酶研究进展(英文)最新文献_第6页

Screening and Statistical Optimization of Physiochemical Parameters for the Production of Xylanases from Agro-Industrial Wastes 农工废弃物生产木聚糖酶理化参数筛选及统计优化

酶研究进展(英文) Pub Date : 2016-03-04 DOI: 10.4236/AER.2016.41003

Mirzaei Ali, M. Irshad, Z. Anwar, M. Zafar, M. Imran

{"title":"Screening and Statistical Optimization of Physiochemical Parameters for the Production of Xylanases from Agro-Industrial Wastes","authors":"Mirzaei Ali, M. Irshad, Z. Anwar, M. Zafar, M. Imran","doi":"10.4236/AER.2016.41003","DOIUrl":"https://doi.org/10.4236/AER.2016.41003","url":null,"abstract":"Xylanases are mostly produced through submerged fermentation; nonetheless solid-state fermentation has increased profound attention and consideration of scholars having high conversion level biomass to energy conservation. This study depicted the purification of xylanases and their possible utilization in industry. The present study was carried out to examine the culture influence of fungal strain Fomes fomentarius (F. fomentarius) using different agro-industrial residues (wheat straw, rice husk, sugarcane bagasse and siris pods). F. fomentarius showed maximum enzyme production after 72 h of fermentation, when grown on wheat straw in solid state fermentation process while maximum activity showed on pH 6.0 at 30°C. The other parameters optimized by statistical design (RSM) showed maximum xylanase activity (146 ± 8 IU/mL) at 65% moisture content, 4 mL inoculums size, 175 mg Ammonium sulphate, 200 mg Calcium carbonate and 1.4 grams of glucose. Xylanase was salted out at 60% ammonium sulphate concentration and enzyme was further purified by Sephadex G-100 gel filtration chromatography with 2.2 fold increase in activity. The purified xylanase from F. fomentarius had optimum pH 6.0 and 40°C. Xylanase showed higher specificity for oat spelt xylan with kinetic constants Km 1.25 mg/mL and Vmax 54 mM/min. Xylanases have an industrial important enzyme used extensively in food, feed and paper industry.","PeriodicalId":65616,"journal":{"name":"酶研究进展(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70485941","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 9

Polyphosphatase PPX1 of Saccharomyces cerevisiae as a Tool for Polyphosphate Assay 酿酒酵母菌的多磷酸酶PPX1作为多磷酸测定工具

酶研究进展(英文) Pub Date : 2015-12-01 DOI: 10.4236/AER.2015.34010

L. Lichko, T. Kulakovskaya

引用次数: 5

Isolation and Screening of Filamentous Fungi Producing Extracellular Lipase with Potential in Biodiesel Production 具有生物柴油生产潜力的产胞外脂肪酶丝状真菌的分离与筛选

酶研究进展(英文) Pub Date : 2015-12-01 DOI: 10.4236/AER.2015.34011

Sabrina Pacheco, Américo Cruz Júnior, Ayres Ferreira Morgado, A. F. Júnior, O. Amadi, J. Guisán, B. Pessela

引用次数: 16

A Novel Exo-Glucanase Explored from a Meyerozyma sp. Fungal Strain 从Meyerozyma sp.真菌菌株中发现一种新的外链葡聚糖酶

酶研究进展(英文) Pub Date : 2015-08-25 DOI: 10.4236/AER.2015.33006

H. Kuo, J. Zeng, Pinyi Wang, Wen-Chin Chen

{"title":"A Novel Exo-Glucanase Explored from a Meyerozyma sp. Fungal Strain","authors":"H. Kuo, J. Zeng, Pinyi Wang, Wen-Chin Chen","doi":"10.4236/AER.2015.33006","DOIUrl":"https://doi.org/10.4236/AER.2015.33006","url":null,"abstract":"Isolating cellulase-secreting microbes followed-by screening their cellulolytic activities has been an essential approach to discover novel and potential cellulases for cellulolytic industrial applications. This study was aimed to explore competitive exoglucanases by screening avicelase activities for 92 fungal strains isolated from environmental airborne-fungal-spore samples. Results showed that an isolated fungal strain numbered 58 exhibited the best avicelase activity of 0.209 U/mL when cultured for six days at pH 5.0 - 5.3 and 25℃ - 27℃, and was lately identified as a yeast strain of Meyerozyma sp. (96% ITS fragment similar with Meyerozyma caribbica, HG970748). Based on amino acid sequences revealed from LC/MS/MS, the target exoglucanase was identical to 1,4-beta-D-glucan cellobiohydrolases and was named Mc-CBHI which had optimal avicelase reaction conditions of pH 5 and 70℃ and could remain fairly stable after 4hr incubation at acid conditions (pH 3 - 5) or wide temperature ranges (30℃ - 80℃). Additionally, the Mc-CBHI (~70 kDa and ~3.6% of crude enzyme) had specific FPase and avicelase activities of 0.179 U/mg and 0.126 U/mg, respectively (which were about 40% - 50% activities of a commercial cellulase Accellerase-1000). These results demonstrated that the newly-found Mc-CBHI could become one of potential exoglucanase resources for related cellulolytic industrial applications.","PeriodicalId":65616,"journal":{"name":"酶研究进展(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70485426","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6

Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions 增强原油生物降解的初步研究揭示了具有显著区别的同类总过氧化物酶

酶研究进展(英文) Pub Date : 2015-08-25 DOI: 10.4236/AER.2015.33007

F. M. Olajuyigbe, K. Ehiosun, K. F. Jaiyesimi

{"title":"Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions","authors":"F. M. Olajuyigbe, K. Ehiosun, K. F. Jaiyesimi","doi":"10.4236/AER.2015.33007","DOIUrl":"https://doi.org/10.4236/AER.2015.33007","url":null,"abstract":"Peroxidases (POXs) are the key extracellular enzymes produced by crude oil degrading microbes. Knowledge of optimum conditions for POXs activity is crucial for providing effective environment for bioremediation. In this study, physicochemical properties of POXs produced by Actinomyces israelii and Actinomyces viscosus during growth on crude oil were studied. The POXs exhibited similarities in activity and stability with striking differences in response to two divalent metal ions. The POXs from both species had optimum pH of 7.0 and were very stable over a narrow pH range (6.0 - 8.0). The POXs demonstrated similar thermostability exhibiting relative residual activity of 62% at 50°C after 30 min incubation and 45% residual activity at the same temperature after 60 min despite the fact that POXs from A. viscosus and A. israelii had optimum temperatures of 50°C and 40°C, respectively. The POXs from A. viscosus and A. israelii were greatly activated by Fe2+ at 5.0 and 10.0 mM. The enzymes were both strongly inhibited by Cu2+, Mg2+ and Hg2+. Surprisingly, these congeneric POXs demonstrated striking differences in their response to Ca2+ and Mn2+. POX from A. viscosus was activated by Ca2+ and Mn2+ exhibiting relative activity of 136% and 106% at 5 mM, respectively. In contrast, POX from A. israelii was strongly inhibited by Ca2+ and Mn2+ exhibiting 62.5% relative activity in the presence of 5 mM of each metal ion. Increasing the concentration of Ca2+ and Mn2+ led to further activation of POX from A. viscosus and inhibition of POX from A. israelii. Results provide deeper insights into functional properties of studied POXs from closely related microbes. The physicochemical properties are very similar; however, notable differences provide a strong basis for structural characterization of these congeneric enzymes.","PeriodicalId":65616,"journal":{"name":"酶研究进展(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70485280","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 5

Production and Characterization of New Fibrinolytic Protease from Mucor subtillissimus UCP 1262 in Solid-State Fermentation 枯草毛霉ucp1262固态发酵生产新型纤溶蛋白酶及其特性研究

酶研究进展(英文) Pub Date : 2015-08-25 DOI: 10.4236/AER.2015.33009

T. Nascimento, A. E. Sales, C. S. Porto, Romero M P Brandão, Galba Maria C Takaki, J. Teixeira, T. S. Porto, A. Porto

{"title":"Production and Characterization of New Fibrinolytic Protease from Mucor subtillissimus UCP 1262 in Solid-State Fermentation","authors":"T. Nascimento, A. E. Sales, C. S. Porto, Romero M P Brandão, Galba Maria C Takaki, J. Teixeira, T. S. Porto, A. Porto","doi":"10.4236/AER.2015.33009","DOIUrl":"https://doi.org/10.4236/AER.2015.33009","url":null,"abstract":"Fibrinolytic enzymes have received attention regarding their medicinal potential for thrombolytic diseases, a leading cause of morbidity and mortality worldwide. Various natural enzymes purified from animal, plant and microbial sources have been extensively studied. The aim of this work was to produce fibrinolytic protease by solid state fermentation using agro industrial substrates. Rhizopus arrhizus var. arrhizus UCP 1295 and Mucor subtillissimus UCP 1262 filamentous fungi species isolated from soil of Caatinga-PE, Brasil, were used as producer microorganisms. Wheat bran was shown to be the best substrate for the production of the enzyme and by using a 23 full factorial design the main effects and interactions of the quantity of the substrate wheat bran, moisture and temperature on the fibrinolytic enzyme production and protease were evaluated. The best results for fibrinolytic and protease activities, 144.58 U/mL and 48.33 U/mL, respectively, were obtained with Mucor subtillissimus UCP 1262 using as culture medium 3 g wheat bran, 50% moisture at a temperature of 25°C for 72 hours. The optimum temperature for the produced enzyme was 45°C and most of its original activity was retained after being subjected to 80°C for 120 min. The protease activity was enhanced by K+, Ca+ and Mn+; but with Cu+ there was an inhibition. The specificity to chromogenic substrate and the inhibition by PMSF indicates that it is a chymotrypsin-like serine protease. Presented results suggest that this enzyme produced by solid-state fermentation is an interesting alternative as a candidate for thrombolytic therapy.","PeriodicalId":65616,"journal":{"name":"酶研究进展(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70485345","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 39

Subunit Arrangement of a 2-Ketoisovalerate Ferredoxin Oxidoreductase from Thermococcus profundus Revealed by a Low Resolution X-Ray Analysis 深热球菌2-酮异戊酸铁氧化还蛋白氧化还原酶亚基排列的低分辨率x射线分析

酶研究进展(英文) Pub Date : 2015-08-25 DOI: 10.4236/AER.2015.33008

Y. Ozawa, Y. Umena, T. Imai, Y. Morimoto

引用次数: 0

Phosphatase Hydrolysis of Organic Phosphorus Compounds 有机磷化合物的磷酸酶水解

酶研究进展(英文) Pub Date : 2015-06-10 DOI: 10.4236/AER.2015.32005

I. Tazisong, Z. Senwo, Zhongqi He

{"title":"Phosphatase Hydrolysis of Organic Phosphorus Compounds","authors":"I. Tazisong, Z. Senwo, Zhongqi He","doi":"10.4236/AER.2015.32005","DOIUrl":"https://doi.org/10.4236/AER.2015.32005","url":null,"abstract":"Phosphatases are diverse groups of enzymes that deserve special attention because of their significant roles in organic phosphorus (OP) mineralization to inorganic available forms (Pi). This work 1) compared the catalytic potentials of commercially acid phosphatase from wheat germ, sweet potato, and potato, and alkaline phosphatase from E. coli; 2) demonstrated that the rate of hydrolysis, catalytic efficiency, thermal stability, and optimal pH of these enzymes depended on enzyme sources and the stereochemical or stereoisomeric structures of the substrates; 3) revealed that both acid and alkaline phosphatases exhibited broad range of substrate hydrolysis with high affinity for p-nitrophenyl phosphate bis (cyclohexylammonium) than the widely used p-nitrophenyl phosphate disodium hexahydrate for phosphatase assay. Sweet potato had relatively higher reaction kinetics (Vmax, Km, Kcat, Kcat/Km) values with most substrates tested. The order of catalytic activity was in the order: sweet potato > wheat germ > potato, while the order of substrate hydrolyzed was: PNPBC > PNP > PNP2A2E > DG6P2Na > DG6PNa > Bis-PNP > phytate. The optimum pH for the acid phosphatase was observed to be 5.0. Generally, the activity of alkaline phosphatase was similar to that of acid phosphatase with optimal pH between 10 and 13, depending on the substrates. Knowledge derived from this work would be helpful in enzyme catalysis in soils and water environments.","PeriodicalId":65616,"journal":{"name":"酶研究进展(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70485415","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 20

Rubber Seed Kernel as Potent Solid Substrate for the Production of Lipase by Pseudomonas aeruginosa Strain BUP2 橡胶种子仁作为铜绿假单胞菌BUP2产脂酶的有效固体底物

酶研究进展(英文) Pub Date : 2015-06-10 DOI: 10.4236/AER.2015.32004

K. N. Unni, P. Faisal, P. Priji, S. Sajith, S. Sreedevi, E. S. Hareesh, Trikariyoor Asokan Nidheesh Roy, S. Benjamin

{"title":"Rubber Seed Kernel as Potent Solid Substrate for the Production of Lipase by Pseudomonas aeruginosa Strain BUP2","authors":"K. N. Unni, P. Faisal, P. Priji, S. Sajith, S. Sreedevi, E. S. Hareesh, Trikariyoor Asokan Nidheesh Roy, S. Benjamin","doi":"10.4236/AER.2015.32004","DOIUrl":"https://doi.org/10.4236/AER.2015.32004","url":null,"abstract":"This study explored the utility of flours of rubber seed, coconut and groundnut kernels, and de-oiled cakes of coconut and groundnut as solid substrate for the production of lipase by Pseudomonas aeruginosa strain BUP2 (MTCC No. 5924), a novel bacterium reported from the rumen of Malabari goat. Various proportions (10%, 20%, 30%, 40% or 50%) of flours or cakes were prepared (w/v) with BUP medium (pH 4, 5, 6, 7 or 8), and incubated at different temperature (25°C, 28°C, 30°C or 32°C) for 24 to 96 h. The samples were assayed for lipase activity at 24 h intervals. The rubber seed flour (20%)-BUP medium supported the maximum lipase production (871 U/gds) at 48h incubation (pH 6, 28°C), followed by ground nut flour (398 U/gds), while ground nut cake supported the least lipase production (244 U/gds). From this, it is evident that the cheaply available rubber seed is an efficient substrate for the production of lipase, irrespective of its known demerit that it contains the limarin, a toxin; in fact, we could not detect limarin in the fermented matter. Thus, the utility of rubber seed for the production of a costly enzyme is reported from a novel rumen bacterium, which would be advantageous for rubber farmers.","PeriodicalId":65616,"journal":{"name":"酶研究进展(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70485363","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 1

Spectrofluorometric Assays of Human Collagenase Activity Using Native Collagen and Acetyl-Peptide Substrates 用天然胶原和乙酰肽底物测定人胶原酶活性的荧光光谱法

酶研究进展(英文) Pub Date : 2015-03-02 DOI: 10.4236/AER.2015.31003

Valon Ejupi, Shpend Dragusha, T. Kabashima, Qinchang Zhu, A. EL-Mahdy, Sheng Yin, T. Shibata, M. Kai

{"title":"Spectrofluorometric Assays of Human Collagenase Activity Using Native Collagen and Acetyl-Peptide Substrates","authors":"Valon Ejupi, Shpend Dragusha, T. Kabashima, Qinchang Zhu, A. EL-Mahdy, Sheng Yin, T. Shibata, M. Kai","doi":"10.4236/AER.2015.31003","DOIUrl":"https://doi.org/10.4236/AER.2015.31003","url":null,"abstract":"A selective, sensitive, and convenient assay for human collagenase is required because of its implication in diseases such as rheumatoid arthritis, osteoarthritis, and tumors. Here, a novel assay for human collagenase activity is described in which enzymatic degradation of native collagen or acetyl peptide is determined by using a fluorogenic reaction for oligopeptides. The oligopeptides are quantified spectrofluorometrically with either 3,4-dihydroxyphenylacetic acid or 1,2-dihydroxybenzen reaction in the presence of sodium periodate and sodium borate (pH 7 - 8). These reactions can selectively convert N-terminal Gly-containing oligopeptides and N-terminal Ile-containing oligopeptides to fluorescence (FL) compounds, respectively, but not proteins, acetyl peptides or amino acids. Under optimized conditions using 1.65 μM collagen IV or 1.5 mM Ac-GPQGI- AGQ as substrates, this assay exhibits a proportional relationship between FL intensities and human collagenase-3 (MMP-13) concentrations. It can assay endogenous collagenase activities in several biological samples, such as cultured human cells and cheek tissue.","PeriodicalId":65616,"journal":{"name":"酶研究进展(英文)","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-03-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4236/AER.2015.31003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70485323","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 1