| Abstract: | An alkaline protease gene (Eap) was isolated for the first time from a marine fungus, Engyodontium album. Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology model of the Engyodontium album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to have two disulfide bonds and more than two Ca2? binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein. |
| Description: | World J Microbiol Biotechnol (2010) 26:1269–1279 DOI 10.1007/s11274-009-0298-6 |
| URI: | http://dyuthi.cusat.ac.in/purl/4019 |
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| Molecular cloni ... yodontium albumBTMFS10.pdf | (590.8Kb) |
| Abstract: | An alkaline protease gene (Eap) was isolated for the first time from a marine fungus, Engyodontium album. Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology model of the Engyodontium album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to have two disulfide bonds and more than two Ca2? binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein. |
| Description: | World J Microbiol Biotechnol (2010) 26:1269–1279 |
| URI: | http://dyuthi.cusat.ac.in/purl/4259 |
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| Molecular cloni ... odontium album BTMFS10.pdf | (590.8Kb) |
| Abstract: | Biofilm forming multidrug resistant Staphylococcus spp. are major reservoirs for transmission of ophthalmic infections. They were isolated from ocular patients suffering from conjunctivitis. In this study we analyzed biofilm forming ability, antibiotic resistance profile of the Staphylococcus spp. isolated from clinical ocular patients, and their phylogenetic relationship with other community MRSA. Sixty Staphylococcus spp. strains isolated from clinical subjects were evaluated for their ability to form biofilm and express biofilm encoding ica gene. Among them 93% were slime producers and 87% were slime positive. Staphylococcus aureus and S. epidermidis were dominant strains among the isolates obtained from ocular patients. The strains also exhibited a differential biofilm formation quantitatively. Antibiotic susceptibility of the strains tested with Penicillin G, Ciprofloxacin, Ofloxacin, Methicillin, Amikacin, and Gentamicin indicated that they were resistant to more than one antibiotic. The amplicon of ica gene of strong biofilm producing S. aureus strains, obtained by polymerase chain reaction, was sequenced and their close genetic relationship with community acquired MRSA was analyzed based on phylogenetic tree. Our results indicate that they are genetically close to other community acquired MRSA |
| Description: | Polish Journal of Microbiology 2010, Vol. 59, No 4, 233 239 |
| URI: | http://dyuthi.cusat.ac.in/purl/4253 |
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| Biofilm Forming ... ts with Conjunctivitis.pdf | (5.361Mb) |
| Abstract: | An alkaline protease from marine Engyodontium album was characterized for its physicochemical properties towards evaluation of its suitability for potential industrial applications. Molecular mass of the enzyme by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) analysis was calculated as 28.6 kDa. Isoelectric focusing yielded pI of 3–4. Enzyme inhibition by phenylmethylsulfonyl fluoride (PMSF) and aprotinin confirmed the serine protease nature of the enzyme.Km, Vmax, and Kcat of the enzyme were 4.727 9 10-2 mg/ml, 394.68 U, and 4.2175 9 10-2 s-1, respectively. Enzyme was noted to be active over a broad range of pH (6–12) and temperature (15–65 C), withmaximumactivity at pH 11 and 60 C. CaCl2 (1 mM), starch (1%), and sucrose (1%) imparted thermal stability at 65 C. Hg2?, Cu2?, Fe3?, Zn2?, Cd?, and Al3? inhibited enzyme activity, while 1 mMCo2? enhanced enzyme activity. Reducing agents enhanced enzyme activity at lower concentrations. The enzyme showed considerable storage stability, and retained its activity in the presence of hydrocarbons, natural oils, surfactants, and most of the organic solvents tested. Results indicate that the marine protease holds potential for use in the detergent industry and for varied applications. |
| Description: | J Ind Microbiol Biotechnol (2011) 38:743–752 DOI 10.1007/s10295-010-0914-3 |
| URI: | http://dyuthi.cusat.ac.in/purl/4264 |
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| Characterizatio ... odontium album BTMFS10.pdf | (382.3Kb) |
| Abstract: | Protease inhibitors have great demand in medicine and biotechnology. We report here the purification and characterization of a protease inhibitor isolated from mature leaf extract of Moringa oleifera that showed maximum inhibitor activity. The protease inhibitor was purified to 41.4-fold by Sephadex G75 and its molecular mass was calculated as 23,600 Da. Inhibitory activity was confirmed by dot-blot and reverse zymogram analyses. Glycine, glutamic acid, alanine, proline and aspartic acid were found as the major amino acids of the inhibitor protein. Maximal activity was recorded at pH 7 and at 40 ◦C. The inhibitor was stable over pH 5–10; and at 50 ◦C for 2 h. Thermostability was promoted by CaCl2, BSA and sucrose. Addition of Zn2+ and Mg2+, SDS, dithiothreitol and -mercaptoethanol enhanced inhibitory activity, while DMSO and H2O2 affected inhibitory activity. Modification of amino acids at the catalytic site by PMSF and DEPC led to an enhancement in the inhibitory activity. Stoichiometry of trypsin–protease inhibitor interaction was 1:1.5 and 0.6 nM of inhibitor effected 50% inhibition. The low Ki value (1.5 nM) obtained indicated scope for utilization of M. oliefera protease inhibitor against serine proteases |
| Description: | Process Biochemistry 46 (2011) 2291–2300 |
| URI: | http://dyuthi.cusat.ac.in/purl/4257 |
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| Protease inhibi ... , and characterisation.pdf | (797.7Kb) |
| Abstract: | Marine Aspergillus awamori BTMFW032, recently reported by us, produce acidophilic tannase as extracellular enzyme. Here, we report the application of this enzyme for synthesis of propyl gallate by direct transesterification of tannic acid and in tea cream solubilisation besides the simultaneous production of gallic acid along with tannase under submerged fermentation by this fungus. This acidophilic tannase enabled synthesis of propyl gallate by direct transesterification of tannic acid using propanol as organic reaction media under low water conditions. The identity of the product was confirmed with thin layer chromatography and Fourier transform infrared spectroscopy. It was noted that 699 U/ml of enzyme could give 60% solubilisation of tea cream within 1 h. Enzyme production medium was optimized adopting Box–Behnken design for simultaneous synthesis of tannase and gallic acid. Process variables including tannic acid, sodium chloride, ferrous sulphate, dipotassium hydrogen phosphate, incubation period and agitation were recognized as the critical factors that influenced tannase and gallic acid production. The model obtained predicted 4,824.61 U/ml of tannase and 136.206 μg/ml gallic acid after 48 h of incubation, whereas optimized medium supported 5,085 U/ml tannase and 372.6 μg/ml of gallic acid production after 36 and 84 h of incubation, respectively, with a 15-fold increase in both enzyme and gallic acid production. Results indicated scope for utilization of this acidophilic tannase for transesterification of tannic acid into propyl gallate, tea cream solubilisation and simultaneous production of gallic acid along with tannase |
| Description: | Appl Biochem Biotechnol (2011) 164:612–628 DOI 10.1007/s12010-011-9162-x |
| URI: | http://dyuthi.cusat.ac.in/purl/4252 |
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| Propyl Gallate ... illus awamori BTMFW032.pdf | (810.6Kb) |
| Abstract: | Protease inhibitors are well known to have several applications in medicine and biotechnology. Several plant sources are known to return potential protease inhibitors. In this study plants belonging to different families of Leguminosae, Malvaceae, Rutaceae, Graminae and Moringaceae were screened for the protease inhibitor. Among them Moringa oleifera, belonging to the family Moringaceae, recorded high level of protease inhibitor activity after ammonium sulfate fractionation. M. oleifera, which grows throughout most of the tropics and having several industrial and medicinal uses, was selected as a source of protease inhibitor since so far no reports were made on isolation of the protease inhibitor. Among the different parts of M. oleifera tested, the crude extract isolated from the mature leaves and seeds showed the highest level of inhibition against trypsin. Among the various extraction media evaluated, the crude extract prepared in phosphate buffer showed maximum recovery of the protease inhibitor. The protease inhibitor recorded high inhibitory activity toward the serine proteases thrombin, elastase, chymotrypsin and the cysteine |
| Description: | Saudi journal of biological sciences(2011) 18,273-281 |
| URI: | http://dyuthi.cusat.ac.in/purl/4258 |
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| Protease inhibi ... s seafood preservative.pdf | (560.5Kb) |
| Abstract: | Biopulping being less energy intensive, inexpensive and causing lesser pollution, can be a viable alternative to chemical and mechanical pulping in paper and pulp industry. In view of shrinking forest reserves, agricultural residues are considered as an alternative raw material for making paper and board. By suitable treatment agriwaste can be converted into substrate for mushroom cultivation. Mushrooms of Pleurotus sp. can preferentially remove lignin from agriwaste with limited degradation to cellulose. The present study examines utilization of Pleurotus eous for biopulping of paddy straw by solid substrate fermentation. SMS, the mushroom growing medium that results from cultivation process, is a good source of fibre and can be pulped easily. Ligninases present in SMS were able to reduce lignin content to nearly half the initial amount by 21st day of cultivation. Highest cellulose content (% dry weight) was observed on 21st day, while cellulase production commenced from 28th day of cultivation. SEM images revealed that SMS fibres are still associated with non-cellulosic materials when compared to chemically (20% w/v NaOH) extracted fibres. |
| Description: | Advanced Biotech. Vol. 11 Issue 01 l July 2011 |
| URI: | http://dyuthi.cusat.ac.in/purl/4729 |
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| Biopulping of Paddy Straw by Pleurotus eous.pdf | (3.974Mb) |
| Abstract: | Marine fungus BTMFW032, isolated from seawater and identified as Aspergillus awamori, was observed to produce an extracellular lipase, which could reduce 92% fat and oil content in the effluent laden with oil. In this study, medium for lipase production under submerged fermentation was optimized statistically employing response surface method toward maximal enzyme production. Medium with soyabean meal- 0.77% (w/v); (NH4)2SO4-0.1 M; KH2PO4-0.05 M; rice bran oil-2% (v/v); CaCl2-0.05 M; PEG 6000-0.05% (w/v); NaCl-1% (w/v); inoculum-1% (v/v); pH 3.0; incubation temperature 35 8C and incubation period-five days were identified as optimal conditions for maximal lipase production. The time course experiment under optimized condition, after statistical modeling, indicated that enzyme production commenced after 36 hours of incubation and reached a maximum after 96 hours (495.0 U/ml), whereas maximal specific activity of enzyme was recorded at 108 hours (1164.63 U/mg protein). After optimization an overall 4.6- fold increase in lipase production was achieved. Partial purification by (NH4)2SO4 precipitation and ion exchange chromatography resulted in 33.7% final yield. The lipase was noted to have a molecular mass of 90 kDa and optimal activity at pH 7 and 40 8C. Results indicated the scope for potential application of this marine fungal lipase in bioremediation. |
| Description: | New Biotechnology Volume 28, Number 6 October 2011 |
| URI: | http://dyuthi.cusat.ac.in/purl/4250 |
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| Lipase from mar ... oil effluent treatment.pdf | (940.8Kb) |
| Abstract: | Spent substrate, the residual material of mushroom cultivation, causes disposal problems for cultivators. Currently the spent substrate of different mushrooms is used mainly for composting. Edible mushrooms of Pleurotus sp. can grow on a wide range of lignocellulosic substrates. In the present study, Pleurotus eous was grown on paddy straw and the spent substrate was used for the production of ethanol. Lignocellulosic biomass cannot be saccharified by enzymes to high yield of ethanol without pretreatment. The root cause for the recalcitrance of lignocellulosic biomass such as paddy straw is the presence of lignin and hemicelluloses on the surface of cellulose. They form a barrier and prevent cellulase from accessing the cellulose in the substrate. In the untreated paddy straw, the amount of hemicelluloses and lignin (in % dry weight) were 20.30 and 20.34 respectively and the total reducing sugar was estimated to be 5.40 mg/g. Extracellular xylanase and ligninases of P. eous could reduce the amount of hemicelluloses and lignin to 16 and 11(% dry weight) respectively, by 21st day of cultivation. Growth of mushroom brought a seven fold increase in the total reducing sugar yield (39.20 mg/g) and six fold increase in the production of ethanol (6.48 g/L) after 48hrs of fermentation, when compared to untreated paddy straw |
| Description: | International Journal of Applied Biology and Pharmaceutical Technology,vol 3,issue 1:jan-mar 2012 |
| URI: | http://dyuthi.cusat.ac.in/purl/4730 |
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| Ethanol Product ... rate Of Pleurotus Eous.pdf | (273.3Kb) |
| Abstract: | Random genetic changes generated during in vitro culture are not desirable for plant micropropagation and genetic transformation. RAPD markers were used to detect the variation in leaf disc callus cultures of Jatropha curcas, maintained in Murashige and Skoog (MS) medium with different auxin and cytokinin combinations. In total 41 scorable bands were produced with 11 primers. Out of 41 bands, 37 were polymorphic (91.12%). The average number of polymorphic bands was 3.36 per primer. The highest similarity (0.82) with mother plant was seen in callus maintained on MS with hormonal combination Indole butyric acid - 0.4mg/l+ N6-benzyladenine purine - 4.0 mg/l. The callus grown on MS with hormonal combinations IBA- 0.4mg/l+ BAP- 2.0mg/l, IBA- 0.4mg/l+ BAP- 2.5mg/l and IBA- 0.6 mg/l+ BAP- 2.0 mg/l also showed similarity with the mother plant. Callus maintained on MS with hormonal combination IBA- 0.2mg/l+ BAP- 2.0 mg/l was found to show least similarity (0.53) with mother plant |
| Description: | World Journal of Agricultural Sciences 8 (6): 616-623, 2012 |
| URI: | http://dyuthi.cusat.ac.in/purl/4734 |
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| Evaluation of S ... ons Using RAPD Markers.pdf | (419.8Kb) |
| Abstract: | Bioethanol is a liquid fuel obtained from fermentation of sugar/starch crops. Lignocellulosic biomass being less expensive is considered a future alternative for the food crops. One of the main challenges for the use of lignocellulosics is the development of an efficient pre-treatment process. Pretreatments are classified into three - physical, chemical, and biological pretreatment. Chemical process has not been proven suitable so far, due to high costs and production of undesired by-products. Biologically, hydrolysis can be enhanced by microbial or enzymatic pretreatment. Studies show that the edible mushrooms of Pleurotus sp. produce several extracellular enzymes which reduce the structural and chemical complexity of fibre. In the present study, P. ostreatus and P. eous were cultivated on paddy straw. Spent substrate left after mushroom cultivation was powdered and used for ethanol production. Saccharomyces sp. was used for fermentation studies. Untreated paddy straw was used as control. Production of ethanol from P. ostreatus substrate was 5.5 times more when compared to untreated paddy straw, while the spent substrate of P. eous gave 5 times increase in ethanol yield. Assays showed the presence of several extracellular enzymes in the spent substrate of both species, which together contributed to the increase in ethanol yield |
| Description: | International Journal of Plant, Animal and Environmental Sciences,vol 2,issue 2,april-june 2012 |
| URI: | http://dyuthi.cusat.ac.in/purl/4731 |
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| Pretreatment Of ... With Pleurotus Sp. For.pdf | (144.1Kb) |
| Abstract: | Phenol is an aromatic hydrocarbon which exists as a colorless or white solid in its pure state. Over the past several decades, there is growing concern about wide spread contamination of surface and ground water by phenol, due to rapid development of chemical and petrochemical industries. Phenol affects aquatic life even at relatively low concentration (5-25mg/L). Treatment for removal of phenol includes chemical as well as biological processes. Studies show that ligninases such as Lignin Peroxidase and Laccase, produced by Pleurotus sp., can degrade phenol. Spent substrate of Pleurotus mushrooms consists of ligninases. Present work was to investigate the potential of spent substrate of edible mushroom P. ostreatus for biodegradation of phenol. P. ostreatus was cultivated on paddy straw. After harvest, spent substrate was utilized for phenol degradation. According to the enzyme profile of two ligninases present in the spent substrate of P. ostreatus, maximum specific activity for Laccase was observed in 35 day old spent substrate and LiP activity was maximum in 56 day old spent substrate, which together contributed significantly for removal of phenol. Spent substrate of 35th and 56th day were each incubated with phenol sample (1:1w/v) for one day, which resulted in degradation of phenol by 48% and 45% respectively. From these results it appears that, spent substrate of P. ostreatus can be used effectively to remove phenol from industrial effluents |
| Description: | World Journal Of Pharmacy And Pharmaceutical Sciences,Volume 1, Issue 2, 656-661. |
| URI: | http://dyuthi.cusat.ac.in/purl/4733 |
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| Biodegradation ... trate Of Pleurotus Sp..pdf | (205.5Kb) |
| Abstract: | The morphological and biochemical response of calli and seedlings of different rice cultivars were compared under acid saline conditions. Calli of both tolerant and sensitive varieties showed severe stress symptoms like browning and necrosis, but the onset of stress symptoms was delayed in Pokkali. Seedlings of Pokkali showed minimal stress symptoms in lower salinities, and curling and senescence of older leaves in higher salinities although plants revived on amelioration of stress. Seedlings of the other varieties showed severe stress symptoms even at low salinities and plant death at higher salinities. Salt stress induced accumulation of the putative osmoprotectant proline in calli and seedlings of all varieties. Proline accumulation was higher in sensitive varieties than in Pokkali. These results indicate that proline accumulation is not directly correlated with salt tolerance in rice. |
| URI: | http://dyuthi.cusat.ac.in/purl/4736 |
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| Proline Accumulation and SaltTolerance in Rice.pdf | (1.866Mb) |
| Abstract: | This study was undertaken to isolate ligninase-producing white-rot fungi for use in the extraction of fibre from pineapple leaf agriwaste. Fifteen fungal strains were isolated from dead tree trunks and leaf litter. Ligninolytic enzymes (lignin peroxidase (LiP), manganese peroxidase (MnP), and laccase (Lac)), were produced by solid-state fermentation (SSF) using pineapple leaves as the substrate. Of the isolated strains, the one showing maximum production of ligninolytic enzymes was identified to be Ganoderma lucidum by 18S ribotyping. Single parameter optimization and response surface methodology of different process variables were carried out for enzyme production. Incubation period, agitation, and Tween-80 were identified to be the most significant variables through Plackett-Burman design. These variables were further optimized by Box-Behnken design. The overall maximum yield of ligninolytic enzymes was achieved by experimental analysis under these optimal conditions. Quantitative lignin analysis of pineapple leaves by Klason lignin method showed significant degradation of lignin by Ganoderma lucidum under SSF |
| Description: | BioResources 8(1), 250-271. |
| URI: | http://dyuthi.cusat.ac.in/purl/4735 |
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| Optimization of ... tion of Pineapple Leaf.pdf | (987.6Kb) |
| Abstract: | The date palm Phoenix dactylifera has played an important role in the day-to-day life of the people for the last 7000 years. Today worldwide production, utilization and industrialization of dates are continuously increasing since date fruits have earned great importance in human nutrition owing to their rich content of essential nutrients. Tons of date palm fruit wastes are discarded daily by the date processing industries leading to environmental problems. Wastes such as date pits represent an average of 10% of the date fruits. Thus, there is an urgent need to find suitable applications for this waste. In spite of several studies on date palm cultivation, their utilization and scope for utilizing date fruit in therapeutic applications, very few reviews are available and they are limited to the chemistry and pharmacology of the date fruits and phytochemical composition, nutritional significance and potential health benefits of date fruit consumption. In this context, in the present review the prospects of valorization of these date fruit processing by-products and wastes’ employing fermentation and enzyme processing technologies towards total utilization of this valuable commodity for the production of biofuels, biopolymers, biosurfactants, organic acids, antibiotics, industrial enzymes and other possible industrial chemicals are discussed |
| Description: | Saudi journal of biological sciences (2013)20,105-120 |
| URI: | http://dyuthi.cusat.ac.in/purl/4254 |
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| Valorization of ... ss technology – Review.pdf | (516.4Kb) |
| Abstract: | Halobacteria, members of the domain Archaea that live under extremely halophilic conditions, are often considered as dependable source for deriving novel enzymes, novel genes, bioactive compounds and other industrially important molecules. Protein antibiotics have potential for application as preserving agents in food industry, leather industry and in control of infectious bacteria. Halocins are proteinaceous antibiotics synthesized and released into the environment by extreme halophiles, a universal characteristic of halophilic bacteria. Herein, we report the production of halocin (SH10) by an extremely halophilic archeon Natrinema sp. BTSH10 isolated from salt pan of Kanyakumari, Tamilnadu, India and optimization of medium for enhanced production of halocin. It was found that the optimal conditions for maximal halocin production were 42 C, pH 8.0, and 104 h of incubation at 200 rpm with 2% (V/V) inoculum concentration in Zobell’s medium containing 3 M NaCl, Galactose, beef extract, and calcium chloride as additional supplements. Results indicated scope for fermentation production of halocin for probable applications using halophilic archeon Natrinema sp. BTSH10 |
| Description: | saudi journal of biological sciences(2013) 20,205-212 |
| URI: | http://dyuthi.cusat.ac.in/purl/4265 |
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| Halocin SH10 pr ... lt pans of South India.pdf | (733.2Kb) |
| Abstract: | Bacillus smithii BTMS 11, isolated from marine sediment, produced alkaline and thermostable lipase. The enzyme was purified to homogeneity by ammonium sulfate precipitation and ion exchange chromatography which resulted in 0.51 % final yield and a 4.33 fold of purification. The purified enzyme was found to have a specific activity of 360 IU/mg protein. SDS-PAGE analyses, under non-reducing and reducing conditions, yielded a single band of 45 kDa indicating the single polypeptide nature of the enzyme and zymogram analysis using methylumbelliferyl butyrate as substrate confirmed the lipolytic activity of the protein band. The enzyme was found to have 50 C and pH 8.0 as optimum conditions for maximal activity. However, the enzyme was active over wide range of temperatures (30–80 C) and pH (7.0–10.0). Effect of a number of metal salts, solvents, surfactants, and other typical enzyme inhibitors on lipase activity was studied to determine the novel characteristics of the enzyme. More than 90 % of the enzyme activity was observed even after 3 h of incubation in the presence of commercial detergents Surf, Sunlight, Ariel, Henko, Tide and Ujala indicating the detergent compatibility of B. smithii lipase. The enzyme was also found to be efficient in stain removal from cotton cloths. Further it was observed that the enzyme could catalyse ester synthesis between fatty acids of varying carbon chain lengths and methanol with high preference for medium to long chain fatty acids showing 70 % of esterification. Results of the study indicated scope for application of this marine bacterial lipase in various industries |
| Description: | World J Microbiol Biotechnol (2013) 29:1349–1360 DOI 10.1007/s11274-013-1298-0 |
| URI: | http://dyuthi.cusat.ac.in/purl/4262 |
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| Detergent compa ... cillus smithii BTMS 11.pdf | (531.4Kb) |
| Abstract: | Prodigiosin is known for its immunomodulatory, antibacterial, antimycotic, antimalarial, algicidal and anticancer activities. Here, we reported the evaluation of prodigiosin pigment as a dyeing agent in rubber latex, paper and polymethyl methacrylate (PMMA) so that it can be considered as an alternative to synthetic pigments. Maximum color shade was obtained in rubber sheet prepared with 0.5 parts per hundred gram of rubber (phr) pigment and PMMA sheet incorporated with 0.08 μg pigment. Results indicate scope for utilization of prodigiosin as dye for PMMA and rubber and also prodigiosin dyed paper as a pH indicator. Further, being a natural and water insoluble pigment, it is ecofriendly |
| Description: | African Journal of Biotechnology Vol. 12(17), pp. 2266-2269, 24 April, 2013 |
| URI: | http://dyuthi.cusat.ac.in/purl/4263 |
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| Marine bacteria ... ylate sheets and paper.pdf | (156.6Kb) |
| Abstract: | Protease inhibitors can be versatile tools mainly in the fields of medicine, agriculture and food preservative applications. Fungi have been recognized as sources of protease inhibitors, although there are only few such reports on mushrooms. This work reports the purification and characterization of a trypsin inhibitor from the fruiting body of edible mushroom Pleurotus floridanus (PfTI) and its effect on the activity of microbial proteases. The protease inhibitor was purified up to 35-fold by DEAE-Sepharose ion exchange column, trypsin-Sepharose column and Sephadex G100 column. The isoelectric point of the inhibitor was 4.4, and its molecular mass was calculated as 37 kDa by SDS-PAGE and 38.3 kDa by MALDI-TOF. Inhibitory activity confirmation was by dot-blot analysis and zymographic activity staining. The specificity of the inhibitor toward trypsin was with Ki of 1.043×10−10 M. The inhibitor was thermostable up to 90 °C with maximal stability at 30 °C, active over a pH range of 4–10 against proteases from Aspergillus oryzae, Bacillus licheniformis, Bacillus sp. and Bacillus amyloliquefaciens. Results indicate the possibility of utilization of protease inhibitor from P. floridanus against serine proteases |
| Description: | Appl Biochem Biotechnol (2014) 173:167–178 DOI 10.1007/s12010-014-0826-1 |
| URI: | http://dyuthi.cusat.ac.in/purl/4268 |
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| Trypsin Inhibit ... es of Microbial Origin.pdf | (597.3Kb) |
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