Enzyme Research最新文献_第10页

A Thermostable Crude Endoglucanase Produced by Aspergillus fumigatus in a Novel Solid State Fermentation Process Using Isolated Free Water. 利用分离自由水的新型固态发酵过程中由曲霉产生的一种恒温粗内切葡聚糖酶

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-07-08 DOI: 10.1155/2012/196853

Abdul A N Saqib, Ansa Farooq, Maryam Iqbal, Jalees Ul Hassan, Umar Hayat, Shahjahan Baig

{"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":"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.","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}

引用次数: 0

Inhibition of heme peroxidases by melamine. 三聚氰胺对血红素过氧化物酶的抑制作用。

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-07-18 DOI: 10.1155/2012/416062

Pattaraporn Vanachayangkul, William H Tolleson

{"title":"Inhibition of heme peroxidases by melamine.","authors":"Pattaraporn Vanachayangkul, William H Tolleson","doi":"10.1155/2012/416062","DOIUrl":"https://doi.org/10.1155/2012/416062","url":null,"abstract":"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.","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}

引用次数: 10

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. 农业残留物固体发酵经济生产热碱稳定型果胶酶的生物技术潜力及其对苎麻纤维的处理效果。

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-08-08 DOI: 10.1155/2012/281384

Deepak Chand Sharma, T Satyanarayana

{"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, T Satyanarayana","doi":"10.1155/2012/281384","DOIUrl":"https://doi.org/10.1155/2012/281384","url":null,"abstract":"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.","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}

引用次数: 28

Application of Statistical Design for the Production of Cellulase by Trichoderma reesei Using Mango Peel. 统计设计在里氏木霉利用芒果皮生产纤维素酶中的应用。

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-12-06 DOI: 10.1155/2012/157643

P Saravanan, R Muthuvelayudham, T Viruthagiri

引用次数: 34

Kinetic Analysis of Guanidine Hydrochloride Inactivation of β-Galactosidase in the Presence of Galactose. 半乳糖存在下盐酸胍对β-半乳糖苷酶失活的动力学分析。

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-09-13 DOI: 10.1155/2012/173831

Charles O Nwamba, Ferdinand C Chilaka

{"title":"Kinetic Analysis of Guanidine Hydrochloride Inactivation of β-Galactosidase in the Presence of Galactose.","authors":"Charles O Nwamba, Ferdinand C Chilaka","doi":"10.1155/2012/173831","DOIUrl":"https://doi.org/10.1155/2012/173831","url":null,"abstract":"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.","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}

引用次数: 5

Brain Levels of Catalase Remain Constant through Strain, Developmental, and Chronic Alcohol Challenges. 大脑过氧化氢酶水平通过应变、发育和慢性酒精挑战保持不变。

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-08-05 DOI: 10.1155/2012/572939

Dennis E Rhoads, Cherly Contreras, Salma Fathalla

{"title":"Brain Levels of Catalase Remain Constant through Strain, Developmental, and Chronic Alcohol Challenges.","authors":"Dennis E Rhoads, Cherly Contreras, Salma Fathalla","doi":"10.1155/2012/572939","DOIUrl":"https://doi.org/10.1155/2012/572939","url":null,"abstract":"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.","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}

引用次数: 10

Hydrolysis of virgin coconut oil using immobilized lipase in a batch reactor. 固定化脂肪酶在间歇反应器中水解初榨椰子油。

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-08-16 DOI: 10.1155/2012/542589

Lee Suan Chua, Meisam Alitabarimansor, Chew Tin Lee, Ramli Mat

{"title":"Hydrolysis of virgin coconut oil using immobilized lipase in a batch reactor.","authors":"Lee Suan Chua, Meisam Alitabarimansor, Chew Tin Lee, Ramli Mat","doi":"10.1155/2012/542589","DOIUrl":"https://doi.org/10.1155/2012/542589","url":null,"abstract":"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.","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}

引用次数: 28

Optimal Conditions for Continuous Immobilization of Pseudozyma hubeiensis (Strain HB85A) Lipase by Adsorption in a Packed-Bed Reactor by Response Surface Methodology. 响应面法连续固定化湖北假酵素(HB85A)脂肪酶的最佳条件研究

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-01-23 DOI: 10.1155/2012/329178

Roberta Bussamara, Luciane Dall'agnol, Augusto Schrank, Kátia Flávia Fernandes, Marilene Henning Vainstein

{"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, Luciane Dall'agnol, Augusto Schrank, Kátia Flávia Fernandes, Marilene Henning Vainstein","doi":"10.1155/2012/329178","DOIUrl":"https://doi.org/10.1155/2012/329178","url":null,"abstract":"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.","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}

引用次数: 42

Pullulanase: role in starch hydrolysis and potential industrial applications. 普鲁兰酶:在淀粉水解中的作用和潜在的工业应用。

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-09-06 DOI: 10.1155/2012/921362

Siew Ling Hii, Joo Shun Tan, Tau Chuan Ling, Arbakariya Bin Ariff

{"title":"Pullulanase: role in starch hydrolysis and potential industrial applications.","authors":"Siew Ling Hii, Joo Shun Tan, Tau Chuan Ling, Arbakariya Bin Ariff","doi":"10.1155/2012/921362","DOIUrl":"https://doi.org/10.1155/2012/921362","url":null,"abstract":"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.","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}

引用次数: 259

Production, Purification, and Characterization of Polygalacturonase from Rhizomucor pusillus Isolated from Decomposting Orange Peels. 从橘子皮分解中分离的根霉聚半乳糖醛酸酶的生产、纯化和特性研究。

Enzyme Research Pub Date : 2012-01-01 Epub Date: 2012-10-17 DOI: 10.1155/2012/138634

Mohd Asif Siddiqui, Veena Pande, Mohammad Arif

{"title":"Production, Purification, and Characterization of Polygalacturonase from Rhizomucor pusillus Isolated from Decomposting Orange Peels.","authors":"Mohd Asif Siddiqui, Veena Pande, Mohammad Arif","doi":"10.1155/2012/138634","DOIUrl":"https://doi.org/10.1155/2012/138634","url":null,"abstract":"A thermophilic fungal strain producing polygalacturonase was isolated after primary screening of 40 different isolates. The fungus was identified as Rhizomucor pusilis by Microbial Type Culture Collection (MTCC), Chandigarh, India. An extracellular polygalacturonase (PGase) from R. pusilis was purified to homogeneity by two chromatographic steps using Sephadex G-200 and Sephacryl S-100. The purified enzyme was a monomer with a molecular weight of 32 kDa. The PGase was optimally active at 55°C and at pH 5.0. It was stable up to 50°C for 120 min of incubation and pH condition between 4.0 and 5.0. The stability of PGase decreases rapidly above 60°C and above pH 5.0. The apparent K(m) and V(max) values were 0.22 mg/mL and 4.34 U/mL, respectively. It was the first time that a polygalacturonase enzyme was purified in this species. It would be worthwhile to exploit this strain for polygalacturonase production. Polygalacturonase from this strain can be recommended for the commercial production because of its constitutive and less catabolically repressive nature, thermostability, wide range of pH, and lower K(m) properties. However, scale-up studies are needed for the better output for commercial production.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2012 ","pages":"138634"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/138634","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31027134","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}

引用次数: 42