Enzyme Research最新文献

{"title":"A Thermostable Crude Endoglucanase Produced by Aspergillus fumigatus in a Novel Solid State Fermentation Process Using Isolated Free Water.","authors":"Abdul A N Saqib, Ansa Farooq, Maryam Iqbal, Jalees Ul Hassan, Umar Hayat, Shahjahan Baig","doi":"10.1155/2012/196853","DOIUrl":"10.1155/2012/196853","url":null,"abstract":"<p><p>Aspergillus fumigatus was grown on chopped wheat straw in a solid state fermentation (SSF) process carried out in constant presence of isolated free water inside the fermentation chamber. The system allowed maintaining a constant vapor pressure inside the fermentor throughout the fermentation process. Crude endoglucanase produced by A. fumigatus under such conditions was more thermostable than previously reported enzymes of the same fungal strain which were produced under different conditions and was also more thermostable than a number of other previously reported endoglucanases as well. Various thermostability parameters were calculated for the crude endoglucanase. Half lives (T(1/2)) of the enzyme were 6930, 866, and 36 min at 60°C, 70°C, and 80°C, respectively. Enthalpies of activation of denaturation (ΔH(D)*) were 254.04, 253.96, and 253.88 K J mole(-1), at 60°C, 70°C and 80°C, respectively, whereas entropies of activation of denaturation (ΔS(D)*) and free energy changes of activation of denaturation (ΔG(D)*) were 406.45, 401.01, and 406.07 J mole(-1) K(-1) and 118.69, 116.41, and 110.53 K J mole(-1) at 60°C, 70°C and 80°C, respectively.</p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"196853"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399398/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30856618","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inhibition of heme peroxidases by melamine.","authors":"Pattaraporn Vanachayangkul,&nbsp;William H Tolleson","doi":"10.1155/2012/416062","DOIUrl":"https://doi.org/10.1155/2012/416062","url":null,"abstract":"<p><p>In 2008 melamine-contaminated infant formula and dairy products in China led to over 50,000 hospitalizations of children due to renal injuries. In North America during 2007 and in Asia during 2004, melamine-contaminated pet food products resulted in numerous pet deaths due to renal failure. Animal studies have confirmed the potent renal toxicity of melamine combined with cyanuric acid. We showed previously that the solubility of melamine cyanurate is low at physiologic pH and ionic strength, provoking us to speculate how toxic levels of these compounds could be transported through the circulation without crystallizing until passing into the renal filtrate. We hypothesized that melamine might be sequestered by heme proteins, which could interfere with heme enzyme activity. Four heme peroxidase enzymes were selected for study: horseradish peroxidase (HRP), lactoperoxidase (LPO), and cyclooxygenase-1 and -2 (COX-1 and -2). Melamine exhibited noncompetitive inhibition of HRP (K(i)  9.5 ± 0.7 mM), and LPO showed a mixed model of inhibition (K(i)  14.5 ± 4.7 mM). The inhibition of HRP and LPO was confirmed using a chemiluminescent peroxidase assay. Melamine also exhibited COX-1 inhibition, but inhibition of COX-2 was not detected. Thus, our results demonstrate that melamine inhibits the activity of three heme peroxidases.</p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"416062"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/416062","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30803613","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biotechnological Potential of Agro Residues for Economical Production of Thermoalkali-Stable Pectinase by Bacillus pumilus dcsr1 by Solid-State Fermentation and Its Efficacy in the Treatment of Ramie Fibres.","authors":"Deepak Chand Sharma,&nbsp;T Satyanarayana","doi":"10.1155/2012/281384","DOIUrl":"https://doi.org/10.1155/2012/281384","url":null,"abstract":"<p><p>The production of a thermostable and highly alkaline pectinase by Bacillus pumilus dcsr1 was optimized in solid-state fermentation (SSF) and the impact of various treatments (chemical, enzymatic, and in combination) on the quality of ramie fibres was investigated. Maximum enzyme titer (348.0 ± 11.8 Ug(-1) DBB) in SSF was attained, when a mixture of agro-residues (sesame oilseed cake, wheat bran, and citrus pectin, 1 : 1 : 0.01) was moistened with mineral salt solution (a(w) 0.92, pH 9.0) at a substrate-to-moistening agent ratio of 1 : 2.5 and inoculated with 25% of 24 h old inoculum, in 144 h at 40°C. Parametric optimization in SSF resulted in 1.7-fold enhancement in the enzyme production as compared to that recorded in unoptimized conditions. A 14.2-fold higher enzyme production was attained in SSF as compared to that in submerged fermentation (SmF). The treatment with the enzyme significantly improved tensile strength and Young's modulus, reduction in brittleness, redness and yellowness, and increase in the strength and brightness of ramie fibres.</p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"281384"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/281384","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30863395","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Application of Statistical Design for the Production of Cellulase by Trichoderma reesei Using Mango Peel.","authors":"P Saravanan,&nbsp;R Muthuvelayudham,&nbsp;T Viruthagiri","doi":"10.1155/2012/157643","DOIUrl":"https://doi.org/10.1155/2012/157643","url":null,"abstract":"<p><p>Optimization of the culture medium for cellulase production using Trichoderma reesei was carried out. The optimization of cellulase production using mango peel as substrate was performed with statistical methodology based on experimental designs. The screening of nine nutrients for their influence on cellulase production is achieved using Plackett-Burman design. Avicel, soybean cake flour, KH(2)PO(4), and CoCl(2)·6H(2)O were selected based on their positive influence on cellulase production. The composition of the selected components was optimized using Response Surface Methodology (RSM). The optimum conditions are as follows: Avicel: 25.30 g/L, Soybean cake flour: 23.53 g/L, KH(2)PO(4): 4.90 g/L, and CoCl(2)·6H(2)O: 0.95 g/L. These conditions are validated experimentally which revealed an enhanced Cellulase activity of 7.8 IU/mL.</p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"157643"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/157643","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31147490","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Kinetic Analysis of Guanidine Hydrochloride Inactivation of β-Galactosidase in the Presence of Galactose.","authors":"Charles O Nwamba,&nbsp;Ferdinand C Chilaka","doi":"10.1155/2012/173831","DOIUrl":"https://doi.org/10.1155/2012/173831","url":null,"abstract":"<p><p>Inactivation of purified β-Galactosidase was done with GdnHCl in the absence and presence of varying [galactose] at 50°C and at pH 4.5. Lineweaver-Burk plots of initial velocity data, in the presence and absence of guanidine hydrochloride (GdnHCl) and galactose, were used to determine the relevant K(m) and V(max) values, with p-nitrophenyl β-D-galactopyranoside (pNPG) as substrate, S. Plots of ln([P](∞) - [P](t)) against time in the presence of GdnHCl yielded the inactivation rate constant, A. Plots of A versus [S] at different galactose concentrations were straight lines that became increasingly less steep as the [galactose] increased, showing that A was dependent on [S]. Slopes and intercepts of the 1/[P](∞) versus 1/[S] yielded k(+0) and k'(+0), the microscopic rate constants for the free enzyme and the enzyme-substrate complex, respectively. Plots of k(+0) and k'(+0) versus [galactose] showed that galactose protected the free enzyme as well as the enzyme-substrate complex (only at the lowest and highest [galactose]) against GdnHCl inactivation. In the absence of galactose, GdnHCl exhibited some degree of non-competitive inhibition. In the presence of GdnHCl, galactose exhibited competitive inhibition at the lower [galactose] of 5 mM which changed to non-competitive as the [galactose] increased. The implications of our findings are further discussed.</p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"173831"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/173831","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30931017","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Brain Levels of Catalase Remain Constant through Strain, Developmental, and Chronic Alcohol Challenges.","authors":"Dennis E Rhoads,&nbsp;Cherly Contreras,&nbsp;Salma Fathalla","doi":"10.1155/2012/572939","DOIUrl":"https://doi.org/10.1155/2012/572939","url":null,"abstract":"<p><p>Catalase (EC 1.11.1.6) oxidizes ethanol to acetaldehyde within the brain and variations in catalase activity may underlie some consequences of ethanol consumption. The goals of this study were to measure catalase activity in subcellular fractions from rat brain and to compare the levels of this enzyme in several important settings. In the first series of studies, levels of catalase were compared between juvenile and adult rats and between the Long-Evans (LE) and Sprague-Dawley (SD) strains. Levels of catalase appear to have achieved the adult level by the preadolescent period defined by postnatal age (P, days) P25-P28, and there were no differences between strains at the developmental stages tested. Thus, variation in catalase activity is unlikely to be responsible for differences in how adolescent and adult rats respond to ethanol. In the second series of studies, periadolescent and adult rats were administered ethanol chronically through an ethanol-containing liquid diet. Diet consumption and blood ethanol concentrations were significantly higher for periadolescent rats. Catalase activities remained unchanged following ethanol consumption, with no significant differences within or between strains. Thus, the brain showed no apparent adaptive changes in levels of catalase, even when faced with the high levels of ethanol consumption characteristic of periadolescent rats.</p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"572939"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/572939","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30856403","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Hydrolysis of virgin coconut oil using immobilized lipase in a batch reactor.","authors":"Lee Suan Chua,&nbsp;Meisam Alitabarimansor,&nbsp;Chew Tin Lee,&nbsp;Ramli Mat","doi":"10.1155/2012/542589","DOIUrl":"https://doi.org/10.1155/2012/542589","url":null,"abstract":"<p><p>Hydrolysis of virgin coconut oil (VCO) had been carried out by using an immobilised lipase from Mucor miehei (Lipozyme) in a water-jacketed batch reactor. The kinetic of the hydrolysis was investigated by varying the parameters such as VCO concentration, enzyme loading, water content, and reaction temperature. It was found that VCO exhibited substrate inhibition at the concentration more than 40% (v/v). Lipozyme also achieved the highest production of free fatty acids, 4.56 mM at 1% (w/v) of enzyme loading. The optimum water content for VCO hydrolysis was 7% (v/v). A relatively high content of water was required because water was one of the reactants in the hydrolysis. The progress curve and the temperature profile of the enzymatic hydrolysis also showed that Lipozyme could be used for free fatty acid production at the temperature up to 50°C. However, the highest initial reaction rate and the highest yield of free fatty acid production were at 45 and 40°C, respectively. A 100 hours of initial reaction time has to be compensated in order to obtain the highest yield of free fatty acid production at 40°C.</p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"542589"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/542589","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30885723","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Optimal Conditions for Continuous Immobilization of Pseudozyma hubeiensis (Strain HB85A) Lipase by Adsorption in a Packed-Bed Reactor by Response Surface Methodology.","authors":"Roberta Bussamara,&nbsp;Luciane Dall'agnol,&nbsp;Augusto Schrank,&nbsp;Kátia Flávia Fernandes,&nbsp;Marilene Henning Vainstein","doi":"10.1155/2012/329178","DOIUrl":"https://doi.org/10.1155/2012/329178","url":null,"abstract":"<p><p>This study aimed to develop an optimal continuous process for lipase immobilization in a bed reactor in order to investigate the possibility of large-scale production. An extracellular lipase of Pseudozyma hubeiensis (strain HB85A) was immobilized by adsorption onto a polystyrene-divinylbenzene support. Furthermore, response surface methodology (RSM) was employed to optimize enzyme immobilization and evaluate the optimum temperature and pH for free and immobilized enzyme. The optimal immobilization conditions observed were 150 min incubation time, pH 4.76, and an enzyme/support ratio of 1282 U/g support. Optimal activity temperature for free and immobilized enzyme was found to be 68°C and 52°C, respectively. Optimal activity pH for free and immobilized lipase was pH 4.6 and 6.0, respectively. Lipase immobilization resulted in improved enzyme stability in the presence of nonionic detergents, at high temperatures, at acidic and neutral pH, and at high concentrations of organic solvents such as 2-propanol, methanol, and acetone.</p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"329178"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/329178","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30443963","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Microbial enzyme: applications in industry and in bioremediation.","authors":"Alane Beatriz Vermelho,&nbsp;Claudiu T Supuran,&nbsp;Jose M Guisan","doi":"10.1155/2012/980681","DOIUrl":"https://doi.org/10.1155/2012/980681","url":null,"abstract":"This special issue is dedicated to the study of microbial enzymes and their applications in various industries. The biocatalytic uses for enzymes have grown immensely in recent years since they are ecologically correct, have a high specificity, present chemo-regio-enantio selectivity, and have a wide diversity of reactions. Moreover, the conditions to obtain and optimize the production of enzymes in terms of nutrients, pH, temperature, and aeration are easily controlled in bioreactors. Microorganisms can also be manipulated genetically to improve the desirable characteristics of a biocatalyzer. Additionally, the substrates used in the cultural medium are sustainable and industrial residuals can be used to produce value-added products. All these characteristics together have encouraged the ever-growing search for biocatalytic processes. The main industries that apply microbial enzymes are the food, textile, leather, pharmaceutical, cosmetics, fine chemicals, energy, biomaterials, paper, cellulose and detergent industries. Immobilization processes allow the reuse of these enzymes and increase stability. The enzymes and the microorganisms themselves have also been much used for bioremediation processes. \u0000 \u0000In this issue, the paper by B. Joseph et al. is about the production of cold-active lipases by semisolid fermentation and the paper by A. L. Willerding et al. is a study about lipases obtained from microorganisms isolated from soils in the Amazon. Studies with lipases immobilized for the synthesis of isopropyl acetate and isopropyl ferulate are presented in the papers by M. Lal Verma et al., A. Kumar and S. S. Kanwar, respectively. \u0000 \u0000The results of cellulase production optimization studies with cellulosic substrates and delignified Bambusa bambos are presented in the papers by D. Deka et al. and A. Kuila et al. The paper by R. C. Kuhad et al. is a review of the innumerous industrial applications of the cellulases. \u0000 \u0000The papers entitled “Bioconversion of agricultural waste to ethanol by SSF using recombinant cellulase from clostridium thermocellum,” “Petroleum-degrading enzymes: bioremediation and new prospects,” and “Assessment of the morphological, biochemical, and kinetic properties for Candida rugosa lipase \u0000 \u0000immobilized on hydrous niobium oxide to be used in the biodiesel synthesis” are about enzymes and biofuels: the use of a recombinant cellulase from Clostridium thermocellum for the production of ethanol from agro-industrial residues, a brief review on the role of enzymes that degrade oil, the use and description of the properties of a Candida rugosa lipase immobilized for the production of biodiesel. \u0000 \u0000The paper entitled “Laccase: microbial sources, production, purification, and potential biotechnological applications” is a review of the industrial applications of laccases, while the “Isolation, purification, and characterization of fungal laccase from Pleurotus sp.” and “Application of asymetrical and Hoke designs for optimization of ","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"980681"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/980681","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30568884","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pullulanase: role in starch hydrolysis and potential industrial applications.","authors":"Siew Ling Hii,&nbsp;Joo Shun Tan,&nbsp;Tau Chuan Ling,&nbsp;Arbakariya Bin Ariff","doi":"10.1155/2012/921362","DOIUrl":"https://doi.org/10.1155/2012/921362","url":null,"abstract":"<p><p>The use of pullulanase (EC 3.2.1.41) has recently been the subject of increased applications in starch-based industries especially those aimed for glucose production. Pullulanase, an important debranching enzyme, has been widely utilised to hydrolyse the α-1,6 glucosidic linkages in starch, amylopectin, pullulan, and related oligosaccharides, which enables a complete and efficient conversion of the branched polysaccharides into small fermentable sugars during saccharification process. The industrial manufacturing of glucose involves two successive enzymatic steps: liquefaction, carried out after gelatinisation by the action of α-amylase; saccharification, which results in further transformation of maltodextrins into glucose. During saccharification process, pullulanase has been used to increase the final glucose concentration with reduced amount of glucoamylase. Therefore, the reversion reaction that involves resynthesis of saccharides from glucose molecules is prevented. To date, five groups of pullulanase enzymes have been reported, that is, (i) pullulanase type I, (ii) amylopullulanase, (iii) neopullulanase, (iv) isopullulanase, and (v) pullulan hydrolase type III. The current paper extensively reviews each category of pullulanase, properties of pullulanase, merits of applying pullulanase during starch bioprocessing, current genetic engineering works related to pullulanase genes, and possible industrial applications of pullulanase.</p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"921362"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/921362","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30917586","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}