID: 23261563 DOI: 10.1016/j.colsurfb.2012.11.015
    The main objective of the current work was to characterize the shear rheological flow behaviour and emulsifying properties of the natural biopolymer from durian seed. The present study revealed that the extraction condition significantly affected the physical and functional characteristics of the natural biopolymer from durian seed. The dynamic oscillatory test indicated that the biopolymer from durian seed showed more gel (or solid) like behaviour than the viscous (or liquid) like behaviour (G'>G″) at a relatively high concentration (20%) in the fixed frequency (0.1 Hz). This might be explained by the fact that the gum coils disentangle at low frequencies during the long period of oscillation, thus resulting in more gel like behaviour than the viscous like behaviour. The average droplet size of oil in water (O/W) emulsions stabilized by durian seed gum significantly varied from 0.42 to 7.48 μm. The results indicated that O/W emulsions showed significant different stability after 4 months storage. This might be interpreted by the considerable effect of the extraction condition on the chemical and molecular structure of the biopolymer, thus affecting its emulsifying capacity. The biopolymer extracted by using low water to seed (W/S) ratio at the low temperature under the alkaline condition showed a relatively high emulsifying activity in O/W emulsion.
    Matched MeSH terms: Plant Proteins/chemistry*
  17. Fulltext Influence of chemical extraction on rheological behavior, viscoelastic properties and functional characteristics of natural heteropolysaccharide/protein polymer from Durio zibethinus seed
    Amid BT, Mirhosseini H
    Int J Mol Sci, 2012 Nov 13;13(11):14871-88.
    PMID: 23203099 DOI: 10.3390/ijms131114871
    In recent years, the demand for a natural plant-based polymer with potential functions from plant sources has increased considerably. The main objective of the current study was to study the effect of chemical extraction conditions on the rheological and functional properties of the heteropolysaccharide/protein biopolymer from durian (Durio zibethinus) seed. The efficiency of different extraction conditions was determined by assessing the extraction yield, protein content, solubility, rheological properties and viscoelastic behavior of the natural polymer from durian seed. The present study revealed that the soaking process had a more significant (p < 0.05) effect than the decolorizing process on the rheological and functional properties of the natural polymer. The considerable changes in the rheological and functional properties of the natural polymer could be due to the significant (p < 0.05) effect of the chemical extraction variables on the protein fraction present in the molecular structure of the natural polymer from durian seed. The natural polymer from durian seed had a more elastic (or gel like) behavior compared to the viscous (liquid like) behavior at low frequency. The present study revealed that the natural heteropolysaccharide/protein polymer from durian seed had a relatively low solubility ranging from 9.1% to 36.0%. This might be due to the presence of impurities, insoluble matter and large particles present in the chemical structure of the natural polymer from durian seed.
    Matched MeSH terms: Plant Proteins/chemistry*
  18. Protein replenishment in pitcher fluids of Nepenthes × ventrata revealed by quantitative proteomics (SWATH-MS) informed by transcriptomics
    Wan Zakaria WNA, Aizat WM, Goh HH, Mohd Noor N
    J Plant Res, 2019 Sep;132(5):681-694.
    PMID: 31422552 DOI: 10.1007/s10265-019-01130-w
    Carnivorous plants capture and digest insects for nutrients, allowing them to survive in soil deprived of nitrogenous nutrients. Plants from the genus Nepenthes produce unique pitchers containing secretory glands, which secrete enzymes into the digestive fluid. We performed RNA-seq analysis on the pitcher tissues and liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis on the pitcher fluids of Nepenthes × ventrata to study protein expression in this carnivory organ during early days of pitcher opening. This transcriptome provides a sequence database for pitcher fluid protein identification. A total of 32 proteins of diverse functions were successfully identified in which 19 proteins can be quantified based on label-free quantitative proteomics (SWATH-MS) analysis while 16 proteins were not reported previously. Our findings show that certain proteins in the pitcher fluid were continuously secreted or replenished after pitcher opening, even without any prey or chitin induction. We also discovered a new aspartic proteinase, Nep6, secreted into pitcher fluid. This is the first SWATH-MS analysis of protein expression in Nepenthes pitcher fluid using a species-specific reference transcriptome. Taken together, our study using a gel-free shotgun proteomics informed by transcriptomics (PIT) approach showed the dynamics of endogenous protein secretion in the digestive organ of N. × ventrata and provides insights on protein regulation during early pitcher opening prior to prey capture.
    Matched MeSH terms: Plant Proteins/chemistry
  19. Monoterpene alcohol metabolism: identification, purification, and characterization of two geraniol dehydrogenase isoenzymes from Polygonum minus leaves
    Hassan M, Maarof ND, Ali ZM, Noor NM, Othman R, Mori N
    Biosci Biotechnol Biochem, 2012;76(8):1463-70.
    PMID: 22878188
    NADP(+)-dependent geraniol dehydrogenase (EC 1.1.1.183) is an enzyme that catalyzes the oxidation of geraniol to geranial. Stable, highly active cell-free extract was obtained from Polygonum minus leaves using polyvinylpolypyrrolidone, Amberlite XAD-4, glycerol, 2-mercaptoethanol, thiourea, and phenylmethylsulfonylfluoride in tricine-NaOH buffer (pH 7.5). The enzyme preparation was separated into two activity peaks, geraniol-DH I and II, by DEAE-Toyopearl 650M column chromatography at pH 7.5. Both isoenzymes were purified to homogeneity in three chromatographic steps. The geraniol-DH isoenzymes were similar in molecular mass, optimal temperature, and pH, but the isoelectric point, substrate specificity, and kinetic parameters were different. The K(m) values for geraniol of geraniol-DH I and II appeared to be 0.4 mM and 0.185 mM respectively. P. minus geraniol-DHs are unusual among geraniol-DHs in view of their thermal stability and optimal temperatures, and also their high specificity for allylic alcohols and NADP(+).
    Matched MeSH terms: Plant Proteins/chemistry*
  20. Fulltext Synergy of antibacterial and antioxidant activities from crude extracts and peptides of selected plant mixture
    Shami AM, Philip K, Muniandy S
    BMC Complement Altern Med, 2013 Dec 16;13:360.
    PMID: 24330547 DOI: 10.1186/1472-6882-13-360
    BACKGROUND: A plant mixture containing indigenous Australian plants was examined for synergistic antimicrobial activity using selected test microorganisms. This study aims to investigate antibacterial activities, antioxidant potential and the content of phenolic compounds in aqueous, ethanolic and peptide extracts of plant mixture.

    METHODS: Well diffusion, minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) assays were used to test antibacterial activity against four pathogenic bacteria namely Staphylococcus aureus, Escherichia coli, Bacillus cereus, and Pseudomonas aeruginosa. DPPH (2, 2-diphenyl-1- picrylhydrazyl) and superoxide dismutase (SOD) assays were used to evaluate antioxidant activity. HPLC and gel filtration were used for purification of the peptides. Scanning electron microscope was applied to investigate the mode of attachment of the peptides on target microbial membranes.

    RESULTS: Aqueous extraction of the mixture showed no inhibition zones against all the test bacteria. Mean diameter of inhibition zones for ethanol extraction of this mixture attained 8.33 mm, 7.33 mm, and 6.33 mm against S. aureus at corresponding concentrations of 500, 250 and 125 mg/ml while E .coli showed inhibition zones of 9.33 mm, 8.00 mm and 6.66 mm at the same concentrations. B. cereus exhibited inhibition zones of 11.33 mm, 10.33 mm and 10.00 mm at concentrations of 500, 250 and 125 mg/ml respectively. The peptide extract demonstrated antibacterial activity against S. aureus, E. coli and B. cereus. The MIC and MBC values for ethanol extracts were determined at 125 mg/ml concentration against S. aureus and E. coli and B. cereus value was 31.5 mg/ml. MIC and MBC values showed that the peptide extract was significantly effective at low concentration of the Australian plant mixture (APM). Phenolic compounds were detected in hot aqueous and ethanolic extracts of the plant mixture. Hot aqueous, ethanol and peptides extracts also exhibited antioxidant activities.

    CONCLUSIONS: It was concluded that APM possessed good antibacterial and antioxidant activities following extraction with different solvents. The results suggest that APM provide a new source with antibacterial agents and antioxidant activity for nutraceutical or medical applications.

    Matched MeSH terms: Plant Proteins/chemistry
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