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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
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
Fulltext Microbial Enzymes and Their Applications in Industries and Medicine 2016

Anbu P, Gopinath SCB, Chaulagain BP, Lakshmipriya T

Biomed Res Int, 2017 03 28;2017:2195808.
PMID: 28459056 DOI: 10.1155/2017/2195808
Matched MeSH terms: Fungal Proteins/chemistry*
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*
Lipase-catalyzed esterification for efficient acylglycerols synthesis in a solvent-free system: Process optimization, mass transfer insights and kinetic modeling

Zou S, Zhang Z, Lee YY, Ai H, Zhang Y, Wang Y

Food Chem, 2025 May 15;474:143151.
PMID: 39891972 DOI: 10.1016/j.foodchem.2025.143151

Acylglycerols are widely used in the food industry due to their antimicrobial, emulsifying and nutritional properties. This study investigated the key reaction parameters, mass transfer mechanisms, and kinetic features of lipase-catalyzed esterification in a solvent-free system. Taguchi method was further employed to explore the relationship between "reaction parameter - yield composition". The results revealed that the maximum selectivity were achieved fror MAG (57.72 %), DAG (82.67 %) and TAG (79.29 %) under different enzymatic conditions. Fatty acid-to-glycerol molar ratio had the greatest impact on DAG selectivity, contributing 38.08 % of total impact level. Mass transfer analysis showed that external mass transfer limitation could be effectively overcome at stirring speeds above 600 rpm. Kinetic analysis confirmed that the reaction followed the Ping-Pong BiBi mechanism with alcohol and acid inhibition (SSE = 0.000643). This work provided a theoretical basis for developing more efficient and selective catalytic processes, aiding in quality control, reactor design, and industrial scale-up.

Matched MeSH terms: Fungal Proteins/chemistry
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*
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
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
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
Fabrication, characterization and application of laccase-nylon 6,6/Fe(3+) composite nanofibrous membrane for 3,3'-dimethoxybenzidine detoxification

Jasni MJ, Sathishkumar P, Sornambikai S, Yusoff AR, Ameen F, Buang NA, et al.

Bioprocess Biosyst Eng, 2017 Feb;40(2):191-200.
PMID: 27757535 DOI: 10.1007/s00449-016-1686-6

In this study, laccase was immobilized on nylon 6,6/Fe(3+) composite (NFC) nanofibrous membrane and used for the detoxification of 3,3'-dimethoxybenzidine (DMOB). The average size and tensile strength of the NFC membrane were found to be 60-80 nm (diameter) and 2.70 MPa, respectively. The FTIR results confirm that the amine (N-H) group of laccase was attached with Fe(3+) particles and the carbonyl (C=O) group of NFC membrane via hydrogen bonding. The half-life of the laccase-NFC membrane storage stability was increased from 6 to 11 weeks and the reusability was significantly extended up to 43 cycles against ABTS oxidation. Enhanced electro-oxidation of DMOB by laccase was observed at 0.33 V and the catalytic current was found to be 30 µA. The DMOB-treated mouse fibroblast 3T3-L1 preadipocytes showed maximum (97 %) cell inhibition at 75 µM L(-1) within 24 h. The cytotoxicity of DMOB was significantly decreased to 78 % after laccase treatment. This study suggests that laccase-NFC membrane might be a good candidate for emerging pollutant detoxification.

Matched MeSH terms: Fungal Proteins/chemistry*
Immobilized Candida antarctica lipase B: Hydration, stripping off and application in ring opening polyester synthesis

Idris A, Bukhari A

Biotechnol Adv, 2012 May-Jun;30(3):550-63.
PMID: 22041165 DOI: 10.1016/j.biotechadv.2011.10.002

This work reviews the stripping off, role of water molecules in activity, and flexibility of immobilized Candida antarctica lipase B (CALB). Employment of CALB in ring opening polyester synthesis emphasizing on a polylactide is discussed in detail. Execution of enzymes in place of inorganic catalysts is the most green alternative for sustainable and environment friendly synthesis of products on an industrial scale. Robust immobilization and consequently performance of enzyme is the essential objective of enzyme application in industry. Water bound to the surface of an enzyme (contact class of water molecules) is inevitable for enzyme performance; it controls enzyme dynamics via flexibility changes and has intensive influence on enzyme activity. The value of pH during immobilization of CALB plays a critical role in fixing the active conformation of an enzyme. Comprehensive selection of support and protocol can develop a robust immobilized enzyme thus enhancing its performance. Organic solvents with a log P value higher than four are more suitable for enzymatic catalysis as these solvents tend to strip away very little of the enzyme surface bound water molecules. Alternatively ionic liquid can work as a more promising reaction media. Covalent immobilization is an exclusively reliable technique to circumvent the leaching of enzymes and to enhance stability. Activated polystyrene nanoparticles can prove to be a practical and economical support for chemical immobilization of CALB. In order to reduce the E-factor for the synthesis of biodegradable polymers; enzymatic ring opening polyester synthesis (eROPS) of cyclic monomers is a more sensible route for polyester synthesis. Synergies obtained from ionic liquids and immobilized enzyme can be much effective eROPS.

Matched MeSH terms: Fungal Proteins/chemistry*
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
Chemoenzymatic and microbial dynamic kinetic resolutions

Kamaruddin AH, Uzir MH, Aboul-Enein HY, Halim HN

Chirality, 2009 Apr;21(4):449-67.
PMID: 18655180 DOI: 10.1002/chir.20619

This review tracks a decade of dynamic kinetic resolution developments with a biocatalytic inclination using enzymatic/microbial means for the resolution part followed by the racemization reactions either by means of enzymatic or chemocatalyst. These fast developments are due to the ability of the biocatalysts to significantly reduce the number of synthetic steps which are common for conventional synthesis. Future developments in novel reactions and products of dynamic kinetic resolutions should consider factors that are needed to be extracted at the early synthetic stage to avoid inhibition at scale-up stage have been highlighted.

Matched MeSH terms: Fungal Proteins/chemistry*
Nonlinear process modeling of fructosyltransferase (FTase) using bootstrap re-sampling neural network model

Ahmad Z, Don MM, Mortan SH, Noor RA

Bioprocess Biosyst Eng, 2010 Jun;33(5):599-606.
PMID: 19915872 DOI: 10.1007/s00449-009-0381-2

Recently, the increased demand of fructooligosaccharides (FOS) as a functional food has alarmed researchers to screen and identify new strains capable of producing fructosyltransferase (FTase). FTase is the enzyme that converts the substrate (sucrose) to glucose and fructose. The characterization of complex sugar such as table sugar, brown sugar, molasses, etc. will be carried out and the sugar that contained the highest sucrose concentration will be selected as a substrate. Eight species of macro-fungi will be screened for its ability to produce FTase and only one strain with the highest FTase activity will be selected for further studies. In this work, neural networks (NN) have been chosen to model the process based on their excellent 'resume' in coping with nonlinear process. Bootstrap re-sampling method has been utilized in re-sampling the data in this work. This method has successfully modeled the process as shown in the results.

Matched MeSH terms: Fungal Proteins/chemistry
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*
Features of the rare pathogen Meyerozyma guilliermondii strain SO and comprehensive in silico analyses of its adherence-contributing virulence factor agglutinin-like sequences

Lim SJ, Muhd Noor ND, Sabri S, Mohamad Ali MS, Salleh AB, Oslan SN

J Biomol Struct Dyn, 2025 Apr;43(7):3728-3748.
PMID: 38189364 DOI: 10.1080/07391102.2023.2300757

Meyerozyma guilliermondii is a rare yeast pathogen contributing to the deadly invasive candidiasis. M. guilliermondii strain SO, as a promising protein expression host, showed 99% proteome similarity with the clinically isolated ATCC 6260 (type strain) in a recent comparative genomic analysis. However, their in vitro virulence features and in vivo pathogenicity were uncharacterized. This study aimed to characterize the in vitro and in vivo pathogenicity of M. guilliermondii strain SO and analyze its Als proteins (MgAls) via comprehensive bioinformatics approaches. M. guilliermondii strain SO showed lower and higher sensitivity towards β-mercaptoethanol and lithium, respectively than the avirulent S. cerevisiae but exhibited the same tolerance towards cell wall-perturbing Congo Red with C. albicans. With 7.5× higher biofilm mass, M. guilliermondii strain SO also demonstrated 75% higher mortality rate in the zebrafish embryos with a thicker biofilm layer on the chorion compared to the avirulent S. cerevisiae. Being one of the most important Candida adhesins, sequence and structural analyses of four statistically identified MgAls showed that MgAls1056 was predicted to exhibit the most conserved amyloid-forming regions, tandem repeat domain and peptide binding cavity (PBC) compared to C. albicans Als3. Favoured from the predicted largest ligand binding site and druggable pockets, it showed the highest affinity towards hepta-threonine. Non-PBC druggable pockets in the most potent virulence contributing MgAls1056 provide new insights into developing antifungal drugs targeting non-albicans Candida spp. Virtual screening of available synthetic or natural bioactive compounds and MgAls1056 deletion from the fungal genome should be further performed and validated experimentally.

Matched MeSH terms: Fungal Proteins/chemistry
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
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
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*
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

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