Enzyme Research最新文献

Isolation of Cellulose Degrading Fungi from Decaying Banana Pseudostem and Strelitzia alba 香蕉假茎和白条中纤维素降解真菌的分离

Enzyme Research Pub Date : 2019-07-25 DOI: 10.1155/2019/1390890

L. M. Legodi, D. L. la Grange, E. van Rensburg, I. Ncube

{"title":"Isolation of Cellulose Degrading Fungi from Decaying Banana Pseudostem and Strelitzia alba","authors":"L. M. Legodi, D. L. la Grange, E. van Rensburg, I. Ncube","doi":"10.1155/2019/1390890","DOIUrl":"https://doi.org/10.1155/2019/1390890","url":null,"abstract":"Cellulases are a group of hydrolytic enzymes that break down cellulose to glucose units. These enzymes are used in the food, beverage, textile, pulp, and paper and the biofuel industries. The aim of this study was to isolate fungi from natural compost and produce cellulases in submerged fermentation (SmF). Initial selection was based on the ability of the fungi to grow on agar containing Avicel followed by cellulase activity determination in the form of endoglucanase and total cellulase activity. Ten fungal isolates obtained from the screening process showed good endoglucanase activity on carboxymethyl cellulose-Congo Red agar plates. Six of the fungal isolates were selected based on high total cellulase activity and identified as belonging to the genera Trichoderma and Aspergillus. In SmF of synthetic media with an initial pH of 6.5 at 30°C Trichoderma longibrachiatum LMLSAUL 14-1 produced total cellulase activity of 8 FPU/mL and endoglucanase activity of 23 U/mL whilst Trichoderma harzianum LMLBP07 13-5 produced 6 FPU/mL and endoglucanase activity of 16 U/mL. The produced levels of both cellulases and endoglucanase by Trichoderma species were higher than the levels for the Aspergillus fumigatus strains. Aspergillus fumigatus LMLPS 13-4 produced higher β-glucosidase 38 U/mL activity than Trichoderma species.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"112 9","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-07-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2019/1390890","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72376904","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: 31

Acetylcholinesterases from Leaf-Cutting ant Atta sexdens: Purification, Characterization, and Capillary Reactors for On-Flow Assays 切叶蚁的乙酰胆碱酯酶:纯化、表征和毛细管反应器的流动分析

Enzyme Research Pub Date : 2019-07-01 DOI: 10.1155/2019/6139863

A. M. dos Santos, A. Moreira, Bianca Rebelo Lopes, Mariana F. Fracola, F. G. de Almeida, O. Bueno, Q. Cass, D. H. Souza

{"title":"Acetylcholinesterases from Leaf-Cutting ant Atta sexdens: Purification, Characterization, and Capillary Reactors for On-Flow Assays","authors":"A. M. dos Santos, A. Moreira, Bianca Rebelo Lopes, Mariana F. Fracola, F. G. de Almeida, O. Bueno, Q. Cass, D. H. Souza","doi":"10.1155/2019/6139863","DOIUrl":"https://doi.org/10.1155/2019/6139863","url":null,"abstract":"Acetylcholinesterase (AChE) is responsible for catalyzing the hydrolysis of the neurotransmitter acetylcholine (ACh) leading to acetate and choline (Ch) release. The inhibition of AChE produces a generalized synaptic collapse that can lead to insect death. Herein we report for the first time the isolation of two AChEs from Atta sexdens which were purified by sulphate ammonium precipitation followed by ion exchange chromatography. AsAChE-A and AsAChE-B enzymes have optimum pH of 9.5 and 9.0 and higher activities in 30/50°C and 20°C, respectively, using acetylthiocholine (ATCh) as substrate. Immobilized capillary enzyme reactors (ICERs) were obtained for both enzymes (AsAChE-A-ICER and AsAChE-B-ICER) and their activities were measured by LC-MS/MS through hydrolysis product quantification of the natural substrate ACh. The comparison of activities by LC-MS/MS of both AChEs using ACh as substrate showed that AsAChE-B (free or immobilized) had the highest affinity. The inverse result was observed when the colorimetric assay (Elman method) was used for ATCh as substrate. Moreover, by mass spectrometry and phylogenetic studies, AsAChE-A and AsAChE-B were classified as belonging to AChE-2 and AChE-1 classes, respectively.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"212 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76161562","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

Lipolytic Enzymes with Hydrolytic and Esterification Activities Produced by Filamentous Fungi Isolated from Decomposition Leaves in an Aquatic Environment. 水生环境中从分解叶中分离的丝状真菌产生的具有水解和酯化活性的脂解酶。

Enzyme Research Pub Date : 2019-06-02 eCollection Date: 2019-01-01 DOI: 10.1155/2019/8182425

D B Mendes, F F Da Silva, P M Guarda, A F Almeida, D P de Oliveira, P B Morais, E A Guarda

{"title":"Lipolytic Enzymes with Hydrolytic and Esterification Activities Produced by Filamentous Fungi Isolated from Decomposition Leaves in an Aquatic Environment.","authors":"D B Mendes, F F Da Silva, P M Guarda, A F Almeida, D P de Oliveira, P B Morais, E A Guarda","doi":"10.1155/2019/8182425","DOIUrl":"10.1155/2019/8182425","url":null,"abstract":"Microbial lipases are prominent biocatalysts able to catalyze a wide variety of reactions in aqueous and nonaqueous media. In this work, filamentous fungi isolated from leaves decomposed in an aquatic environment were screened for lipase production with hydrolytic activity and esterification. Agar plates with Tween 20 and Rhodamine B were used for selection, while submerged cultures with olive oil were subsequently used to select 38 filamentous fungi. Trichoderma harzianum, Fusarium solani, Trichoderma harzianum F5, and Penicillium sp. F36 were grown in six different culture media. F. solani presented the highest lipase production (2.37 U/mL) with esterification activity of 0.07 U/mL using medium composed of (g.L-1) KH2PO4 1.00, MgSO4 H2O 1.123, and CuSO4 0.06. Supplementation of this culture medium with organic nitrogen sources increased lipase production by 461.3% using tryptone and by 419.4% using yeast extract. Among the vegetable oils from the Amazon region, degummed cotton oil induced lipase production up to 8.14 U/mL. The lipase produced by F. solani F61 has great potential to application in conventional processes and biodiesel production by transesterification of vegetable oils, as well as food industries in the production of fatty acid esters by hydrolysis and esterification.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2019 ","pages":"8182425"},"PeriodicalIF":0.0,"publicationDate":"2019-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2019/8182425","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37397558","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: 13

Enzymatic Conversion of RBCs by α-N-Acetylgalactosaminidase from Spirosoma linguale. 舌螺虫α- n -乙酰半乳糖胺酶转化红细胞的研究。

Enzyme Research Pub Date : 2019-05-02 eCollection Date: 2019-01-01 DOI: 10.1155/2019/6972835

Thomas J Malinski, Harkewal Singh

引用次数: 2

Thermostable Cellulases from the Yeast Trichosporon sp. 酵母Trichosporon sp.的耐热纤维素酶。

Enzyme Research Pub Date : 2019-04-17 eCollection Date: 2019-01-01 DOI: 10.1155/2019/2790414

Hanane Touijer, Najoua Benchemsi, Mohamed Ettayebi, Abdellatif Janati Idrissi, Bouchra Chaouni, Hicham Bekkari

{"title":"Thermostable Cellulases from the Yeast Trichosporon sp.","authors":"Hanane Touijer, Najoua Benchemsi, Mohamed Ettayebi, Abdellatif Janati Idrissi, Bouchra Chaouni, Hicham Bekkari","doi":"10.1155/2019/2790414","DOIUrl":"https://doi.org/10.1155/2019/2790414","url":null,"abstract":"Objectives: Identification of cellulolytic microorganisms is of great interest to the hydrolysis of cellulosic biomass. This study focuses on the identification of cellulolytic yeasts and the optimization of cellulase activities produced by the best performing isolate.Results: 30 cellulolytic yeast isolates were selected. Enzymes produced by an isolate from the Trichosporon genus showed the property to hydrolyze different substrates: carboxymethyl cellulose (CMC), cellulose fiber, and filter paper (FP). The optimum measured temperature was 55°C for CMCase and 60°C for FPase. The optimal pH was 5 for CMCase and 4 to 6 for FPase. The effect of the substrates concentration showed that the best activities were obtained at 100 mg/mL CMC or FP. The highest activities were 0.52 for the CMCase and 0.56 for the cellulase fiber at 10 min incubation, 0.44 IU/mL at 15 min incubation, and 24 h FPase preincubation.Conclusion: Cellulases produced by the studied yeast are capable of hydrolyzing soluble and insoluble substrates at elevated temperatures and at a wide pH range. They are considerable interest in the production of fermentable sugars from lignocellulosic substrates.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2019 ","pages":"2790414"},"PeriodicalIF":0.0,"publicationDate":"2019-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2019/2790414","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37281000","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: 14

Insight into the Mechanistic Basis of the Hysteretic-Like Kinetic Behavior of Thioredoxin-Glutathione Reductase (TGR). 硫氧还蛋白-谷胱甘肽还原酶(TGR)滞回动力学行为的机理基础研究。

Enzyme Research Pub Date : 2018-09-05 eCollection Date: 2018-01-01 DOI: 10.1155/2018/3215462

Juan L Rendón, Mauricio Miranda-Leyva, Alberto Guevara-Flores, José de Jesús Martínez-González, Irene Patricia Del Arenal, Oscar Flores-Herrera, Juan P Pardo

{"title":"Insight into the Mechanistic Basis of the Hysteretic-Like Kinetic Behavior of Thioredoxin-Glutathione Reductase (TGR).","authors":"Juan L Rendón, Mauricio Miranda-Leyva, Alberto Guevara-Flores, José de Jesús Martínez-González, Irene Patricia Del Arenal, Oscar Flores-Herrera, Juan P Pardo","doi":"10.1155/2018/3215462","DOIUrl":"https://doi.org/10.1155/2018/3215462","url":null,"abstract":"A kinetic study of thioredoxin-glutathione reductase (TGR) from Taenia crassiceps metacestode (cysticerci) was carried out. The results obtained from both initial velocity and product inhibition experiments suggest the enzyme follows a two-site ping-pong bi bi kinetic mechanism, in which both substrates and products are bound in rapid equilibrium fashion. The substrate GSSG exerts inhibition at moderate or high concentrations, which is concomitant with the observation of hysteretic-like progress curves. The effect of NADPH on the apparent hysteretic behavior of TGR was also studied. At low concentrations of NADPH in the presence of moderate concentrations of GSSG, atypical time progress curves were observed, consisting of an initial burst-like stage, followed by a lag whose amplitude and duration depended on the concentration of both NADPH and GSSG. Based on all the kinetic and structural evidence available on TGR, a mechanism-based model was developed. The model assumes a noncompetitive mode of inhibition by GSSG in which the disulfide behaves as an affinity label-like reagent through its binding and reduction at an alternative site, leading the enzyme into an inactive state. The critical points of the model are the persistence of residual GSSG reductase activity in the inhibited GSSG-enzyme complexes and the regeneration of the active form of the enzyme by GSH. Hence, the hysteretic-like progress curves of GSSG reduction by TGR are the result of a continuous competition between GSH and GSSG for driving the enzyme into active or inactive states, respectively. By using an arbitrary but consistent set of rate constants, the experimental full progress curves were successfully reproduced in silico.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2018 ","pages":"3215462"},"PeriodicalIF":0.0,"publicationDate":"2018-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2018/3215462","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36525311","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: 2

A Midgut Digestive Phospholipase A₂ in Larval Mosquitoes, Aedes albopictus and Culex quinquefasciatus. 蚊幼虫、白纹伊蚊和致倦库蚊中肠消化磷脂酶A2的研究。

Enzyme Research Pub Date : 2018-05-15 eCollection Date: 2018-01-01 DOI: 10.1155/2018/9703413

Nor Aliza Abdul Rahim, Marlini Othman, Muna Sabri, David W Stanley

{"title":"A Midgut Digestive Phospholipase A2 in Larval Mosquitoes, Aedes albopictus and Culex quinquefasciatus.","authors":"Nor Aliza Abdul Rahim, Marlini Othman, Muna Sabri, David W Stanley","doi":"10.1155/2018/9703413","DOIUrl":"https://doi.org/10.1155/2018/9703413","url":null,"abstract":"Phospholipase A2 (PLA2) is a secretory digestive enzyme that hydrolyzes ester bond at sn-2 position of dietary phospholipids, creating free fatty acid and lysophospholipid. The free fatty acids (arachidonic acid) are absorbed into midgut cells. Aedes albopictus and Culex quinquefasciatus digestive PLA2 was characterized using a microplate PLA2 assay. The enzyme showed substantial activities at 6 and 8 μg/μl of protein concentration with optimal activity at 20 and 25 μg/μl of substrate concentration in Aedes albopictus and Culex quinquefasciatus, respectively. PLA2 activity from both mosquitoes increased in a linear function up to 1 hour of the reaction time. Both enzymes were sensitive to pH and temperature. PLA2 showed higher enzyme activities in pH 8.0 and pH 9.0 from Aedes albopictus and Culex quinquefasciatus, respectively, at 40°C of incubation. The PLA2 activity decreased in the presence of 5 mM (Aedes albopictus) and 0.5 mM (Culex quinquefasciatus) site specific PLA2 inhibitor, oleyloxyethylphosphorylcholine. Based on the migration pattern of the partially purified PLA2 on SDS-PAGE, the protein mass of PLA2 is approximately 20-25 kDa for both mosquitoes. The information on PLA2 properties derived from this study may facilitate in devising mosquitoes control strategies especially in the development of inhibitors targeting the enzyme active site.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2018 ","pages":"9703413"},"PeriodicalIF":0.0,"publicationDate":"2018-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2018/9703413","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36189424","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: 6

Optimization of Xylanase Production from Aspergillus foetidus in Soybean Residue. 大豆渣中胎儿曲霉产木聚糖酶的优化研究。

Enzyme Research Pub Date : 2018-04-11 eCollection Date: 2018-01-01 DOI: 10.1155/2018/6597017

Luana Cunha, Raquel Martarello, Paula Monteiro de Souza, Marcela Medeiros de Freitas, Kleber Vanio Gomes Barros, Edivaldo Ximenes Ferreira Filho, Mauricio Homem-de-Mello, Pérola Oliveira Magalhães

引用次数: 37

Extracellular Pectinase from a Novel Bacterium Chryseobacterium indologenes Strain SD and Its Application in Fruit Juice Clarification. 一株产紫黄杆菌的胞外果胶酶及其在果汁澄清中的应用。

Enzyme Research Pub Date : 2018-03-21 eCollection Date: 2018-01-01 DOI: 10.1155/2018/3859752

Karabi Roy, Sujan Dey, Md Kamal Uddin, Rasel Barua, Md Towhid Hossain

{"title":"Extracellular Pectinase from a Novel Bacterium Chryseobacterium indologenes Strain SD and Its Application in Fruit Juice Clarification.","authors":"Karabi Roy, Sujan Dey, Md Kamal Uddin, Rasel Barua, Md Towhid Hossain","doi":"10.1155/2018/3859752","DOIUrl":"https://doi.org/10.1155/2018/3859752","url":null,"abstract":"Pectinase is one of the important enzymes of industrial sectors. Presently, most of the pectinases are of plant origin but there are only a few reports on bacterial pectinases. The aim of the present study was to isolate a novel and potential pectinase producing bacterium as well as optimization of its various parameters for maximum enzyme production. A total of forty bacterial isolates were isolated from vegetable dump waste soil using standard plate count methods. Primary screening was done by hydrolysis of pectin. Pectinase activity was determined by measuring the increase in reducing sugar formed by the enzymatic hydrolysis of pectin. Among the bacterial isolates, the isolate K6 exhibited higher pectinase activity in broth medium and was selected for further studies. The selected bacterial isolate K6 was identified as Chryseobacterium indologenes strain SD. The isolate was found to produce maximum pectinase at 37°C with pH 7.5 upon incubation for 72 hours, while cultured in production medium containing citrus pectin and yeast extract as C and N sources, respectively. During enzyme-substrate reaction phase, the enzyme exhibited its best activity at pH of 8.0 and temperature of 40°C using citrus pectin as substrate. The pectinase of the isolate showed potentiality on different types of fruit juice clarification.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2018 ","pages":"3859752"},"PeriodicalIF":0.0,"publicationDate":"2018-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2018/3859752","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36094474","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: 34

Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications. 植物植酸酶、蛋白酪氨酸磷酸酶样植酸酶和组氨酸植酸酶催化结构的表征及其生物技术应用。

Enzyme Research Pub Date : 2018-03-11 eCollection Date: 2018-01-01 DOI: 10.1155/2018/8240698

Alex Sander Rodrigues Cangussu, Deborah Aires Almeida, Raimundo Wagner de Souza Aguiar, Sidnei Emilio Bordignon-Junior, Kelvinson Fernandes Viana, Luiz Carlos Bertucci Barbosa, Edson Wagner da Silva Cangussu, Igor Viana Brandi, Augustus Caeser Franke Portella, Gil Rodrigues Dos Santos, Eliane Macedo Sobrinho, William James Nogueira Lima

{"title":"Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications.","authors":"Alex Sander Rodrigues Cangussu, Deborah Aires Almeida, Raimundo Wagner de Souza Aguiar, Sidnei Emilio Bordignon-Junior, Kelvinson Fernandes Viana, Luiz Carlos Bertucci Barbosa, Edson Wagner da Silva Cangussu, Igor Viana Brandi, Augustus Caeser Franke Portella, Gil Rodrigues Dos Santos, Eliane Macedo Sobrinho, William James Nogueira Lima","doi":"10.1155/2018/8240698","DOIUrl":"10.1155/2018/8240698","url":null,"abstract":"Phytase plays a prominent role in monogastric animal nutrition due to its ability to improve phytic acid digestion in the gastrointestinal tract, releasing phosphorus and other micronutrients that are important for animal development. Moreover, phytase decreases the amounts of phytic acid and phosphate excreted in feces. Bioinformatics approaches can contribute to the understanding of the catalytic structure of phytase. Analysis of the catalytic structure can reveal enzymatic stability and the polarization and hydrophobicity of amino acids. One important aspect of this type of analysis is the estimation of the number of β-sheets and α-helices in the enzymatic structure. Fermentative processes or genetic engineering methods are employed for phytase production in transgenic plants or microorganisms. To this end, phytase genes are inserted in transgenic crops to improve the bioavailability of phosphorus. This promising technology aims to improve agricultural efficiency and productivity. Thus, the aim of this review is to present the characterization of the catalytic structure of plant and microbial phytases, phytase genes used in transgenic plants and microorganisms, and their biotechnological applications in animal nutrition, which do not impact negatively on environmental degradation.","PeriodicalId":11835,"journal":{"name":"Enzyme Research","volume":"2018 ","pages":"8240698"},"PeriodicalIF":0.0,"publicationDate":"2018-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5866894/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36057652","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