Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Seabra, Inês J.; Gil, M.H.

doi:10.1590/s1516-93322007000400006

Cited by 22 publications

(13 citation statements)

References 25 publications

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“…As shown, the trypsin has a high activity to cleave the urease enzyme in the pH 9.4. The result has a good agreement with the previous report 55 . The reasonable reason to explain this phenomenon is the structure of the enzyme is changed www.nature.com/scientificreports www.nature.com/scientificreports/ and the active site is distorted in the higher than 9.5 and pH solution and the activity of trypsin decreased.…”

Section: Optimization Of Effective Parameters On the Response Of The supporting

confidence: 93%

Remote biosensor for the determination of trypsin by using nanoporous anodic alumina as a three-dimensional nanostructured material

Tabrizi

Ferré‐Borrull

Marsal

2020

Sci Rep

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tabrizi, Josep ferré-Borrull & Lluis f. Marsal * the determination of trypsin in the human real sample is a routine medical investigation to assess the pancreatic disease. Herein, we fabricated an interferometric reflectance spectroscopy based biosensor for the determination trypsin. For this purpose, urease and fluorescein 5(6)-isothiocyanate (FLITC) were immobilized on the nanoporous anodic alumina (NAA). The operation principle of the proposed biosensor is based on the change in the pH of the solution during the reaction of urease and urea and therefore change in the light-absorbing ability of fLitc in the presence of trypsin. the reaction of the urease enzyme with urea increased the pH of the solution because of producing ammonia. this increase in the pH of solution increased the light-absorbing ability of the immobilized fLitc on nAA and therefore the intensity of the reflected light from the NAA to the charge-coupled device detector decreased. in the presence of trypsin, the catalytic activity of immobilized urease on nAA decreased. this decrease in the activity of urease enzyme consequent on the decrease in the amount of the generated ammonia. therefore, the immobilized fLitc on the nAA did not absorb more light and consciously, the intensity of the light reflected light into the detector increased. The proposed biosensor exhibited a good response to the concentration of trypsin in the range of 0.25-20 μg.mL −1 with the limit of detection of 0.06 μg.mL −1. Millions of people in the world suffer from some form of pancreatic diseases 1. According to world health statistics reports, pancreatic diseases id associated with a tremendous economic burden 2,3. Due to reduce the economic losses caused by this disease and also to improve the public health, the fabrication of a device to diagnose this disease is important for every government. The routine laboratory test for pancreatic disease diagnosis is the determination of trypsin the human real sample. Trypsin is a serine protease with a potential role in pancreatic cancer that can cleavage the peptides on the carbonyl side of arginine and lysine amino acids 4. In the acute pancreatitis patient that is a fatal disease, the concentration of trypsin reaches up to 84.4 µg.mL −1 in the urine sample that is so higher than its normal rage (115-350 ng.mL −1) 5. Therefore, it is necessary to develop a simple, selective, sensitive, and low-cost sensor for trypsin detection. However, most of them are complicated, low sensitivity, time-consuming, and expensive method 6-10. To overcome these problems, biosensors become more interested to detect trypsin 11,12. The biosensor is an analytical device which includes a transducer and a biomolecule (such as the enzymes, antibodies, and aptamers) 13-15. Among the various biosensors that have been reported for the sensing of bio-targets, the optical biosensors are more interested because of their high sensitivity, small and lightweight, remote sensing ability, immunity to electromagnetic interference, capability for monitoring a wide...

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Section: Optimization Of Effective Parameters On the Response Of The supporting

confidence: 93%

Remote biosensor for the determination of trypsin by using nanoporous anodic alumina as a three-dimensional nanostructured material

Tabrizi

Ferré‐Borrull

Marsal

2020

Sci Rep

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“…Further increasing the temperature above 20°C led to a decline in enzyme activity. This was thought to be because high protein load at higher temperature might lead to enzyme denaturation by protein–protein interactions and/or distortion of protein molecules enzyme . Also, the active sites of the enzyme molecules might be hidden by excessive enzyme molecules accumulated on the support surface, which would be disadvantageous for enzyme catalysis capability .…”

Section: Resultsmentioning

confidence: 79%

Preparation of immobilized pectinase on regenerated cellulose beads for removing anionic trash in whitewater from papermaking

Zhang

et al. 2013

J. Chem. Technol. Biotechnol.

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BACKGROUND: Anionic pectic compounds in whitewater (the aqueous solution that drains from a wet sheet of paper as it is being formed) negatively impact the papermaking process as well as the product quality. In order to remove these substances, regenerated cellulose beads were prepared and used as a new carrier for commercially available pectinase via physical adsorption to treat whitewater. RESULTS: The optimum immobilization temperature, time and pH of the immobilized pectinase on regenerated cellulose beadswere 20 • C, 2 h and 7.0, respectively, under which the enzyme showed high protein loading and enzymatic activity of 2.9 mg g -1 and 178 U g -1 of the immobilized biocatalyst, respectively. Compared with the free pectinase, the immobilized enzyme on regenerated cellulose beads showed higher thermo and pH stabilities. Furthermore, the immobilized pectinase showed good mechanical strength and high catalytic capability in lowering the cationic demand of whitewater. CONCLUSION:The preparation of immobilized enzyme on regenerated cellulose beads was simple, facile, cost effective and environmentally friendly. It was also demonstrated that the resultant pectinase thus obtained could potentially be utilized for treatment of whitewater in the papermaking industry due to its effectiveness in reducing cationic demand.

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“…In addition, multipoint covalent immobilization may also cause physical obstacle for the adsorption of oil on lipase (Seabra and Gil, 2007), thus increasing the diffusion resistance of oil to celite-lipase. As a result, a larger K m value was observed for the celite-lipase.…”

Section: Enzyme Kinetics Of Celite-lipasementioning

confidence: 99%

Characterization of Burkholderia lipase immobilized on celite carriers

Liu

Lin

Chen

et al. 2009

Journal of the Taiwan Institute of Chemical Engineers

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Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Cited by 22 publications

References 25 publications

Remote biosensor for the determination of trypsin by using nanoporous anodic alumina as a three-dimensional nanostructured material

Remote biosensor for the determination of trypsin by using nanoporous anodic alumina as a three-dimensional nanostructured material

Preparation of immobilized pectinase on regenerated cellulose beads for removing anionic trash in whitewater from papermaking

Characterization of Burkholderia lipase immobilized on celite carriers

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