Displaying publications 21 - 40 of 61 in total

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  1. GCTTCA as a novel motif for regulating mesocarp-specific expression of the oil palm (Elaeis guineensis Jacq.) stearoyl-ACP desaturase gene
    Hanifiah FHA, Abdullah SNA, Othman A, Shaharuddin NA, Saud HM, Hasnulhadi HAH, et al.
    Plant Cell Rep, 2018 Aug;37(8):1127-1143.
    PMID: 29789886 DOI: 10.1007/s00299-018-2300-y
    KEY MESSAGE: TAAAAT and a novel motif, GCTTCA found in the oil palm stearoyl-ACP desaturase (SAD1) promoter are involved in regulating mesocarp-specific expression. Two key fatty acid biosynthetic genes, stearoyl-ACP desaturase (SAD1), and acyl-carrier protein (ACP3) in Elaeis guineensis (oil palm) showed high level of expression during the period of oil synthesis in the mesocarp [12-19 weeks after anthesis (w.a.a.)] and kernel (12-15 w.a.a.). Both genes are expressed in spear leaves at much lower levels and the expression increased by 1.5-fold to 2.5-fold following treatments with ethylene and abscisic acid (ABA). Both SAD1 and ACP3 promoters contain phytohormone-responsive, light-responsive, abiotic factors/wounding-responsive, endosperm specificity and fruit maturation/ripening regulatory motifs. The activities of the full length and six 5' deletion fragments of the SAD1 promoter were analyzed in transiently transformed oil palm tissues by quantitative β-glucuronidase (GUS) fluorometric assay. The highest SAD1 promoter activity was observed in the mesocarp followed by kernel and the least in the leaves. GUS activity in the D3 deletion construct (- 486 to + 108) was the highest, while the D2 (- 535 to + 108) gave the lowest suggesting the presence of negative cis-acting regulatory element(s) in the deleted - 535 to - 486 (49 bp). It was found that the 49-bp region binds to the nuclear protein extract from mesocarp but not from leaves in electrophoretic mobility shift assay (EMSA). Further fine-tuned analysis of this 49-bp region using truncated DNA led to the identification of GCTTCA as a novel motif in the SAD1 promoter. Interestingly, another known fruit ripening-related motif, LECPLEACS2 (TAAAAT) was found to be required for effective binding of the novel motif to the mesocarp nuclear protein extract.
    Matched MeSH terms: Plant Proteins/chemistry*
  2. Generation, Fractionation, and Characterization of Iron-Chelating Protein Hydrolysate from Palm Kernel Cake Proteins
    Zarei M, Ghanbari R, Tajabadi N, Abdul-Hamid A, Bakar FA, Saari N
    J Food Sci, 2016 Feb;81(2):C341-7.
    PMID: 26720491 DOI: 10.1111/1750-3841.13200
    Palm kernel cake protein was hydrolyzed with different proteases namely papain, bromelain, subtilisin, flavourzyme, trypsin, chymotrypsin, and pepsin to generate different protein hydrolysates. Peptide content and iron-chelating activity of each hydrolysate were evaluated using O-phthaldialdehyde-based spectrophotometric method and ferrozine-based colorimetric assay, respectively. The results revealed a positive correlation between peptide contents and iron-chelating activities of the protein hydrolysates. Protein hydrolysate generated by papain exhibited the highest peptide content of 10.5 mM and highest iron-chelating activity of 64.8% compared with the other hydrolysates. Profiling of the papain-generated hydrolysate by reverse phase high performance liquid chromatography fractionation indicated a direct association between peptide content and iron-chelating activity in most of the fractions. Further fractionation using isoelectric focusing also revealed that protein hydrolysate with basic and neutral isoelectric point (pI) had the highest iron-chelating activity, although a few fractions in the acidic range also exhibited good metal chelating potential. After identification and synthesis of papain-generated peptides, GGIF and YLLLK showed among the highest iron-chelating activities of 56% and 53%, whereas their IC50 were 1.4 and 0.2 μM, respectively.
    Matched MeSH terms: Plant Proteins/chemistry*
  3. Harvesting of the Microalga Nannochloropsis sp. by Bioflocculation with Mung Bean Protein Extract
    Kandasamy G, Shaleh SRM
    Appl Biochem Biotechnol, 2017 Jun;182(2):586-597.
    PMID: 27957653 DOI: 10.1007/s12010-016-2346-7
    Harvesting microalgae from medium is a major challenge due to their small size and low concentrations. In an attempt to find a cost-effective and eco-friendly harvesting technique, mung bean (Vigna radiata) protein extract (MBPE) was used for flocculation of Nannochloropsis sp. The effects of parameters such as pH, flocculant dose, algae concentration, and mixing time were used to study the flocculation efficiency (FE) of MBPE. Optimum parameters of MBPE dosage of 20 mL L(-1) and a mixing rate of 300 rpm for 6 min achieved a FE of >92% after 2 h of settling time. MBPE-aggregated microlga flocs were characterized by microscopy. Zeta potential values decreased with increasing flocculant dose, and the values obtained were -6.93 ± 0.60, -5.36 ± 0.64, and -4.44 ± 0.22 for doses of 10, 20, and 30 mL L(-1), respectively. In conclusion, MBPE flocculants used in this study are safe, nontoxic, and pollution free, so they could be used for an effective, convenient, and rapid harvesting of microalgae in an eco-friendly approach. These methods are sustainable and could be applied in industrial scale for aquaculture nutrition.
    Matched MeSH terms: Plant Proteins/chemistry*
  4. Hev b 5 and Hev b 13 as allergen markers to estimate the allergenic potency of latex gloves
    Yeang HY, Arif SA, Raulf-Heimsoth M, Loke YH, Sander I, Sulong SH, et al.
    J Allergy Clin Immunol, 2004 Sep;114(3):593-8.
    PMID: 15356563 DOI: 10.1016/j.jaci.2004.05.039
    BACKGROUND:
    Sensitization to natural rubber latex has been linked to proteins from medical latex gloves. Various assays to estimate the amount of residual allergenic proteins extractable from latex gloves to assess their potential exposure hazard have inherent weaknesses.

    OBJECTIVE:
    This investigation was aimed at developing 2-site immunoenzymetric assays and identifying appropriate protein markers to assess the allergenic potential of latex gloves.

    METHODS:
    The presence of 6 latex allergens--Hev b 1, 2, 3, 5, 6, and 13--was measured in a cross-section of commercial latex medical gloves by using monoclonal and polyclonal antibody-based 2-site immunoenzymetric assays. The overall allergenic potential of these gloves was assessed by IgE-inhibition assay. Stepwise multiple regression analyses were performed to identify marker allergens that best explained the variation in latex glove allergenicity.

    RESULTS:
    All 6 latex allergens were detected in at least some of the glove samples. Hev b 5 and Hev b 13 were identified as the marker allergens that combined best to explain the variation in the glove allergenicity. The significant multiple correlation (R=0.855) between these 2 markers and glove allergenic potency forms the basis of an assay to gauge latex glove allergenicity.

    CONCLUSION:
    The overall allergenic potential of latex gloves can be estimated by using Hev b 5 and Hev b 13 as indicator allergens. The correlation between glove allergenicity and the level of these allergens was maintained for low-protein gloves (<200 microg/g). This estimation of glove allergenicity was superior to that obtained by using total protein readings.
    Matched MeSH terms: Plant Proteins/chemistry
  5. Improving protein production of indigenous microalga Chlorella vulgaris FSP-E by photobioreactor design and cultivation strategies
    Chen CY, Lee PJ, Tan CH, Lo YC, Huang CC, Show PL, et al.
    Biotechnol J, 2015 Jun;10(6):905-14.
    PMID: 25865941 DOI: 10.1002/biot.201400594
    Fish meal is currently the major protein source for commercial aquaculture feed. Due to its unstable supply and increasing price, fish meal is becoming more expensive and its availability is expected to face significant challenges in the near future. Therefore, feasible alternatives to fish meal are urgently required. Microalgae have been recognized as the most promising candidates to replace fish meal because the protein composition of microalgae is similar to fish meal and the supply of microalgae-based proteins is sustainable. In this study, an indigenous microalga (Chlorella vulgaris FSP-E) with high protein content was selected, and its feasibility as an aquaculture protein source was explored. An innovative photobioreactor (PBR) utilizing cold cathode fluorescent lamps as an internal light source was designed to cultivate the FSP-E strain for protein production. This PBR could achieve a maximum biomass and protein productivity of 699 and 365 mg/L/day, respectively, under an optimum urea and iron concentration of 12.4 mM and 90 μM, respectively. In addition, amino acid analysis of the microalgal protein showed that up to 70% of the proteins in this microalgal strain consist of indispensable amino acids. Thus, C. vulgaris FSP-E appears to be a viable alternative protein source for the aquaculture industry.
    Matched MeSH terms: Plant Proteins/chemistry
  6. 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*
  7. 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
  8. Isolation and characterization of differentially expressed transcripts from the suspension cells of oil palm (Elaeis guineensis Jacq.) in response to different concentration of auxins
    Roowi SH, Ho CL, Alwee SS, Abdullah MO, Napis S
    Mol Biotechnol, 2010 Sep;46(1):1-19.
    PMID: 20390382 DOI: 10.1007/s12033-010-9262-9
    Oil palm suspension cultures were initiated by transferring the gel-like friable embryogenic tissue onto liquid medium supplemented with auxins. In this study, transcripts that were differentially expressed in oil palm suspension cells cultured at different auxin concentrations were examined using suppression subtractive hybridization. Total RNA was first isolated from oil palm suspension cells proliferated in liquid medium with different hormone concentrations for 6 months. Four different hormone combinations: T1 (0.1 mg/l 2,4-D and 1.0 mg/l NAA), T2 (0.4 mg/l 2,4-D and 1.0 mg/l NAA), T3 (1.0 mg/l NAA), and T4 (0.4 mg/l 2,4-D) were used for the treatments. The first and second subtractions were performed using samples T1 and T2 in forward and reverse order. The other two subtractions were forward and reverse subtractions of T3 and T4, respectively. Reverse northern analyses showed that 14.13% of these clones were preferentially expressed in T1, 13.70% in T2, 14.75% in T3, and 15.70% in T4. Among the 294 cDNA clones that were sequenced, 61 contigs (assembled from 165 sequences) and 129 singletons were obtained. Among the 61 contigs, 10 contigs consist of sequences from treatment T1, 8 contigs were from treatment T2, 10 contigs were contains sequences of treatment T3 and 13 contigs contains sequences of treatment T4. Northern analyses of five transcripts that were shown to be differentially expressed in the oil palm suspension cells by reverse northern analysis revealed that transcripts 16A1 (a putative lignostilbene-alpha,beta-dioxygenase, EgLSD) and 16H12 (a putative ethylene responsive 6, EgER6) were differentially expressed in oil palm suspension cells treated with different levels of auxin.
    Matched MeSH terms: Plant Proteins/chemistry
  9. Fulltext Kinetic studies and homology modeling of a dual-substrate linalool/nerolidol synthase from Plectranthus amboinicus
    Ashaari NS, Ab Rahim MH, Sabri S, Lai KS, Song AA, Abdul Rahim R, et al.
    Sci Rep, 2021 Aug 24;11(1):17094.
    PMID: 34429465 DOI: 10.1038/s41598-021-96524-z
    Linalool and nerolidol are terpene alcohols that occur naturally in many aromatic plants and are commonly used in food and cosmetic industries as flavors and fragrances. In plants, linalool and nerolidol are biosynthesized as a result of respective linalool synthase and nerolidol synthase, or a single linalool/nerolidol synthase. In our previous work, we have isolated a linalool/nerolidol synthase (designated as PamTps1) from a local herbal plant, Plectranthus amboinicus, and successfully demonstrated the production of linalool and nerolidol in an Escherichia coli system. In this work, the biochemical properties of PamTps1 were analyzed, and its 3D homology model with the docking positions of its substrates, geranyl pyrophosphate (C10) and farnesyl pyrophosphate (C15) in the active site were constructed. PamTps1 exhibited the highest enzymatic activity at an optimal pH and temperature of 6.5 and 30 °C, respectively, and in the presence of 20 mM magnesium as a cofactor. The Michaelis-Menten constant (Km) and catalytic efficiency (kcat/Km) values of 16.72 ± 1.32 µM and 9.57 × 10-3 µM-1 s-1, respectively, showed that PamTps1 had a higher binding affinity and specificity for GPP instead of FPP as expected for a monoterpene synthase. The PamTps1 exhibits feature of a class I terpene synthase fold that made up of α-helices architecture with N-terminal domain and catalytic C-terminal domain. Nine aromatic residues (W268, Y272, Y299, F371, Y378, Y379, F447, Y517 and Y523) outlined the hydrophobic walls of the active site cavity, whilst residues from the RRx8W motif, RxR motif, H-α1 and J-K loops formed the active site lid that shielded the highly reactive carbocationic intermediates from the solvents. The dual substrates use by PamTps1 was hypothesized to be possible due to the architecture and residues lining the catalytic site that can accommodate larger substrate (FPP) as demonstrated by the protein modelling and docking analysis. This model serves as a first glimpse into the structural insights of the PamTps1 catalytic active site as a multi-substrate linalool/nerolidol synthase.
    Matched MeSH terms: Plant Proteins/chemistry
  10. Fulltext Low concentration of silver nanoparticles not only enhances the activity of horseradish peroxidase but alter the structure also
    Karim Z, Adnan R, Ansari MS
    PLoS One, 2012;7(7):e41422.
    PMID: 22848490 DOI: 10.1371/journal.pone.0041422
    Chemical synthesis of Ag-NPs was carried out using reduction method. The reduction mechanistic approach of silver ions was found to be a basic clue for the formation of the Ag-NPs. The nanoparticles were characterized by UV-vis, FT-IR and TEM analysis. We had designed some experiments in support of our hypothesis, "low concentrations of novel nanoparticles (silver and gold) increases the activity of plant peroxidases and alter their structure also", we had used Ag-NPs and HRP as models. The immobilization/interaction experiment had demonstrated the specific concentration range of the Ag-NPs and within this range, an increase in HRP activity was reported. At 0.08 mM concentration of Ag-NPs, 50% increase in the activity yield was found. The U.V-vis spectra had demonstrated the increase in the absorbance of HRP within the reported concentration range (0.06-0.12 mM). Above and below this concentration range there was a decrease in the activity of HRP. The results that we had found from the fluorescence spectra were also in favor of our hypothesis. There was a maximum increase in ellipticity and α-helix contents in the presence of 0.08 mM concentration of Ag-NPs, demonstrated by circular dichroism (CD) spectra. Finally, incubation of a plant peroxidase, HRP with Ag-NPs, within the reported concentration range not only enhances the activity but also alter the structure.
    Matched MeSH terms: Plant Proteins/chemistry*
  11. Method development for analysis of proteins extracted from the leaves of Orthosiphon aristatus
    Koay SY, Gam LH
    J Chromatogr B Analyt Technol Biomed Life Sci, 2011 Jul 15;879(22):2179-83.
    PMID: 21689998 DOI: 10.1016/j.jchromb.2011.05.041
    Orthosiphon aristatus is a traditionally used medicinal plant. In order to study the proteome of the plant, we have developed a simple plant protein extraction method by direct extraction of protein using a modified 2D-gel compatible tris-sucrose buffer followed by a double TCA-acetone precipitation. This method omitted the use of toxic phenol which is widely used in the studies of plants proteins. Moreover, it shortens the lengthy extraction procedure of phenol extraction and back-extraction method and therefore reduced the extraction time (by 2h) while increased in protein yields (by 50%). Comparison of the 2D-gel images of the two extracts revealed that >60 extra protein spots were detected in the extract of our current method. The method was applied on the leaves of O. aristatus collected from six geographical areas in Malaysia. The correlation coefficient of each replicate gels from the six areas ranged from 0.70 to 0.90 indicating good reproducibility of the method.
    Matched MeSH terms: Plant Proteins/chemistry*
  12. Molecular Modeling and Simulation of Transketolase from Orthosiphon stamineus
    Ng ML, Rahmat ZB, Bin Omar MSS
    Curr Comput Aided Drug Des, 2019;15(4):308-317.
    PMID: 30345923 DOI: 10.2174/1573409914666181022141753
    BACKGROUND: Orthosiphon stamineus is a traditional medicinal plant in Southeast Asia countries with various well-known pharmacological activities such as antidiabetic, diuretics and antitumor activities. Transketolase is one of the proteins identified in the leaves of the plant and transketolase is believed able to lower blood sugar level in human through non-pancreatic mechanism. In order to understand the protein behavioral properties, 3D model of transketolase and analysis of protein structure are of obvious interest.

    METHODS: In the present study, 3D model of transketolase was constructed and its atomic characteristics revealed. Besides, molecular dynamic simulation of the protein at 310 K and 368 K deciphered transketolase may be a thermophilic protein as the structure does not distort even at elevated temperature. This study also used the protein at 310 K and 368 K resimulated back at 310 K environment.

    RESULTS: The results revealed that the protein is stable at all condition which suggest that it has high capacity to adapt at different environment not only at high temperature but also from high temperature condition to low temperature where the structure remains unchanged while retaining protein function.

    CONCLUSION: The thermostability properties of transketolase is beneficial for pharmaceutical industries as most of the drug making processes are at high temperature condition.

    Matched MeSH terms: Plant Proteins/chemistry*
  13. 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
  14. 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*
  15. Neoculin as a new taste-modifying protein occurring in the fruit of Curculigo latifolia
    Shirasuka Y, Nakajima K, Asakura T, Yamashita H, Yamamoto A, Hata S, et al.
    Biosci Biotechnol Biochem, 2004 Jun;68(6):1403-7.
    PMID: 15215616
    A unique taste-modifying activity that converts the sense of sourness to the sense of sweetness occurs in the fruit of the plant Curculigo latifolia, intrinsic to West Malaysia. The active component, known as curculin, is a protein consisting of two identical subunits. We have found a new taste-modifying protein, named neoculin, of the same origin. Both chemical analysis and cDNA cloning characterized neoculin as a heterodimeric protein consisting of an acidic, glycosylated subunit of 113 amino acid residues and a basic subunit that is the monomeric curculin itself.
    Matched MeSH terms: Plant Proteins/chemistry
  16. 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*
  17. Oil palm drought inducible DREB1 induced expression of DRE/CRT- and non-DRE/CRT-containing genes in lowland transgenic tomato under cold and PEG treatments
    Azzeme AM, Abdullah SNA, Aziz MA, Wahab PEM
    Plant Physiol Biochem, 2017 Mar;112:129-151.
    PMID: 28068641 DOI: 10.1016/j.plaphy.2016.12.025
    Dehydration-responsive element binding (DREB) transcription factor plays an important role in controlling the expression of abiotic stress responsive genes. An intronless oil palm EgDREB1 was isolated and confirmed to be a nuclear localized protein. Electrophoretic mobility shift and yeast one-hybrid assays validated its ability to interact with DRE/CRT motif. Its close evolutionary relation to the dicot NtDREB2 suggests a universal regulatory role. In order to determine its involvement in abiotic stress response, functional characterization was performed in oil palm seedlings subjected to different levels of drought severity and in EgDREB1 transgenic tomato seedlings treated by abiotic stresses. Its expression in roots and leaves was compared with several antioxidant genes using quantitative real-time PCR. Early accumulation of EgDREB1 in oil palm roots under mild drought suggests possible involvement in the initiation of signaling communication from root to shoot. Ectopic expression of EgDREB1 in T1 transgenic tomato seedlings enhanced expression of DRE/CRT and non-DRE/CRT containing genes, including tomato peroxidase (LePOD), ascorbate peroxidase (LeAPX), catalase (LeCAT), superoxide dismutase (LeSOD), glutathione reductase (LeGR), glutathione peroxidase (LeGP), heat shock protein 70 (LeHSP70), late embryogenesis abundant (LeLEA), metallothionine type 2 (LeMET2), delta 1-pyrroline-5- carboxylate synthetase (LePCS), ABA-aldehyde oxidase (LeAAO) and 9-cis- Epoxycarotenoid dioxygenase (LeECD) under PEG treatment and cold stress (4 °C). Altogether, these findings suggest that EgDREB1 is a functional regulator in enhancing tolerance to drought and cold stress.
    Matched MeSH terms: Plant Proteins/chemistry
  18. 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*
  19. Optimization of hexametaphosphate-assisted extraction and functional characterization of palm kernel cake protein
    Chee KL, Ayob MK
    Food Sci Technol Int, 2013 Apr;19(2):109-22.
    PMID: 23520324 DOI: 10.1177/1082013212442185
    Response surface methodology was applied to study the optimization of palm kernel cake protein (PKCP) hexametaphosphate-assisted extraction. The optimum PKCP yield (28.37%) when extracted using 1.50% sodium hexametaphosphate (SHMP) of pH 10, at 50 °C, and the 1:70 (w/v) ratio of cake-to-solvent was significantly (P 
    Matched MeSH terms: Plant Proteins/chemistry*
  20. 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
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