Immobilization of alkaline protease on nylon

Chellapandian, M.; Sastry, C. S. P.

doi:10.1007/bf00369610

Cited by 21 publications

(20 citation statements)

References 11 publications

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“…Above these concentrations for immobilized urease, a reduction in the relative activity was observed. Similar observations were made by Chellapandian and Sastry [1] with alkaline protease immobilized on nylon. The decrease in relative activity for higher concentrations of the enzyme may be due to enzyme-enzyme interactions and stearic hindrance.…”

Section: Resultssupporting

confidence: 81%

“…Commerical grade nylon 6/6 tubes of one gram were treated as reported by Chellapandian and Sastry [1] with 20 ml of 3.5 M hydrochloric acid at 50°C for 30 minutes. Then the partially hydrolyzed nylon was washed with distilled water.…”

Section: Preparation and Activation Of Nylonmentioning

confidence: 99%

“…Nylon 6/6 tubes are used as support material for the immobilization of Jackbean type 4 urease because they are non-porous, have mechanical strength, have good¯ow through properties, have resistance to microbial attack and high relative hydrophilicity [1]. Enzymes such as alkaline protease [1], glucoamylase, glucose oxidase, b-Dgalactosidase [2] glucose oxidase [3] are immobilized on nylon.…”

Section: Introductionmentioning

confidence: 99%

“…Enzymes such as alkaline protease [1], glucoamylase, glucose oxidase, b-Dgalactosidase [2] glucose oxidase [3] are immobilized on nylon. For the determination of urea [4], ureases immobilized on low molecular weight nylon powder, inside surface of nylon tubes and within the matrix of a nylon membrane have been separately employed.…”

Section: Introductionmentioning

confidence: 99%

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Urease immobilized on nylon: preparation and properties

Anita

Sastry

Hashim

1997

Bioprocess Engineering

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Urease (EC 3.5.1.5) was covalently attached through glutaraldehyde to partially hydrolysed nylon 6/6 tubes. The highest activity of immobilized enzyme was obtained at 65°C and pH 6.5, while the optimum temperature for free urease was found to be 25°C. Immobilized urease showed an improved thermal stability in comparison to free urease. It retained 76% of the original activity after 60 days when stored at 4°C and 78% of the activity after 5 repeated uses.

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Section: Resultssupporting

confidence: 81%

Section: Preparation and Activation Of Nylonmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Urease immobilized on nylon: preparation and properties

Anita

Sastry

Hashim

1997

Bioprocess Engineering

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“…Thermogravimetric analysis of sample was done in the range of 40-400 C in nitrogen atmosphere (flow rate ¼ 60 cm 3 /min) at a heating rate of 10 C/min. A sample mass of 10 AE 2 mg was used.…”

Section: Thermo Gravimetric Analysismentioning

confidence: 99%

Surface modification of cellulose filter paper by glycidyl methacrylate grafting for biomolecule immobilization: Influence of grafting parameters and urease immobilization

Tyagi

Tomar

Singh

2008

J of Applied Polymer Sci

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Graft copolymerization of glycidyl methacrylate (GMA) onto cellulose filter paper (CFP) was carried out by a free-radical initiating process using ceric ammonium nitrate (CAN) as an initiator. Optimum conditions pertaining to different grafting percentages were evaluated as a function of monomer and initiator concentrations, polymerization time and temperature. CFP with various graft levels of GMA was characterized by fourier transform infrared (FTIR) spectroscopy and thermo gravimetric analysis (TGA). Surface morphology of ungrafted and grafted CFP was evaluated by scanning electron microscopy (SEM). Attenuated total reflectance (ATR)-FTIR spectral analysis provided the evidence of grafting of GMA onto CFP. The maximum grafting of 102% was achieved by using 4 Â 10 À3 molL À1 CAN and 5% of GMA (w/v) monomer at 60 C in 25 min. The CFP-g-GMA surfaces with different graft levels were evaluated as a support for immobilization of biomolecules. Urease was selected as the model enzyme to be covalently coupled through the surface epoxy groups of the CFP-g-GMA discs. Immobilized discs were further studied for urea estimation and their reusability. Although the highest degree of urease immobilization was observed at 100% (162-lg urease/disc) graft level, the urease immobilized on discs with 70% (105-lg urease/disc) graft level gave the maximum activity of the enzyme.

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In situ entrapment of urease in cryogels of poly(N‐isopropylacrylamide): An effective strategy for noncovalent immobilization of enzymes

Petrov

Pavlova

Tsvetanov

et al. 2011

J of Applied Polymer Sci

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Supermacroporous poly(N-isopropylacrylamide) (PNIPAAm) cryogels containing urease were prepared via UV irradiation technique and hydrogen peroxide as initiator. Specifically, due to the cryostructuration phenomenon urease molecules were embedded into the dense cryogel walls. Thus, although the enzyme is physically entrapped, the system exhibited remarkable resistance against leaking due to the dense polymer network formed in the cryogel walls. The immobilized urease can catalyze the hydrolysis of urea in a broad temperature range in both batch and flow regime. The interconnected macropores assist for unhindered diffusion of the substrate and reaction products through the gel, thus, paving the way for consecutive reuse at a constant activity, in contrast to the conventional PNIPAAm hydrogel. Due to the spongy-like morphology PNIPAAm cryogels containing urease can be exploited as highly permeable membrane for direct removal of traces of urea from continuously flowing feed solutions.

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Immobilization of alkaline protease on nylon

Cited by 21 publications

References 11 publications

Urease immobilized on nylon: preparation and properties

Urease immobilized on nylon: preparation and properties

Surface modification of cellulose filter paper by glycidyl methacrylate grafting for biomolecule immobilization: Influence of grafting parameters and urease immobilization

In situ entrapment of urease in cryogels of poly(N‐isopropylacrylamide): An effective strategy for noncovalent immobilization of enzymes

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