Displaying publications 1 - 20 of 38 in total

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  1. Fulltext Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica
    Yusof NA, Hashim NH, Beddoe T, Mahadi NM, Illias RM, Bakar FD, et al.
    Cell Stress Chaperones, 2016 Jul;21(4):707-15.
    PMID: 27154490 DOI: 10.1007/s12192-016-0696-2
    The ability of eukaryotes to adapt to an extreme range of temperatures is critically important for survival. Although adaptation to extreme high temperatures is well understood, reflecting the action of molecular chaperones, it is unclear whether these molecules play a role in survival at extremely low temperatures. The recent genome sequencing of the yeast Glaciozyma antarctica, isolated from Antarctic sea ice near Casey Station, provides an opportunity to investigate the role of molecular chaperones in adaptation to cold temperatures. We isolated a G. antarctica homologue of small heat shock protein 20 (HSP20), GaSGT1, and observed that the GaSGT1 mRNA expression in G. antarctica was markedly increased following culture exposure at low temperatures. Additionally, we demonstrated that GaSGT1 overexpression in Escherichia coli protected these bacteria from exposure to both high and low temperatures, which are lethal for growth. The recombinant GaSGT1 retained up to 60 % of its native luciferase activity after exposure to luciferase-denaturing temperatures. These results suggest that GaSGT1 promotes cell thermotolerance and employs molecular chaperone-like activity toward temperature assaults.
    Matched MeSH terms: Fungal Proteins/chemistry
  2. Efficient removal of lignin with the maintenance of hemicellulose from kenaf by two-stage pretreatment process
    Wan Azelee NI, Md Jahim J, Rabu A, Abdul Murad AM, Abu Bakar FD, Md Illias R
    Carbohydr Polym, 2014 Jan;99:447-53.
    PMID: 24274529 DOI: 10.1016/j.carbpol.2013.08.043
    The enhancement of lignocellulose hydrolysis using enzyme complexes requires an efficient pretreatment process to obtain susceptible conditions for the enzyme attack. This study focuses on removing a major part of the lignin layer from kenaf (Hibiscus cannabinus) while simultaneously maintaining most of the hemicellulose. A two-stage pretreatment process is adopted using calcium hydroxide, Ca(OH)₂, and peracetic acid, PPA, to break the recalcitrant lignin layer from other structural polysaccharides. An experimental screening of several pretreatment chemicals, concentrations, temperatures and solid-liquid ratios enabled the production of an optimally designed pretreatment process for kenaf. Our results showed that the pretreatment process has provide 59.25% lignin removal while maintaining 87.72% and 96.17% hemicellulose and cellulose, respectively, using 1g of Ca(OH)₂/L and a 8:1 (mL:g) ratio of liquid-Ca(OH)₂ at 50 °C for 1.5 h followed by 20% peracetic acid pretreatment at 75 °C for 2 h. These results validate this mild approach for aiding future enzymatic hydrolysis.
    Matched MeSH terms: Fungal Proteins/chemistry
  3. 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: Fungal Proteins/chemistry*
  4. Novel lipase purification methods - a review of the latest developments
    Tan CH, Show PL, Ooi CW, Ng EP, Lan JC, Ling TC
    Biotechnol J, 2015 Jan;10(1):31-44.
    PMID: 25273633 DOI: 10.1002/biot.201400301
    Microbial lipases are popular biocatalysts due to their ability to catalyse diverse reactions such as hydrolysis, esterification, and acidolysis. Lipases function efficiently on various substrates in aqueous and non-aqueous media. Lipases are chemo-, regio-, and enantio-specific, and are useful in various industries, including those manufacturing food, detergents, and pharmaceuticals. A large number of lipases from fungal and bacterial sources have been isolated and purified to homogeneity. This success is attributed to the development of both conventional and novel purification techniques. This review highlights the use of these techniques in lipase purification, including conventional techniques such as: (i) ammonium sulphate fractionation; (ii) ion-exchange; (iii) gel filtration and affinity chromatography; as well as novel techniques such as (iv) reverse micellar system; (v) membrane processes; (vi) immunopurification; (vi) aqueous two-phase system; and (vii) aqueous two-phase floatation. A summary of the purification schemes for various bacterial and fungal lipases are also provided.
    Matched MeSH terms: Fungal Proteins/chemistry
  5. Inhibition and kinetic studies of cellulose- and hemicellulose-degrading enzymes of Ganoderma boninense by naturally occurring phenolic compounds
    Surendran A, Siddiqui Y, Ali NS, Manickam S
    J Appl Microbiol, 2018 Jun;124(6):1544-1555.
    PMID: 29405525 DOI: 10.1111/jam.13717
    AIM: Ganoderma sp, the causal pathogen of the basal stem rot (BSR) disease of oil palm, secretes extracellular hydrolytic enzymes. These play an important role in the pathogenesis of BSR by nourishing the pathogen through the digestion of cellulose and hemicellulose of the host tissue. Active suppression of hydrolytic enzymes secreted by Ganoderma boninense by various naturally occurring phenolic compounds and estimation of their efficacy on pathogen suppression is focused in this study.

    METHODS AND RESULTS: Ten naturally occurring phenolic compounds were assessed for their inhibitory effect on the hydrolytic enzymes of G. boninense. The enzyme kinetics (Vmax and Km ) and the stability of the hydrolytic enzymes were also characterized. The selected compounds had shown inhibitory effect at various concentrations. Two types of inhibitions namely uncompetitive and noncompetitive were observed in the presence of phenolic compounds. Among all the phenolic compounds tested, benzoic acid was the most effective compound suppressive to the growth and production of hydrolytic enzymes secreted by G. boninense. The phenolic compounds as inhibitory agents can be a better replacement for the metal ions which are known as conventional inhibitors till date. The three hydrolytic enzymes were stable in a wide range of pH and temperature.

    CONCLUSION: These findings highlight the efficacy of the applications of phenolic compounds to control Ganoderma.

    SIGNIFICANCE AND IMPACT OF THE STUDY: The study has proved a replacement for chemical controls of G. boninense with naturally occurring phenolic compounds.

    Matched MeSH terms: Fungal Proteins/chemistry
  6. Fulltext Solution structures, dynamics, and ice growth inhibitory activity of peptide fragments derived from an antarctic yeast protein
    Shah SH, Kar RK, Asmawi AA, Rahman MB, Murad AM, Mahadi NM, et al.
    PLoS One, 2012;7(11):e49788.
    PMID: 23209600 DOI: 10.1371/journal.pone.0049788
    Exotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group isolated the Antarctic yeast Glaciozyma antarctica that expresses antifreeze protein to assist it in its survival mechanism at sub-zero temperatures. The protein is unique and novel, indicated by its low sequence homology compared to those of other AFPs. We explore the structure-function relationship of G. antarctica AFP using various approaches ranging from protein structure prediction, peptide design and antifreeze activity assays, nuclear magnetic resonance (NMR) studies and molecular dynamics simulation. The predicted secondary structure of G. antarctica AFP shows several α-helices, assumed to be responsible for its antifreeze activity. We designed several peptide fragments derived from the amino acid sequences of α-helical regions of the parent AFP and they also showed substantial antifreeze activities, below that of the original AFP. The relationship between peptide structure and activity was explored by NMR spectroscopy and molecular dynamics simulation. NMR results show that the antifreeze activity of the peptides correlates with their helicity and geometrical straightforwardness. Furthermore, molecular dynamics simulation also suggests that the activity of the designed peptides can be explained in terms of the structural rigidity/flexibility, i.e., the most active peptide demonstrates higher structural stability, lower flexibility than that of the other peptides with lower activities, and of lower rigidity. This report represents the first detailed report of downsizing a yeast AFP into its peptide fragments with measurable antifreeze activities.
    Matched MeSH terms: Fungal Proteins/chemistry*
  7. Studies of reaction parameters on synthesis of Citronellyl laurate ester via immobilized Candida rugosa lipase in organic media
    Serri NA, Kamaruddin AH, Long WS
    Bioprocess Biosyst Eng, 2006 Oct;29(4):253-60.
    PMID: 16868763
    Immobilized Candida rugosa lipase was used for the synthesis of citronellyl laurate from citronellol and lauric acid. Screening of different types of support (Amberlite MB-1 and Celite) for immobilization of lipase and solvent (n-hexane, n-heptane, and iso-octane) and optimization of reaction conditions, such as catalyst loading, effect of substrates molar ratio and temperature, have been studied. The maximum enzyme activity was obtained at 310 K. The immobilized C. rugosa lipase onto Amberlite MB-1 support was found to be the best support with a conversion of 89% of citronellyl laurate ester in iso-octane compared to Celite 545. Deactivation of C. rugosa lipase at 313, 318 and 323 K were observed. Ordered bi bi mechanism with dead end complex of lauric acid was found to fit the initial rate data and the kinetic parameters were obtained by non-linear regression analysis.
    Matched MeSH terms: Fungal Proteins/chemistry*
  8. The effect of water activity on modified lipase during esterification
    Salleh AB, Taib M, Basri M, Ampon K, Yunus WM, Razak CN
    Ann N Y Acad Sci, 1996 Oct 12;799:328-31.
    PMID: 8958097
    Matched MeSH terms: Fungal Proteins/chemistry
  9. Thermokinetic comparison of trypan blue decolorization by free laccase and fungal biomass
    Razak NN, Annuar MS
    Appl Biochem Biotechnol, 2014 Mar;172(6):2932-44.
    PMID: 24464534 DOI: 10.1007/s12010-014-0731-7
    Free laccase and fungal biomass from white-rot fungi were compared in the thermokinetics study of the laccase-catalyzed decolorization of an azo dye, i.e., Trypan Blue. The decolorization in both systems followed a first-order kinetics. The apparent first-order rate constant, k1', value increases with temperature. Apparent activation energy of decolorization was similar for both systems at ∼ 22 kJ mol(-1), while energy for laccase inactivation was 18 kJ mol(-1). Although both systems were endothermic, fungal biomass showed higher enthalpy, entropy, and Gibbs free energy changes for the decolorization compared to free laccase. On the other hand, free laccase showed reaction spontaneity over a wider range of temperature (ΔT = 40 K) as opposed to fungal biomass (ΔT = 15 K). Comparison of entropy change (ΔS) values indicated metabolism of the dye by the biomass.
    Matched MeSH terms: Fungal Proteins/chemistry*
  10. Sequence and structural investigation of a novel psychrophilic α-amylase from Glaciozyma antarctica PI12 for cold-adaptation analysis
    Ramli AN, Azhar MA, Shamsir MS, Rabu A, Murad AM, Mahadi NM, et al.
    J Mol Model, 2013 Aug;19(8):3369-83.
    PMID: 23686283 DOI: 10.1007/s00894-013-1861-5
    A novel α-amylase was isolated successfully from Glaciozyma antarctica PI12 using DNA walking and reverse transcription-polymerase chain reaction (RT-PCR) methods. The structure of this psychrophilic α-amylase (AmyPI12) from G. antarctica PI12 has yet to be studied in detail. A 3D model of AmyPI12 was built using a homology modelling approach to search for a suitable template and to generate an optimum target-template alignment, followed by model building using MODELLER9.9. Analysis of the AmyPI12 model revealed the presence of binding sites for a conserved calcium ion (CaI), non-conserved calcium ions (CaII and CaIII) and a sodium ion (Na). Compared with its template-the thermostable α-amylase from Bacillus stearothermophilus (BSTA)-the binding of CaII, CaIII and Na ions in AmyPI12 was observed to be looser, which suggests that the low stability of AmyPI12 allows the protein to work at different temperature scales. The AmyPI12 amino acid sequence and model were compared with thermophilic α-amylases from Bacillus species that provided the highest structural similarities with AmyPI12. These comparative studies will enable identification of possible determinants of cold adaptation.
    Matched MeSH terms: Fungal Proteins/chemistry*
  11. Fulltext Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12
    Ramli AN, Mahadi NM, Rabu A, Murad AM, Bakar FD, Illias RM
    Microb Cell Fact, 2011;10:94.
    PMID: 22050784 DOI: 10.1186/1475-2859-10-94
    Cold-adapted enzymes are proteins produced by psychrophilic organisms that display a high catalytic efficiency at extremely low temperatures. Chitin consists of the insoluble homopolysaccharide β-(1, 4)-linked N-acetylglucosamine, which is the second most abundant biopolymer found in nature. Chitinases (EC 3.2.1.14) play an important role in chitin recycling in nature. Biodegradation of chitin by the action of cold-adapted chitinases offers significant advantages in industrial applications such as the treatment of chitin-rich waste at low temperatures, the biocontrol of phytopathogens in cold environments and the biocontrol of microbial spoilage of refrigerated food.
    Matched MeSH terms: Fungal Proteins/chemistry*
  12. Fulltext Saccharification of rice straw by cellulase from a local Trichoderma harzianum SNRS3 for biobutanol production
    Rahnama N, Foo HL, Abdul Rahman NA, Ariff A, Md Shah UK
    BMC Biotechnol, 2014;14:103.
    PMID: 25496491 DOI: 10.1186/s12896-014-0103-y
    Rice straw has shown to be a promising agricultural by-product in the bioconversion of biomass to value-added products. Hydrolysis of cellulose, a main constituent of lignocellulosic biomass, is a requirement for fermentable sugar production and its subsequent bioconversion to biofuels such as biobutanol. The high cost of commercial enzymes is a major impediment to the industrial application of cellulases. Therefore, the use of local microbial enzymes has been suggested. Trichoderma harzianum strains are potential CMCase and β-glucosidase producers. However, few researches have been reported on cellulase production by T. harzianum and the subsequent use of the crude cellulase for cellulose enzymatic hydrolysis. For cellulose hydrolysis to be efficiently performed, the presence of the whole set of cellulase components including exoglucanase, endoglucanase, and β-glucosidase at a considerable concentration is required. Biomass recalcitrance is also a bottleneck in the bioconversion of agricultural residues to value-added products. An effective pretreatment could be of central significance in the bioconversion of biomass to biofuels.
    Matched MeSH terms: Fungal Proteins/chemistry*
  13. Enzymatic Production of Bioxylitol from Sawdust Hydrolysate: Screening of Process Parameters
    Rafiqul IS, Sakinah AM, Zularisam AW
    Appl Biochem Biotechnol, 2015 Jun;176(4):1071-83.
    PMID: 25904039 DOI: 10.1007/s12010-015-1630-2
    Xylose-rich sawdust hydrolysate can be an economic substrate for the enzymatic production of xylitol, a specialty product. It is important to identify the process factors influencing xylitol production. This research aimed to screen the parameters significantly affecting bioxylitol synthesis from wood sawdust by xylose reductase (XR). Enzymatic bioxylitol production was conducted to estimate the effect of different variables reaction time (2-18 h), temperature (20-70 °C), pH (4.0-9.0), NADPH (1.17-5.32 g/L), and enzyme concentration (2-6 %) on the yield of xylitol. Fractional factorial design was followed to identify the key process factors. The screening design identified that time, temperature, and pH are the most significant factors influencing bioxylitol production among the variables with the values of 12 h, 35 °C, and 7.0, respectively. These conditions led to a xylitol yield of 71 % (w/w). This is the first report on the statistical screening of process variables influencing enzyme-based bioxylitol production from lignocellulosic biomass.
    Matched MeSH terms: Fungal Proteins/chemistry*
  14. Extraction of nanosilica from oil palm leaves and its application as support for lipase immobilization
    Onoja E, Chandren S, Razak FIA, Wahab RA
    J Biotechnol, 2018 Oct 10;283:81-96.
    PMID: 30063951 DOI: 10.1016/j.jbiotec.2018.07.036
    The study reports the preparation of a composite consisting of magnetite coated with nanosilica extracted from oil palm leaves (OPL) ash as nanosupports for immobilization of Candida rugosa lipase (CRL) and its application for the synthesis of butyl butyrate. Results of immobilization parameters showed that ∼ 80% of CRL (84.5 mg) initially offered was immobilized onto the surface of the nanosupports to yield a maximum protein loading and specific activity of 67.5 ± 0.72 mg/g and 320.8 ± 0.42 U/g of support, respectively. Surface topography, morphology as well as information on surface composition obtained by Raman spectroscopy, atomic force microscopy, field emission scanning electron microscopy and transmission electron microscopy showed that CRL was successfully immobilized onto the nanosupports, affirming its biocompatibility. Under optimal conditions (3.5 mg/mL protein loading, at 45 ℃, 3 h and molar ratio 2:1 (1-butanol:n-butyric acid) the CRL/Gl-A-SiO2-MNPs gave a maximum yield of 94 ± 0.24% butyl butyrate as compared to 84 ± 0.32% in the lyophilized CRL. CRL/Gl-A-SiO2-MNPs showed an extended operational stability, retaining 50% of its initial activity after 17 consecutive esterification cycles. The results indicated that OPL derived nanosilica coated on magnetite can potentially be employed as carrier for lipase immobilization in replacement of the non-renewable conventionalsilica sources.
    Matched MeSH terms: Fungal Proteins/chemistry
  15. Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
    Noorbatcha IA, Sultan AM, Salleh HM, Amid A
    Protein J, 2013 Apr;32(4):309-16.
    PMID: 23636517 DOI: 10.1007/s10930-013-9489-y
    Molecular dynamics simulation was used to study the dynamic differences between native Aspergillus niger PhyA phytase and a mutant with 20 % greater thermostability. Atomic root mean square deviation, radius of gyration, and number of hydrogen bonds and salt bridges are examined to determine thermostability factors. The results suggest that, among secondary structure elements, loops have the most impact on the thermal stability of A. niger phytase. In addition, the location rather than the number of hydrogen bonds is found to have an important contribution to thermostability. The results also show that salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly.
    Matched MeSH terms: Fungal Proteins/chemistry*
  16. A combination of evolutionary trace method, molecular surface accessibility and hydrophobicity analysis to design a high hydrophobicity laccase
    Mohamad SB, Ong AL, Khairuddin RF, Ripen AM
    In Silico Biol. (Gedrukt), 2010;10(3):145-53.
    PMID: 22430288 DOI: 10.3233/ISB-2010-0423
    Laccases are industrially attractive enzymes and their applications have expanded to the field of bioremediation. The challenge of today's biotechnology in enzymatic studies is to design enzymes that not only have a higher activity but are also more stable and could fit well with the condition requirements. Laccases are known to oxidize non-natural substrates like polycyclic aromatic hydrocarbons (PAHs). We suppose by increasing the hydrophobicity of laccase, it would increase the chance of the enzyme to meet the hydrophobic substrates in a contamination site, therefore increasing the bioremediation efficacy of PAHs from environment. In this attempt, the applications of evolutionary trace (ET), molecular surface accessibility and hydrophobicity analysis on laccase sequences and laccase's crystal structure (1KYA) are described for optimal design of an enzyme with higher hydrophobicity. Our analysis revealed that Q23A, Q45I, N141A, Q237V, N262L, N301V, N331A, Q360L and Q482A could be promising exchanges to be tested in mutagenesis experiments.
    Matched MeSH terms: Fungal Proteins/chemistry*
  17. Functional and structural analyses of an expansin-like protein from the antarctic yeast Glaciozyma antarctica PI12 reveal strategies of nutrient scavenging in the sea ice environment
    Mohamad Nor N, Hashim NHF, Quay DHX, Mahadi NM, Illias RM, Abu Bakar FD, et al.
    Int J Biol Macromol, 2020 Feb 01;144:231-241.
    PMID: 31843615 DOI: 10.1016/j.ijbiomac.2019.12.099
    Genome data mining of the Antarctic yeast, Glaciozyma antarctica PI12 revealed an expansin-like protein encoding sequence (GaEXLX1). The GaEXLX1 protein is 24.8 kDa with a high alkaline pI of 9.81. Homology modeling of GaEXLX1 showed complete D1 and D2 domains of a conventional expansin. The protein exhibited 36% sequence similarity to Clavibacter michiganensis EXLX1 (PDB: 4JCW). Subsequently, a recombinant GaEXLX1 protein was produced using Escherichia coli expression system. Incubation with Avicel, filter paper and cotton fiber showed that the protein can disrupt the surface of crystalline and pure cellulose, suggesting a cell wall modification activity usually exhibited by expansin-like proteins. Binding assays displayed that GaEXLX1 can bind to polymeric substrates, including those postulated to be present in the sea ice ecosystem such as crab chitin and moss lichenan. GaEXLX1 may assist in the recognition and loosening of these substrates in the sea ice prior to hydrolysis by other extracellular enzymes. Similar loosening mechanism to classical expansin-like protein has been postulated for this psychrophilic protein based on several conserved residues of GaEXLX1 involved in binding interaction identified by docking analyses.
    Matched MeSH terms: Fungal Proteins/chemistry
  18. Fulltext Anti-angiotensin converting enzyme (ACE) proteins from mycelia of Ganoderma lucidum (Curtis) P. Karst
    Mohamad Ansor N, Abdullah N, Aminudin N
    BMC Complement Altern Med, 2013;13:256.
    PMID: 24093919 DOI: 10.1186/1472-6882-13-256
    Ganoderma lucidum has been purported as a potent remedy in the treatment and prevention of several ailments, including hypertension. This study aimed to explore the anti-ACE potential of protein fractions from the mycelia of G. lucidum.
    Matched MeSH terms: Fungal Proteins/chemistry
  19. Synthesis of conjugated linoleic acid-rich triacylglycerols by immobilized mutant lipase with excellent capability and recyclability
    Lian W, Li D, Zhang L, Wang W, Faiza M, Tan CP, et al.
    Enzyme Microb Technol, 2018 Oct;117:56-63.
    PMID: 30037552 DOI: 10.1016/j.enzmictec.2018.06.007
    Conjugated linoleic acid (CLA)-rich triacylglycerols (TAG) have received significant attention owing to their health promoting properties. In this study, CLA-rich TAG were successfully synthesized by an immobilized mutant lipase (MAS1-H108A)-catalyzed esterification of CLA-rich fatty acids and glycerol under vacuum. MAS1-H108A was first immobilized onto ECR1030 resin. Results showed that the lipase/support ratio of 41 mg/g was suitable for the immobilization and the thermostability of immobilized MAS1-H108A was greatly enhanced. Subsequently, the immobilized MAS1-H108A was employed for the synthesis of CLA-rich TAG and 95.21% TAG with 69.19% CLA was obtained under the optimized conditions. The TAG content (95.21%) obtained by immobilized MAS1-H108A is the reported highest value thus far, which was significantly higher than that (9.26%) obtained by Novozym 435 under the same conditions. Although the TAG content comparable to the results obtained in this study could also be obtained by Novozym 435, the used enzyme amount is approximately 5-fold of the immobilized MAS1-H108A. Additionally, the immobilized MAS1-H108A exhibited excellent recyclability during esterification retaining 95.11% of its initial activity after 10 batches. Overall, such immobilized mutant lipase with superior esterification activity and recyclability has the potential to be used in oils and fats industry.
    Matched MeSH terms: Fungal Proteins/chemistry
  20. Proteomic analysis of antihypertensive proteins in edible mushrooms
    Lau CC, Abdullah N, Shuib AS, Aminudin N
    J Agric Food Chem, 2012 Dec 19;60(50):12341-8.
    PMID: 23190208 DOI: 10.1021/jf3042159
    Mushrooms are high in protein content, which makes them potentially a good source of antihypertensive peptides. Among the mushrooms tested, protein extracts from Pleurotus cystidiosus (E1Pc and E5Pc) and Agaricus bisporus (E1Ab and E3Ab) had high levels of antihypertensive activity. The protein extracts were fractionated by reverse-phase high-performance liquid chromatography (RPHPLC) into six fractions. Fraction 3 from E5Pc (E5PcF3) and fraction 6 from E3Ab (E3AbF6) had the highest antihypertensive activities. SDS-PAGE analysis showed E5PcF3 consisted mainly of low molecular weight proteins, whereas E3AbF6 contained a variety of high to low molecular weight proteins. There were 22 protein clusters detected by SELDI-TOF-MS analysis with five common peaks found in E5PcF3 and E3AbF6, which had m/z values in the range of 3940-11413. This study suggests that the antihypertensive activity in the two mushroom species could be due to proteins with molecular masses ranging from 3 to 10 kDa.
    Matched MeSH terms: Fungal Proteins/chemistry
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