Immobolization of alkaline phosphatase on silk using diazo, adsorption, glutaraldehyde, and azide method: Optimum pH and properties of the conjugates

Grasset, Laurent; Cordier, D; Couturier, Roger; Ville, A.E. La

doi:10.1002/bit.260250520

Cited by 31 publications

(12 citation statements)

References 8 publications

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“…The effect of the pH on immobilized alkaline phosphatase activity was investigated using free enzyme and comparing its activity with the immobilized enzyme. The result have indicated that the optimal pH value for immobilized and free enzyme are quite similar (≈9.5) which is in agreement with the previous reports (19,20). Interestingly, the immobilized enzyme showed higher activity in pH 10 compared to the native enzyme which might be attributed to the effect of the pH on electrostatic interactions of the collagen (21).…”

Section: Discussionsupporting

confidence: 90%

Immobilization of the Alkaline Phosphatase on Collagen Surface via Cross-Linking Method

Hanachi¹,

Jafary²,

Motamedi³

2015

Iran J Biotech

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Section: Discussionsupporting

confidence: 90%

Immobilization of the Alkaline Phosphatase on Collagen Surface via Cross-Linking Method

Hanachi¹,

Jafary²,

Motamedi³

2015

Iran J Biotech

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“…Ribonuclease immobilized onto woven silk substrates using diazo‐coupling retained 63% of its activity after 7.2 months of storage in 0.1 M NaCl at 0–4°C 45. Preparations of alkaline phosphatase immobilized on woven silk by covalent (diazo, azide, or glutaraldehyde) or adsorption methods retained bioactivity 46. Stability of β‐glucosidase entrapped in ethyl alcohol‐treated silk films was protected against heating, electrodialysis, and protease treatment 47.…”

Section: Protein and Peptide Stabilization By Silkmentioning

confidence: 99%

Alkylated hyperbranched polymers as molecular nanosponges for the purification of water from polycyclic aromatic hydrocarbons

Arkas¹,

Eleades²,

Paleos³

et al. 2005

J of Applied Polymer Sci

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A series of hyperbranched polymers functionalized with long aliphatic chains has been prepared and characterized. The property of films prepared from these polymers to encapsulate lipophilic polyaromatic pollutants dissolved in water has been established. The level of pyrene and fluoranthene remaining in water after treatment ranged from 1 to 30 ppb for most of the hyperbranched polymers, while for the relatively more water-soluble phenanthrene a final concentration of about 50 to 70 ppb could be attained. The inclusion formation constants determined for the polycyclic aromatics were 2.0 ϫ 10 8 -6.3 ϫ 10 6 M Ϫ1 for pyrene, 1.2 ϫ 10 7 -1.6 ϫ 10 6 M Ϫ1 for fluoranthene, and 3.8 ϫ 10 6 -4 ϫ 10 5 M Ϫ1 for phenanthrene. The loading capacities depend on the nature of the polycyclic aromatic compounds and the chemical structure of the parent hyperbranched polymers, ranging from 6 to 31 mg/g of polymer for fluoranthene, 15-54 mg/g for phenanthrene, and 6 -35 mg/g for pyrene.Regeneration of the absorbing films was achieved by their treatment with acetonitrile.

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“…The aspartate aminotransferase enzyme, calf intestine alkaline phosphatase enzyme and ribonuclease enzymes have been covalently linked to Bombyx mori fibroin effectively and were shown their activity efficiently. Many enzymes effectively immobilized through physical entrapment method within the silk films [37][38][39][40].…”

Section: Biomedical Applications Of Silk Proteinsmentioning

confidence: 99%

Bioactive Secondary Metabolites of Wild Antheraea mylitta Silkworm Cocoons

Ahamad¹,

Neetha²,

Vootla³

2021

Moths and Caterpillars

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The wild silkworm Antheraea mylitta is grown and cultivated in several parts of India ranging from Bihar to West Bengal and several parts of Telangana. The wild silkworm rearing has been a source of income for the tribal populations who rely on it as income source; the intervention of government agencies has increased the cultivation. Our research involves understanding the secondary metabolites in the silkworm Cocoons and elucidating how the pupa survives the harsh environment during pupal diapause of the insect. We have realized the role of insect repellent compounds and other metabolites and their interaction with the insect. Wild silkworm Cocoons are the specialized natural structures constructed by Antheraea mylitta silkworms. They are the protein composites of sericin and fibroin as a structural material. The silkworm cocoons are presumed to be evolved structures through the course of evolution over millions of years. This chapter focuses on Biophysical analysis of chemical compounds, proteins and other secondary metabolites traced in the Wild Antheraea mylitta Tasar cocoons which are predicted to be the key factors to achieve the unique structural and chemical barriers to protect the pupa within the cocoons.

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Immobolization of alkaline phosphatase on silk using diazo, adsorption, glutaraldehyde, and azide method: Optimum pH and properties of the conjugates

Cited by 31 publications

References 8 publications

Immobilization of the Alkaline Phosphatase on Collagen Surface via Cross-Linking Method

Immobilization of the Alkaline Phosphatase on Collagen Surface via Cross-Linking Method

Alkylated hyperbranched polymers as molecular nanosponges for the purification of water from polycyclic aromatic hydrocarbons

Bioactive Secondary Metabolites of Wild Antheraea mylitta Silkworm Cocoons

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