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":"19 1","pages":""},"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":"79 1-2 1","pages":""},"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":"<p><p>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. </p>","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2016 ","pages":"7517928"},"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

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":"53 1","pages":""},"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

Extracellular Polyhydroxyalkanoate Depolymerase by Acidovorax sp. DP5 胞外聚羟基烷酸解聚酶(Acidovorax sp. DP5)

Enzyme Research Pub Date : 2015-11-17 DOI: 10.1155/2015/212159

S. Vigneswari, T. S. Lee, K. Bhubalan, A. Amirul

{"title":"Extracellular Polyhydroxyalkanoate Depolymerase by Acidovorax sp. DP5","authors":"S. Vigneswari, T. S. Lee, K. Bhubalan, A. Amirul","doi":"10.1155/2015/212159","DOIUrl":"https://doi.org/10.1155/2015/212159","url":null,"abstract":"Bacteria capable of degrading polyhydroxyalkanoates (PHA) by secreting extracellular depolymerase enzymes were isolated from water and soil samples collected from various environments in Malaysia. A total of 8 potential degraders exhibited clear zones on poly(3-hydroxybutyrate) [P(3HB)] based agar, indicating the presence of extracellular PHA depolymerase. Among the isolates, DP5 exhibited the largest clearing zone with a degradation index of 6.0. The highest degradation activity of P(3HB) was also observed with depolymerase enzyme of DP5 in mineral salt medium containing P(3HB). Based on biochemical characterization and 16S rRNA cloning and sequencing, isolate DP5 was found to belong to the genus Acidovorax and subsequently named as Acidovorax sp. DP5. The highest extracellular depolymerase enzyme activity was achieved when 0.25% (w/v) of P(3HB) and 1 g/L of urea were used as carbon and nitrogen source, respectively, in the culture media. The most suitable assay condition of the depolymerase enzyme in response to pH and temperature was tested. The depolymerase produced by strain Acidovorax sp. DP5 showed high percentage of degradation with P(3HB) films in an alkaline condition with pH 9 and at a temperature of 40°C.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"12 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2015-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78917110","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: 25

Determining the IC50 Values for Vorozole and Letrozole, on a Series of Human Liver Cytochrome P450s, to Help Determine the Binding Site of Vorozole in the Liver 测定Vorozole和来曲唑在一系列人肝细胞色素p450上的IC50值，以帮助确定Vorozole在肝脏中的结合位点

Enzyme Research Pub Date : 2015-11-09 DOI: 10.1155/2015/321820

Lendelle Raymond, Nikita Rayani, Grace Polson, Kylie F. Sikorski, Ailin Lian, Melissa A. VanAlstine-Parris

{"title":"Determining the IC50 Values for Vorozole and Letrozole, on a Series of Human Liver Cytochrome P450s, to Help Determine the Binding Site of Vorozole in the Liver","authors":"Lendelle Raymond, Nikita Rayani, Grace Polson, Kylie F. Sikorski, Ailin Lian, Melissa A. VanAlstine-Parris","doi":"10.1155/2015/321820","DOIUrl":"https://doi.org/10.1155/2015/321820","url":null,"abstract":"Vorozole and letrozole are third-generation aromatase (cytochrome P450 19A1) inhibitors. [11C]-Vorozole can be used as a radiotracer for aromatase in living animals but when administered by IV, it collects in the liver. Pretreatment with letrozole does not affect the binding of vorozole in the liver. In search of finding the protein responsible for the accumulation of vorozole in the liver, fluorometric high-throughput screening assays were used to test the inhibitory capability of vorozole and letrozole on a series of liver cytochrome P450s (CYP1A1, CYP1A2, CYP2A6, and CYP3A4). It was determined that vorozole is a potent inhibitor of CYP1A1 (IC50 = 0.469 μM) and a moderate inhibitor of CYP2A6 and CYP3A4 (IC50 = 24.4 and 98.1 μM, resp.). Letrozole is only a moderate inhibitor of CYP1A1 and CYP2A6 (IC50 = 69.8 and 106 μM) and a very weak inhibitor of CYP3A4 (<10% inhibition at 1 mM). Since CYP3A4 makes up the majority of the CYP content found in the human liver, and vorozole inhibits it moderately well but letrozole does not, CYP3A4 is a good candidate for the protein that [11C]-vorozole is binding to in the liver.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"59 3 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2015-11-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83030966","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

Lactose Hydrolysis in Milk and Dairy Whey Using Microbial β-Galactosidases 利用微生物β-半乳糖苷酶水解牛奶和乳清中的乳糖

Enzyme Research Pub Date : 2015-10-26 DOI: 10.1155/2015/806240

Michele Dutra Rosolen, Adriano Gennari, G. Volpato, C. F. Volken de Souza

{"title":"Lactose Hydrolysis in Milk and Dairy Whey Using Microbial β-Galactosidases","authors":"Michele Dutra Rosolen, Adriano Gennari, G. Volpato, C. F. Volken de Souza","doi":"10.1155/2015/806240","DOIUrl":"https://doi.org/10.1155/2015/806240","url":null,"abstract":"This work aimed at evaluating the influence of enzyme concentration, temperature, and reaction time in the lactose hydrolysis process in milk, cheese whey, and whey permeate, using two commercial β-galactosidases of microbial origins. We used Aspergillus oryzae (at temperatures of 10 and 55°C) and Kluyveromyces lactis (at temperatures of 10 and 37°C) β-galactosidases, both in 3, 6, and 9 U/mL concentrations. In the temperature of 10°C, the K. lactis β-galactosidase enzyme is more efficient in the milk, cheese whey, and whey permeate lactose hydrolysis when compared to A. oryzae. However, in the enzyme reaction time and concentration conditions evaluated, 100% lactose hydrolysis was not reached using the K. lactis β-galactosidase. The total lactose hydrolysis in whey and permeate was obtained with the A. oryzae enzyme, when using its optimum temperature (55°C), at the end of a 12 h reaction, regardless of the enzyme concentration used. For the lactose present in milk, this result occurred in the concentrations of 6 and 9 U/mL, with the same time and temperature conditions. The studied parameters in the lactose enzymatic hydrolysis are critical for enabling the application of β-galactosidases in the food industry.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"33 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2015-10-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91256147","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: 56