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Artificial cells, blood substitutes, and immobilization biotechnology最新文献

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Development and characterization of rifampicin loaded floating microspheres. 载利福平漂浮微球的研制与表征。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-06-02 DOI: 10.3109/10731199.2011.573482
Pankaj Goyal, S Gill, U D Gupta, Goutam Rath, Raj K Narang, Amit K Goyal
{"title":"Development and characterization of rifampicin loaded floating microspheres.","authors":"Pankaj Goyal,&nbsp;S Gill,&nbsp;U D Gupta,&nbsp;Goutam Rath,&nbsp;Raj K Narang,&nbsp;Amit K Goyal","doi":"10.3109/10731199.2011.573482","DOIUrl":"https://doi.org/10.3109/10731199.2011.573482","url":null,"abstract":"<p><p>Gastroretentive floating microspheres have a potential for enhancing the bioavailability and controlled delivery of drugs. The present study involves development of rifampicin floating microspheres in order to increase the gastric retention time. The microspheres were prepared by solvent evaporation technique and characterized for particle size, shape, zeta-potential, entrapment, and release kinetics. The developed systems were almost spherical in shape. The entrapment efficiency was found to be 86.34%. The percentage buoyancy after 8 hours was found to be 61.06. The prepared microspheres exhibited prolonged drug release in gastric medium and hence could be utilized for sustained delivery of anti-tubercular drugs.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.573482","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29906058","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
A biosensor for the determination of β-galactosidase activity: a different viewpoint on biosensors. 用于测定β-半乳糖苷酶活性的生物传感器:生物传感器的不同观点。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-02-25 DOI: 10.3109/10731199.2011.560119
Mustafa Kemal Sezgintürk, Erhan Dinçkaya
{"title":"A biosensor for the determination of β-galactosidase activity: a different viewpoint on biosensors.","authors":"Mustafa Kemal Sezgintürk,&nbsp;Erhan Dinçkaya","doi":"10.3109/10731199.2011.560119","DOIUrl":"https://doi.org/10.3109/10731199.2011.560119","url":null,"abstract":"<p><p>β-galactosidase splits lactose into glucose and galactose. Because of its biotechnological interest, we presented a biosensor system in order to monitor β-galactosidase activity. Immobilization steps of the biosensor were identified by cyclic voltammograms and electrochemical impedance spectroscopy. β-galactosidase was voltammetrically detected at about +150 mV (vs. Ag/AgCl) in citrate buffer solution (0.05 M, pH 4.8). The linear response for β-galactosidase detection was in the range of 0.0118 U mL(-1)to 0.47 U mL(-1)and a shorter response time of ∼50 s. Our results demonstrated the biosensor's electrochemical properties and analytical characteristics were very useful and effective for monitoring of β-galactosidase activity.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.560119","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29697288","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: 0
A novel biosensor based on glucose oxidase for activity determination of α - amylase. 一种基于葡萄糖氧化酶的新型α -淀粉酶活性传感器。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-05-17 DOI: 10.3109/10731199.2011.574635
Cagrı Altug, Umut Mengulluoglu, Elif Kurt, Secil Kaya, Erhan Dinckaya
{"title":"A novel biosensor based on glucose oxidase for activity determination of α - amylase.","authors":"Cagrı Altug,&nbsp;Umut Mengulluoglu,&nbsp;Elif Kurt,&nbsp;Secil Kaya,&nbsp;Erhan Dinckaya","doi":"10.3109/10731199.2011.574635","DOIUrl":"https://doi.org/10.3109/10731199.2011.574635","url":null,"abstract":"<p><p>A glucose oxidase-based biosensor was developed for the determination of α-amylase activity. The determination method is based on monitoring the decrease in dissolved oxygen concentration related to the starch concentration, for which starch gives a reaction with α-amylase. Optimization parameters, including glucose oxidase amount, gelatin amount, and glutaraldehyde percentage for cross-linking, were investigated. The effects of pH, buffer system, and temperature on the biosensor system were also investigated. The biosensor had a linear relation to α-amylase activity and good measurement correlation between 0.66 and 9.83 U/ml. In sample analysis studies, α-amylase activity in baker's yeast was determined by the biosensor.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.574635","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30188079","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: 4
Collagen fibers constructed by gravity filament forming process. 采用重力成丝工艺构建胶原纤维。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-05-11 DOI: 10.3109/10731199.2011.574634
Fu I Tung, Chih T Chiu, Yi P Chang, Yng J Wang
{"title":"Collagen fibers constructed by gravity filament forming process.","authors":"Fu I Tung,&nbsp;Chih T Chiu,&nbsp;Yi P Chang,&nbsp;Yng J Wang","doi":"10.3109/10731199.2011.574634","DOIUrl":"https://doi.org/10.3109/10731199.2011.574634","url":null,"abstract":"<p><p>Fibers comprised of reconstituted type I collagen were prepared by a gravity filament forming process and crosslinked with 0.1% glutaraldehyde. These fibers have a crosslinking index of about 90% (89.89 ± 1.82%) with higher denature temperature (74.43 ± 0.08°C) as compared to that without glutaraldehyde treatment (52.1 ± 0.17°C). The ultimate tensile strength of the collagen fibers increases from 99.4 ± 12.9 to 174.4 ± 9.0 MPa after glutaraldehyde-crosslinking. L929 fibroblast cells were seeded and cultured using these newly developed collagen fibers. The fibroblast cells proliferated well and covered all surface areas of the collagen fiber. These collagen fibers have a great potential for application in 3-D tissue engineering.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.574634","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29871414","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: 0
Rapid immobilization of enzymes onto solid supports by ultrasound waves. 用超声波将酶快速固定在固体载体上。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-03-14 DOI: 10.3109/10731199.2011.563361
Pragya Sharma, Dileep Kumar Kannoujia, Seemi Farhat Basir, Pradip Nahar
{"title":"Rapid immobilization of enzymes onto solid supports by ultrasound waves.","authors":"Pragya Sharma,&nbsp;Dileep Kumar Kannoujia,&nbsp;Seemi Farhat Basir,&nbsp;Pradip Nahar","doi":"10.3109/10731199.2011.563361","DOIUrl":"https://doi.org/10.3109/10731199.2011.563361","url":null,"abstract":"<p><p>Herein, we describe a non-conventional method for immobilization of enzymes onto different solid surfaces using ultrasound as a source of energy. When horseradish peroxidase (HRP) was taken on the surface of an activated support and allowed to float on a sonicator bath operating at a frequency of 40 KHz, it readily started binding itself to the surface. Maximum binding was observed in 10 min whereas a control experiment carried out similarly without ultrasound waves showed insignificant immobilization. Ultrasound wave-mediated immobilization is rapid and reproducible and is better suitable for versatile applications in different fields, including fabrication of enzyme-based biosensors or bioreactors.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.563361","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29738006","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: 7
Photochemical immobilization of cucurbita fruit ascorbate oxidase onto polyethylene disc for determination of ascorbate in serum and foodstuffs. 聚乙烯圆盘上葫芦果抗坏血酸氧化酶测定血清和食品中抗坏血酸的光化学固定化。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-04-20 DOI: 10.3109/10731199.2011.573481
Shikha Pundir, Amita Gera, C S Pundir
{"title":"Photochemical immobilization of cucurbita fruit ascorbate oxidase onto polyethylene disc for determination of ascorbate in serum and foodstuffs.","authors":"Shikha Pundir,&nbsp;Amita Gera,&nbsp;C S Pundir","doi":"10.3109/10731199.2011.573481","DOIUrl":"https://doi.org/10.3109/10731199.2011.573481","url":null,"abstract":"<p><p>Abstract: An ascorbate oxidase purified from the green fruit of zucchini squash (Cucurbita pepo medullosa) was immobilized photochemically on a polyethylene disc with 85% retention of initial activity of free enzyme. The optimum pH (5.5) was unchanged, while K(m) was decreased. The polyethylene discs were employed for determination of ascorbic acid in serum and foodstuffs. The working linear range was 2.8 μM to 16 μM. The mean value of ascorbic acid in serum as measured by the method was 0.16 mg/dl in males and 0.209 mg/dl in females. The immobilized enzyme was used 100 times over 4 months, when stored at 4°C.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.573481","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29828226","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: 3
Alkaline phosphatase based amperometric biosensor immobilized by cysteamine-glutaraldehyde modified self-assembled monolayer. 半胱氨酸-戊二醛修饰自组装单层固定化碱性磷酸酶安培型生物传感器。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-06-10 DOI: 10.3109/10731199.2011.563363
Emine Yorganci, Erol Akyilmaz
{"title":"Alkaline phosphatase based amperometric biosensor immobilized by cysteamine-glutaraldehyde modified self-assembled monolayer.","authors":"Emine Yorganci,&nbsp;Erol Akyilmaz","doi":"10.3109/10731199.2011.563363","DOIUrl":"https://doi.org/10.3109/10731199.2011.563363","url":null,"abstract":"<p><p>Alkaline phosphatase (ALP) was immobilized with cross-linking agents glutaraldehyde and cysteamine by forming a self-assembled monolayer on a screen printed gold electrode. ALP converts p-nitrophenyl phosphate to p-nitrophenol and phosphate. p-Nitrophenol loses H(+) ion and turns into the negatively charged compound p-nitrophenolate at medium pH. As a result, the unstable product formed is measured chronoamperometrically at an application potential of + 0.95 V. The biosensor response depends linearly on p-nitrophenyl phosphate concentration between 0.05 - 0.6 mM with a response time of 40 seconds. Detection limit of the biosensor is 0.033 mM.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.563363","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29927259","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: 7
β-galactosidase determination by an electrochemical biosensor mediated with ferrocene. 二茂铁介导电化学生物传感器测定β-半乳糖苷酶。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-02-22 DOI: 10.3109/10731199.2011.559644
Mustafa Kemal Sezgintürk, Erhan Dinçkaya
{"title":"β-galactosidase determination by an electrochemical biosensor mediated with ferrocene.","authors":"Mustafa Kemal Sezgintürk,&nbsp;Erhan Dinçkaya","doi":"10.3109/10731199.2011.559644","DOIUrl":"https://doi.org/10.3109/10731199.2011.559644","url":null,"abstract":"<p><p>Abstract: In this paper, a new viewpoint on the activity determination of β-galactosidase is reported. Glucose oxidase was directly immobilized on a glassy carbon electrode and mediated by ferrocene. The biosensor's performance was based on mediated electron transfer by ferrocene, which reduced via glucose oxidase reaction. In this reaction, substrate of glucose oxidase, glucose was provided by the activity of β-galactosidase in the sample. The parameters of the fabrication process for the electrode were optimized. Experimental conditions influencing the biosensor performance, such as pH, ferrocene and lactose concentrations, and temperature, were investigated and assessed. Finally, the biosensor was successfully applied to determination of β-galactosidase activity of artificial intestinal juice.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.559644","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29687000","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: 0
High throughput miniaturization of artificial cells. 人工细胞的高通量小型化。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-05-24 DOI: 10.3109/10731199.2011.574637
Maryam Mobed-Miremadi, Erik Acks, Sutthipong Polsaward, Ding Chen
{"title":"High throughput miniaturization of artificial cells.","authors":"Maryam Mobed-Miremadi,&nbsp;Erik Acks,&nbsp;Sutthipong Polsaward,&nbsp;Ding Chen","doi":"10.3109/10731199.2011.574637","DOIUrl":"https://doi.org/10.3109/10731199.2011.574637","url":null,"abstract":"<p><p>In this study, inkjet bio-printing has been used to produce miniaturized alginate microcapsules. A parametric study using subsequent Taguchi L(18) (3(1) × 2(7)) and L(16) (4(5)) designs was performed to elucidate the effect of inkjet parameters on microcapsule size. A 120-minute pilot run using the optimal waveform parameters and 0.5% alginate ink yielded a throughput of 1.8×10(6) microcapsules/hr, averaging 40 μm in diameter. Real-time stable jetting conditions were confirmed visually by the generation of a single droplet with a straight trajectory and non-fluctuating Ohnesorge numbers. The rate of stirring of the cross-linking CaCl(2) solution determined scaffold vs. single vesicle formation.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.574637","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40102753","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: 11
Hemoglobin-albumin crosslinked copolymers: reduced prooxidant reactivity. 血红蛋白-白蛋白交联共聚物:降低促氧化反应性。
Artificial cells, blood substitutes, and immobilization biotechnology Pub Date : 2011-10-01 Epub Date: 2011-05-31 DOI: 10.3109/10731199.2011.563362
Bianca Iacob, Florina Deac, Daniela Cioloboc, Grigore Damian, Radu Silaghi-Dumitrescu
{"title":"Hemoglobin-albumin crosslinked copolymers: reduced prooxidant reactivity.","authors":"Bianca Iacob,&nbsp;Florina Deac,&nbsp;Daniela Cioloboc,&nbsp;Grigore Damian,&nbsp;Radu Silaghi-Dumitrescu","doi":"10.3109/10731199.2011.563362","DOIUrl":"https://doi.org/10.3109/10731199.2011.563362","url":null,"abstract":"<p><p>We have previously reported that derivatization of hemoglobin with periodate-modified sugar derivatives such as oxidized adenosine triphosphate (oATP) leads to an increase in prooxidant reactivity at the heme. Here, we report that copolymerization of hemoglobin with serum albumin alleviates this problem completely, to the extent where the copolymer even has a slightly lower autooxidation rate compared to native hemoglobin. A similar, although not as potent, effect is obtained when hemoglobin is derivatized with oATP in the presence of small-molecule antioxidants instead of albumin.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2011.563362","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29900067","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: 10
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