Displaying publications 1 - 20 of 38 in total

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  1. Fulltext Chemoenzymatic epoxidation of alkenes and reusability study of the phenylacetic acid
    Abdulmalek E, Arumugam M, Mizan HN, Abdul Rahman MB, Basri M, Salleh AB
    ScientificWorldJournal, 2014;2014:756418.
    PMID: 24587751 DOI: 10.1155/2014/756418
    Here, we focused on a simple enzymatic epoxidation of alkenes using lipase and phenylacetic acid. The immobilised Candida antarctica lipase B, Novozym 435 was used to catalyse the formation of peroxy acid instantly from hydrogen peroxide (H2O2) and phenylacetic acid. The peroxy phenylacetic acid generated was then utilised directly for in situ oxidation of alkenes. A variety of alkenes were oxidised with this system, resulting in 75-99% yield of the respective epoxides. On the other hand, the phenylacetic acid was recovered from the reaction media and reused for more epoxidation. Interestingly, the waste phenylacetic acid had the ability to be reused for epoxidation of the 1-nonene to 1-nonene oxide, giving an excellent yield of 90%.
    Matched MeSH terms: Fungal Proteins/chemistry
  2. 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*
  3. 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*
  4. Fulltext Development of an amperometric-based glucose biosensor to measure the glucose content of fruit
    Ang LF, Por LY, Yam MF
    PLoS One, 2015;10(3):e0111859.
    PMID: 25789757 DOI: 10.1371/journal.pone.0111859
    An amperometric enzyme-electrode was introduced where glucose oxidase (GOD) was immobilized on chitosan membrane via crosslinking, and then fastened on a platinum working electrode. The immobilized enzyme showed relatively high retention activity. The activity of the immobilized enzyme was influenced by its loading, being suppressed when more than 0.6 mg enzyme was used in the immobilization. The biosensor showing the highest response to glucose utilized 0.21 ml/cm2 thick chitosan membrane. The optimum experimental conditions for the biosensors in analysing glucose dissolved in 0.1 M phosphate buffer (pH 6.0) were found to be 35°C and 0.6 V applied potential. The introduced biosensor reached a steady-state current at 60 s. The apparent Michaelis-Menten constant ([Formula: see text]) of the biosensor was 14.2350 mM, and its detection limit was 0.05 mM at s/n > 3, determined experimentally. The RSD of repeatability and reproducibility of the biosensor were 2.30% and 3.70%, respectively. The biosensor was showed good stability; it retained ~36% of initial activity after two months of investigation. The performance of the biosensors was evaluated by determining the glucose content in fruit homogenates. Their accuracy was compared to that of a commercial glucose assay kit. There was no significance different between two methods, indicating the introduced biosensor is reliable.
    Matched MeSH terms: Fungal Proteins/chemistry*
  5. Fulltext Imidazole-rich copper peptides as catalysts in xenobiotic degradation
    Begum SZ, Nizam NSM, Muhamad A, Saiman MI, Crouse KA, Abdul Rahman MB
    PLoS One, 2020;15(11):e0238147.
    PMID: 33147237 DOI: 10.1371/journal.pone.0238147
    Laccases, oxidative copper-enzymes found in fungi and bacteria were used as the basis in the design of nona- and tetrapeptides. Laccases are known to be excellent catalysts for the degradation of phenolic xenobiotic waste. However, since solvent extraction of laccases is environmentally-unfriendly and yields obtained are low, they are less preferred compared to synthetic catalysts. The histidine rich peptides were designed based on the active site of laccase extracted from Trametes versicolor through RCSB Protein Data Bank, LOMETS and PyMol software. The peptides were synthesized using Fmoc-solid phase peptide synthesis (SPPS) with 30-40% yield. These peptides were purified and characterized using LC-MS (purities >75%), FTIR and NMR spectroscopy. Synthesized copper(II)-peptides were crystallized and then analyzed spectroscopically. Their structures were elucidated using 1D and 2D NMR. Standards (o,m,p-cresol, 2,4-dichlorophenol) catalysed using laccase from Trametes versicolor (0.66 U/mg) were screened under different temperatures and stirring rate conditions. After optimizing the degradation of the standards with the best reaction conditions reported herein, medications with phenolic and aromatic structures such as ibuprofen, paracetamol (acetaminophen), salbutamol, erythromycin and insulin were screened using laccase (positive control), apo-peptides and copper-peptides. Their activities evaluated using GC-MS, were compared with those of peptide and copper-peptide catalysts. The tetrapeptide was found to have the higher degradation activity towards salbutamol (96.8%) compared with laccase at 42.8%. Ibuprofen (35.1%), salbutamol (52.9%) and erythromycin (49.7%) were reported to have the highest degradation activities using Cu-tetrapeptide as catalyst when compared with the other medications. Consequently, o-cresol (84%) was oxidized by Tp-Cu while the apo-peptides failed to oxidize the cresols. Copper(II)-peptides were observed to have higher catalytic activity compared to their parent peptides and the enzyme laccase for xenobiotic degradation.
    Matched MeSH terms: Fungal Proteins/chemistry
  6. Fulltext Synthesis, spectroscopic investigations (X-ray, NMR and TD-DFT), antimicrobial activity and molecular docking of 2,6-bis(hydroxy(phenyl)methyl)cyclohexanone
    Barakat A, Ghabbour HA, Al-Majid AM, Soliman SM, Ali M, Mabkhot YN, et al.
    Molecules, 2015;20(7):13240-63.
    PMID: 26197312 DOI: 10.3390/molecules200713240
    The synthesis of 2,6-bis(hydroxy(phenyl)methyl)cyclohexanone 1 is described. The molecular structure of the title compound 1 was confirmed by NMR, FT-IR, MS, CHN microanalysis, and X-ray crystallography. The molecular structure was also investigated by a set of computational studies and found to be in good agreement with the experimental data obtained from the various spectrophotometric techniques. The antimicrobial activity and molecular docking of the synthesized compound was investigated.
    Matched MeSH terms: Fungal Proteins/chemistry*
  7. Fulltext Enhancing the Bioconversion of Azelaic Acid to Its Derivatives by Response Surface Methodology
    Khairudin N, Basri M, Fard Masoumi HR, Samson S, Ashari SE
    Molecules, 2018 Feb 13;23(2).
    PMID: 29438284 DOI: 10.3390/molecules23020397
    Azelaic acid (AzA) and its derivatives have been known to be effective in the treatment of acne and various cutaneous hyperpigmentary disorders. The esterification of azelaic acid with lauryl alcohol (LA) to produce dilaurylazelate using immobilized lipase B from Candida antarctica (Novozym 435) is reported. Response surface methodology was selected to optimize the reaction conditions. A well-fitting quadratic polynomial regression model for the acid conversion was established with regards to several parameters, including reaction time and temperature, enzyme amount, and substrate molar ratios. The regression equation obtained by the central composite design of RSM predicted that the optimal reaction conditions included a reaction time of 360 min, 0.14 g of enzyme, a reaction temperature of 46 °C, and a molar ratio of substrates of 1:4.1. The results from the model were in good agreement with the experimental data and were within the experimental range (R² of 0.9732).The inhibition zone can be seen at dilaurylazelate ester with diameter 9.0±0.1 mm activities against Staphylococcus epidermidis S273. The normal fibroblasts cell line (3T3) was used to assess the cytotoxicity activity of AzA and AzA derivative, which is dilaurylazelate ester. The comparison of the IC50 (50% inhibition of cell viability) value for AzA and AzA derivative was demonstrated. The IC50 value for AzA was 85.28 μg/mL, whereas the IC50 value for AzA derivative was more than 100 μg/mL. The 3T3 cell was still able to survive without any sign of toxicity from the AzA derivative; thus, it was proven to be non-toxic in this MTT assay when compared with AzA.
    Matched MeSH terms: Fungal Proteins/chemistry*
  8. 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*
  9. Bioinformatics survey of the metal usage by psychrophilic yeast Glaciozyma antarctica PI12
    Foong PM, Abedi Karjiban R, Normi YM, Salleh AB, Abdul Rahman MB
    Metallomics, 2015 Jan;7(1):156-64.
    PMID: 25412156 DOI: 10.1039/c4mt00163j
    Metal ions are one of the essential elements which are extensively involved in many cellular activities. With rapid advancements in genome sequencing techniques, bioinformatics approaches have provided a promising way to extract functional information of a protein directly from its primary structure. Recent findings have suggested that the metal content of an organism can be predicted from its complete genome sequences. Characterizing the biological metal usage of cold-adapted organisms may help to outline a comprehensive understanding of the metal-partnerships between the psychrophile and its adjacent environment. The focus of this study is targeted towards the analysis of the metal composition of a psychrophilic yeast Glaciozyma antarctica PI12 isolated from sea ice of Antarctica. Since the cellular metal content of an organism is usually reflected in the expressed metal-binding proteins, the putative metal-binding sequences from G. antarctica PI12 were identified with respect to their sequence homologies, domain compositions, protein families and cellular distribution. Most of the analyses revealed that the proteome was enriched with zinc, and the content of metal decreased in the order of Zn > Fe > Mg > Mn, Ca > Cu. Upon comparison, it was found that the metal compositions among yeasts were almost identical. These observations suggested that G. antarctica PI12 could have inherited a conserved trend of metal usage similar to modern eukaryotes, despite its geographically isolated habitat.
    Matched MeSH terms: Fungal Proteins/chemistry
  10. Interesterification of engkabang (Shorea macrophylla) fat--canola oil blend with lipase from Candida antarctica to simulate the properties of lard
    Illiyin MR, Marikkar JM, Loke MK, Shuhaimi M, Mahiran B, Miskandar MS
    J Oleo Sci, 2014;63(1):39-46.
    PMID: 24389796
    A study was carried out to compare the composition and thermal properties of lard (LD) and engkabang fat (EF) - canola oil (CaO) blend interesterified with Candida antartica lipase (C. antartica). A fat blend EF-4 (40% EF in CaO) was prepared and interesterified using C. antartica lipase at 60°C for different time intervals (6 h, 12 h and 24 h) with 200 rpm agitation. The fat blends before and after interesterification were compared to LD with respect to their slip melting points (SMP), fatty acid and triacyglycerol (TAG) compositions, melting, solidification and polymorphic properties. Result showed that the slip melting point (SMP) of the fat blend interesterified for 6 h was the closest to that of LD. The solid fat content (SFC) values of fat blends interesterified for 12 and 24 h were found to become equal to those of LD within the temperature range of 0 to 20°C. In addition, all three interesterified blends had SFC values similar to those of LD within the temperature range of 30-40°C. According to thermal analysis, the transition of the fat blend interesterified for 24 h appearing at -2.39°C was similar to the low melting thermal transition of LD and the transition of the fat blend interesterified for 12 h appearing at 26.25°C was similar to the high melting thermal transition of LD. However, there is no compatibility between LD and all three interesterified blends with regard to polymorphic behaviour.
    Matched MeSH terms: Fungal Proteins/chemistry*
  11. 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*
  12. 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*
  13. Comparative SELDI-TOF-MS profiling of low-molecular-mass proteins from Lignosus rhinocerus (Cooke) Ryvarden grown under stirred and static conditions of liquid fermentation
    Lau BF, Aminudin N, Abdullah N
    J Microbiol Methods, 2011 Oct;87(1):56-63.
    PMID: 21801760 DOI: 10.1016/j.mimet.2011.07.005
    Mushrooms are considered as important source of biologically active compounds which include low-molecular-mass protein/peptides (LMMP). In this study, we attempted to profile the LMMP from Lignosus rhinocerus, a wild medicinal mushroom, grown by static cultures (SC) and in stirred tank reactor (STR). Crude water extract (CWE) and protein fractions were profiled using H50 ProteinChip® arrays and SELDI-TOF-MS. Three protein peaks of 5.8, 6.9 and 9.1 kDa were found to be common to spectra of L. rhinocerus CWE from both culture conditions. Partial protein purification has resulted in detection of more peaks in the spectra of protein fractions. For protein fractions of L. rhinocerus cultured in STR, most peaks were observed in the range of 3-8 kDa whereas some peaks with molecular mass up to 14.3 kDa were noted in spectra of protein fractions from SC. Our results have demonstrated the optimization of profiling method using SELDI-TOF-MS for fungal LMMP.
    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. 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
  16. 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
  17. Response Surface Methodology Modelling of an Aqueous Two-Phase System for Purification of Protease from Penicillium candidum (PCA 1/TT031) under Solid State Fermentation and Its Biochemical Characterization
    Alhelli AM, Abdul Manap MY, Mohammed AS, Mirhosseini H, Suliman E, Shad Z, et al.
    Int J Mol Sci, 2016 Nov 11;17(11).
    PMID: 27845736
    Penicillium candidum (PCA 1/TT031) synthesizes different types of extracellular proteases. The objective of this study is to optimize polyethylene glycol (PEG)/citrate based on an aqueous two-phase system (ATPS) and Response Surface Methodology (RSM) to purify protease from Penicillium candidum (PCA 1/TT031). The effects of different PEG molecular weights (1500-10,000 g/mol), PEG concentration (9%-20%), concentrations of NaCl (0%-10%) and the citrate buffer (8%-16%) on protease were also studied. The best protease purification could be achieved under the conditions of 9.0% (w/w) PEG 8000, 5.2% NaCl, and 15.9% sodium citrate concentration, which resulted in a one-sided protease partitioning for the bottom phase with a partition coefficient of 0.2, a 6.8-fold protease purification factor, and a yield of 93%. The response surface models displayed a significant (p ≤ 0.05) response which was fit for the variables that were studied as well as a high coefficient of determination (R²). Similarly, the predicted and observed values displayed no significant (p > 0.05) differences. In addition, our enzyme characterization study revealed that Penicillium candidum (PCA 1/TT031) produced a slight neutral protease with a molecular weight between 100 and 140 kDa. The optimal activity of the purified enzyme occurred at a pH of 6.0 and at a temperature of 50 °C. The stability between different pH and temperature ranges along with the effect of chemical metal ions and inhibitors were also studied. Our results reveal that the purified enzyme could be used in the dairy industry such as in accelerated cheese ripening.
    Matched MeSH terms: Fungal Proteins/chemistry
  18. Fulltext Novel Safranin-Tinted Candida rugosa Lipase Nanoconjugates Reagent for Visualizing Latent Fingerprints on Stainless Steel Knives Immersed in a Natural Outdoor Pond
    Azman AR, Mahat NA, Abdul Wahab R, Abdul Razak FI, Hamzah HH
    Int J Mol Sci, 2018 May 25;19(6).
    PMID: 29799469 DOI: 10.3390/ijms19061576
    Waterways are popular locations for the disposition of criminal evidence because the recovery of latent fingerprints from such evidence is difficult. Currently, small particle reagent is a method often used to visualize latent fingerprints containing carcinogenic and hazardous compounds. This study proposes an eco-friendly, safranin-tinted Candida rugosa lipase (triacylglycerol ester hydrolysis EC 3.1.1.3) with functionalized carbon nanotubes (CRL-MWCNTS/GA/SAF) as an alternative reagent to the small particle reagent. The CRL-MWCNTS/GA/SAF reagent was compared with the small particle reagent to visualize groomed, full fingerprints deposited on stainless steel knives which were immersed in a natural outdoor pond for 30 days. The quality of visualized fingerprints using the new reagent was similar (modified-Centre for Applied Science and Technology grade: 4; p > 0.05) to small particle reagent, even after 15 days of immersion. Despite the slight decrease in quality of visualized fingerprints using the CRL-MWCNTS/GA/SAF on the last three immersion periods, the fingerprints remained forensically identifiable (modified-Centre for Applied Science and Technology grade: 3). The possible chemical interactions that enabled successful visualization is also discussed. Thus, this novel reagent may provide a relatively greener alternative for the visualization of latent fingerprints on immersed non-porous objects.
    Matched MeSH terms: Fungal Proteins/chemistry*
  19. Surface Decoration of Selenium Nanoparticles by Proteins from the Culinary-Medicinal Shiitake Mushroom, Lentinus edodes (Agaricomycetes), for Enhanced Fibrinolytic Activity
    Ali SM, Raman J, Lakshmanan H, Ling TC, Phan CW, Tan YS, et al.
    Int J Med Mushrooms, 2018;20(11):1021-1030.
    PMID: 30806227 DOI: 10.1615/IntJMedMushrooms.2018028307
    Lentinus edodes (shiitake mushroom) has exhibited fibrinolytic activity. We synthesized and characterized selenium nanoparticles (SeNPs) using protein precipitated from the mushroom. We also investigated the fibrinolytic activity of the SeNPs. The proteins from a crude extract of L. edodes were recovered through the use of aqueous 2-phase separation, and these we used as the capping agent in SeNP biosynthesis. We characterized the SeNPs using UV-visible spectrophotometry, field emission scanning electron microscopy (FESEM), energy dispersive X-ray (EDX), transmission electron microscopy (TEM), particle size distribution analysis, and Fourier transform infrared spectroscopy (FT-IR). The fibrinolytic capability of the SeNPs was tested through an in vitro fibrin plate assay. The UV-visible spectra showed maximal absorbance at 220 nm. FESEM images showed that the SeNPs were dispersed and did not clump. The TEM images revealed a spherical shape and average size of the SeNPs. The particle size distribution analysis confirmed the mean size of the SeNPs at 64.53 nm. A strong signal for the presence of selenium was observed in the EDX analysis. The FT-IR spectrum revealed the involvement of protein functional groups in the reduction of sel-enite. Overall, the SeNPs capped with protein from shiitake mushroom were effective as an in vitro fibrinolytic agent.
    Matched MeSH terms: Fungal Proteins/chemistry
  20. Characterization, optimization and stability studies on Candida rugosa lipase supported on nanocellulose reinforced chitosan prepared from oil palm biomass
    Elias N, Chandren S, Razak FIA, Jamalis J, Widodo N, Wahab RA
    Int J Biol Macromol, 2018 Jul 15;114:306-316.
    PMID: 29578010 DOI: 10.1016/j.ijbiomac.2018.03.095
    The contribution of chitosan/nanocellulose (CS-NC) to the enzymatic activity of Candida rugosa lipase covalently bound on the surface of CS-NC (CRL/CS-NC) was investigated. Cellulosic material from oil palm frond leaves (OPFL) were bleached, alkaline treated and acid hydrolyzed to obtain the purified NC and used as nano-fillers in CS. XRD, Raman spectroscopy and optical fluorescence microscopic analyses revealed existence of strong hydrogen bonds between CS and the NC nanofillers. The CRLs were successfully conjugated to the surface of the CS-NC supports via imine bonds that occurred through a Schiff's based mechanism. Process parameters for the immobilization of CRL were assessed for factors temperature, concentration of glutaraldehyde and pH, to afford the highest enzyme activity to achieve maximum conversion of butyl butyrate within 3h of incubation. Conversion as high as 88% was reached under an optimized condition of 25°C, 0.3% glutaraldehyde concentration and buffer at pH7. Thermal stability of CRL/CS-NCs was 1.5-fold greater than that of free CRL, with biocatalysts reusability for up to 8 successive esterification cycles. This research provides a promising approach for expanding the use of NC from OPFL for enhancing enzyme activity in favour of an alternative eco-friendly means to synthesize butyl butyrate.
    Matched MeSH terms: Fungal Proteins/chemistry*
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