Enzyme Research最新文献_第3页

Highly Active and Stable Large Catalase Isolated from a Hydrocarbon Degrading Aspergillus terreus MTCC 6324 土曲霉MTCC 6324高效稳定的大型过氧化氢酶

Enzyme Research Pub Date : 2016-01-19 DOI: 10.1155/2016/4379403

Preety Vatsyayan, P. Goswami

{"title":"Highly Active and Stable Large Catalase Isolated from a Hydrocarbon Degrading Aspergillus terreus MTCC 6324","authors":"Preety Vatsyayan, P. Goswami","doi":"10.1155/2016/4379403","DOIUrl":"https://doi.org/10.1155/2016/4379403","url":null,"abstract":"A hydrocarbon degrading Aspergillus terreus MTCC 6324 produces a high level of extremely active and stable cellular large catalase (CAT) during growth on n-hexadecane to combat the oxidative stress caused by the hydrocarbon degrading metabolic machinery inside the cell. A 160-fold purification with specific activity of around 66 × 105 U mg−1 protein was achieved. The native protein molecular mass was 368 ± 5 kDa with subunit molecular mass of nearly 90 kDa, which indicates that the native CAT protein is a homotetramer. The isoelectric pH (pI) of the purified CAT was 4.2. BLAST aligned peptide mass fragments of CAT protein showed its highest similarity with the catalase B protein from other fungal sources. CAT was active in a broad range of pH 4 to 12 and temperature 25°C to 90°C. The catalytic efficiency (K cat/K m) of 4.7 × 108 M−1 s−1 within the studied substrate range and alkaline pH stability (half-life, t 1/2 at pH 12~15 months) of CAT are considerably higher than most of the extensively studied catalases from different sources. The storage stability (t 1/2) of CAT at physiological pH 7.5 and 4°C was nearly 30 months. The haem was identified as haem b by electrospray ionization tandem mass spectroscopy (ESI-MS/MS).","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89613629","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: 14

Immunomodulatory Effects of Chitotriosidase Enzyme 壳三酸苷酶的免疫调节作用

Enzyme Research Pub Date : 2016-01-03 DOI: 10.1155/2016/2682680

M. A. Elmonem, L. P. Van den Heuvel, E. Levtchenko

引用次数: 51

Production of Thermoalkaliphilic Lipase from Geobacillus thermoleovorans DA2 and Application in Leather Industry 热嗜碱地杆菌DA2产热嗜碱脂肪酶及其在皮革工业中的应用

Enzyme Research Pub Date : 2016-01-03 DOI: 10.1155/2016/9034364

Deyaa M. Abol Fotouh, R. Bayoumi, M. Hassan

{"title":"Production of Thermoalkaliphilic Lipase from Geobacillus thermoleovorans DA2 and Application in Leather Industry","authors":"Deyaa M. Abol Fotouh, R. Bayoumi, M. Hassan","doi":"10.1155/2016/9034364","DOIUrl":"https://doi.org/10.1155/2016/9034364","url":null,"abstract":"Thermophilic and alkaliphilic lipases are meeting a growing global attention as their increased importance in several industrial fields. Over 23 bacterial strains, novel strain with high lipolytic activity was isolated from Southern Sinai, Egypt, and it was identified as Geobacillus thermoleovorans DA2 using 16S rRNA as well as morphological and biochemical features. The lipase was produced in presence of fatty restaurant wastes as an inducing substrate. The optimized conditions for lipase production were recorded to be temperature 60°C, pH 10, and incubation time for 48 hrs. Enzymatic production increased when the organism was grown in a medium containing galactose as carbon source and ammonium phosphate as nitrogen source at concentrations of 1 and 0.5% (w/v), respectively. Moreover, the optimum conditions for lipase production such as substrate concentration, inoculum size, and agitation rate were found to be 10% (w/v), 4% (v/v), and 120 rpm, respectively. The TA lipase with Triton X-100 had the best degreasing agent by lowering the total lipid content to 2.6% as compared to kerosene (7.5%) or the sole crude enzyme (8.9%). It can be concluded that the chemical leather process can be substituted with TA lipase for boosting the quality of leather and reducing the environmental hazards.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77853204","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: 66

Salivary Myeloperoxidase, Assessed by 3,3'-Diaminobenzidine Colorimetry, Can Differentiate Periodontal Patients from Nonperiodontal Subjects. 用3,3′-二氨基联苯胺比色法评估唾液髓过氧化物酶，可以区分牙周患者和非牙周受试者。

Enzyme Research Pub Date : 2016-01-01 Epub Date: 2016-05-05 DOI: 10.1155/2016/7517928

Supaporn Klangprapan, Ponlatham Chaiyarit, Doosadee Hormdee, Amonrujee Kampichai, Tueanjit Khampitak, Jureerut Daduang, Ratree Tavichakorntrakool, Bhinyo Panijpan, Patcharee Boonsiri

{"title":"Salivary Myeloperoxidase, Assessed by 3,3'-Diaminobenzidine Colorimetry, Can Differentiate Periodontal Patients from Nonperiodontal Subjects.","authors":"Supaporn Klangprapan, Ponlatham Chaiyarit, Doosadee Hormdee, Amonrujee Kampichai, Tueanjit Khampitak, Jureerut Daduang, Ratree Tavichakorntrakool, Bhinyo Panijpan, Patcharee Boonsiri","doi":"10.1155/2016/7517928","DOIUrl":"https://doi.org/10.1155/2016/7517928","url":null,"abstract":"Periodontal diseases, which result from inflammation of tooth supporting tissues, are highly prevalent worldwide. Myeloperoxidase (MPO), from certain white blood cells in saliva, is a biomarker for inflammation. We report our study on the salivary MPO activity and its association with severity of periodontal diseases among Thai patients. Periodontally healthy subjects (n = 11) and gingivitis (n = 32) and periodontitis patients (n = 19) were enrolled. Assessments of clinically periodontal parameters were reported as percentages for gingival bleeding index (GI) and bleeding on probing (BOP), whereas pocket depth (PD) and clinical attachment loss (CAL) were measured in millimeters and then made to index scores. Salivary MPO activity was measured by colorimetry using 3,3'-diaminobenzidine as substrate. The results showed that salivary MPO activity in periodontitis patients was significantly higher than in healthy subjects (p = 0.003) and higher than in gingivitis patients (p = 0.059). No difference was found between gingivitis and healthy groups (p = 0.181). Significant correlations were observed (p < 0.01) between salivary MPO activity and GI (r = 0.632, p < 0.001), BOP (r = 0.599, p < 0.001), PD (r = 0.179, p = 0.164), and CAL (r = 0.357, p = 0.004) index scores. Sensitivity (94.12%), specificity (54.55%), and positive (90.57%) and negative (66.67%) predictive values indicate that salivary MPO activity has potential use as a screening marker for oral health of the Thai community. ","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2016/7517928","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34620763","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: 9

Agroindustrial Wastes as Alternative for Lipase Production by Candida viswanathii under Solid-State Cultivation: Purification, Biochemical Properties, and Its Potential for Poultry Fat Hydrolysis. 农用工业废料作为固态培养条件下由 Candida viswanathii 生产脂肪酶的替代品：纯化、生化特性及其用于家禽脂肪水解的潜力。

Enzyme Research Pub Date : 2016-01-01 Epub Date: 2016-09-20 DOI: 10.1155/2016/1353497

Alex Fernando de Almeida, Kleydiane Braga Dias, Ana Carolina Cerri da Silva, César Rafael Fanchini Terrasan, Sâmia Maria Tauk-Tornisielo, Eleonora Cano Carmona

{"title":"Agroindustrial Wastes as Alternative for Lipase Production by Candida viswanathii under Solid-State Cultivation: Purification, Biochemical Properties, and Its Potential for Poultry Fat Hydrolysis.","authors":"Alex Fernando de Almeida, Kleydiane Braga Dias, Ana Carolina Cerri da Silva, César Rafael Fanchini Terrasan, Sâmia Maria Tauk-Tornisielo, Eleonora Cano Carmona","doi":"10.1155/2016/1353497","DOIUrl":"10.1155/2016/1353497","url":null,"abstract":"The aims of this work were to establish improved conditions for lipase production by Candida viswanathii using agroindustrial wastes in solid-state cultivation and to purify and evaluate the application of this enzyme for poultry fat hydrolysis. Mixed wheat bran plus spent barley grain (1 : 1, w/w) supplemented with 25.0% (w/w) olive oil increased the lipase production to 322.4%, compared to the initial conditions. When olive oil was replaced by poultry fat, the highest lipase production found at 40% (w/w) was 31.43 U/gds. By selecting, yeast extract supplementation (3.5%, w/w), cultivation temperature (30°C), and substrate moisture (40%, w/v), lipase production reached 157.33 U/gds. Lipase was purified by hydrophobic interaction chromatography, presenting a molecular weight of 18.5 kDa as determined by SDS-PAGE. The crude and purified enzyme showed optimum activity at pH 5.0 and 50°C and at pH 5.5 and 45°C, respectively. The estimated half-life at 50°C was of 23.5 h for crude lipase and 6.7 h at 40°C for purified lipase. Lipase presented high activity and stability in many organic solvents. Poultry fat hydrolysis was maximum at pH 4.0, reaching initial hydrolysis rate of 33.17 mmol/L/min. Thus, C. viswanathii lipase can be successfully produced by an economic and sustainable process and advantageously applied for poultry fat hydrolysis without an additional acidification step to recover the released fatty acids.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5048095/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80100616","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

A Comparative Study of New Aspergillus Strains for Proteolytic Enzymes Production by Solid State Fermentation. 利用固体发酵法生产蛋白水解酶的曲霉新菌株比较研究

Enzyme Research Pub Date : 2016-01-01 Epub Date: 2016-02-16 DOI: 10.1155/2016/3016149

Gastón Ezequiel Ortiz, Diego Gabriel Noseda, María Clara Ponce Mora, Matías Nicolás Recupero, Martín Blasco, Edgardo Albertó

{"title":"A Comparative Study of New Aspergillus Strains for Proteolytic Enzymes Production by Solid State Fermentation.","authors":"Gastón Ezequiel Ortiz, Diego Gabriel Noseda, María Clara Ponce Mora, Matías Nicolás Recupero, Martín Blasco, Edgardo Albertó","doi":"10.1155/2016/3016149","DOIUrl":"10.1155/2016/3016149","url":null,"abstract":"A comparative study of the proteolytic enzymes production using twelve Aspergillus strains previously unused for this purpose was performed by solid state fermentation. A semiquantitative and quantitative evaluation of proteolytic activity were carried out using crude enzymatic extracts obtained from the fermentation cultures, finding seven strains with high and intermediate level of protease activity. Biochemical, thermodynamics, and kinetics features such as optimum pH and temperature values, thermal stability, activation energy (E a), quotient energy (Q 10), K m , and V max were studied in four enzymatic extracts from the selected strains that showed the highest productivity. Additionally, these strains were evaluated by zymogram analysis obtaining protease profiles with a wide range of molecular weight for each sample. From these four strains with the highest productivity, the proteolytic extract of A. sojae ATCC 20235 was shown to be an appropriate biocatalyst for hydrolysis of casein and gelatin substrates, increasing its antioxidant activities in 35% and 125%, respectively. ","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4771904/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76393693","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

Diagnostic Value of Adenosine Deaminase and Its Isoforms in Type II Diabetes Mellitus. 腺苷脱氨酶及其同工酶对 II 型糖尿病的诊断价值

Enzyme Research Pub Date : 2016-01-01 Epub Date: 2016-12-05 DOI: 10.1155/2016/9526593

Bagher Larijani, Ramin Heshmat, Mina Ebrahimi-Rad, Shohreh Khatami, Shirin Valadbeigi, Reza Saghiri

引用次数: 0

Modulation of Aromatase by Phytoestrogens 植物雌激素对芳香酶的调节作用

Enzyme Research Pub Date : 2015-12-21 DOI: 10.1155/2015/594656

E. Lephart

{"title":"Modulation of Aromatase by Phytoestrogens","authors":"E. Lephart","doi":"10.1155/2015/594656","DOIUrl":"https://doi.org/10.1155/2015/594656","url":null,"abstract":"The aromatase enzyme catalyzes the conversion of androgens to estrogens in many human tissues. Estrogens are known to stimulate cellular proliferation associated with certain cancers and protect against adverse symptoms during the peri- and postmenopausal intervals. Phytoestrogens are a group of plant derived naturally occurring compounds that have chemical structures similar to estrogen. Since phytoestrogens are known to be constituents of animal/human food sources, these compounds have received increased research attention. Phytoestrogens may contribute to decreased cancer risk by the inhibition of aromatase enzyme activity and CYP19 gene expression in human tissues. This review covers (a) the aromatase enzyme (historical descriptions on function, activity, and gene characteristics), (b) phytoestrogens in their classifications and applications to human health, and (c) a chronological coverage of aromatase activity modulated by phytoestrogens from the early 1980s to 2015. In general, phytoestrogens act as aromatase inhibitors by (a) decreasing aromatase gene expression, (b) inhibiting the aromatase enzyme itself, or (c) in some cases acting at both levels of regulation. The findings presented herein are consistent with estrogen's impact on health and phytoestrogen's potential as anticancer treatments, but well-controlled, large-scale studies are warranted to determine the effectiveness of phytoestrogens on breast cancer and age-related diseases.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82694612","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: 53

Estimation of Inhibitory Effect against Tyrosinase Activity through Homology Modeling and Molecular Docking 基于同源建模和分子对接的酪氨酸酶活性抑制效应评估

Enzyme Research Pub Date : 2015-12-15 DOI: 10.1155/2015/262364

Daungkamon Nokinsee, L. Shank, V. Lee, P. Nimmanpipug

引用次数: 33

Chitinases from Bacteria to Human: Properties, Applications, and Future Perspectives 从细菌到人类的几丁质酶:性质、应用和未来展望

Enzyme Research Pub Date : 2015-11-19 DOI: 10.1155/2015/791907

A. Rathore, R. Gupta

引用次数: 152