Attachment of biomolecules on gold, silicon or glass surfaces has direct implications for the development of novel biosensors in the context of nanoscale detection of pathogens and other metabolites related to issues of human health. In this critical review, we have highlighted the current developments in various techniques of immobilization of biomolecules, specifically biological macromolecules on surfaces through the modification of a functional self-assembled monolayer. The utility of such immobilized biomolecules in the area of biosensing in nanoscale has been surveyed. Merits and demerits of some of the methods with reference to sensitivity of detection and practical use have been discussed (221 references).

Immobilization of bio-macromolecules on self-assembled monolayers: methods and sensor applications

Natural protective glue protein, sericin bioengineered by silkworms: Potential for biomedical and biotechnological applications ☆

Silk sericin: A versatile material for tissue engineering and drug delivery.

This article comprises detailed information about L-asparaginase, encompassing topics such as microbial and plant sources of L-asparaginase, treatment with L-asparaginase, mechanism of action of L-...

L-asparaginase: a promising chemotherapeutic agent.

Potential applications of silk sericin, a natural protein from textile industry by-products.

Immobilization of L-asparaginase on the microparticles of the natural silk sericin protein and its characters.

The natural silk sericin, recovered from Bombyx mori silk waste by degumming and degrading, is a water-soluble peptide with different molecular masses, ranging from 20 to 60 kDa. It is composed of 15 sorts of amino acids, among which the polar amino acids with hydroxyl, carboxyl and amino groups such as aspartic acid, serine and lysine account for 72%. The covalent attachment of the silk sericin peptides to L-asparaginase (ASNase) produces silk sericin peptides–L-asparaginase (SS–ASNase) bioconjugates that are active, stable, have a lower immune response, and have extended half-lives in vitro in human serum. The modified enzyme coupled with sericin protein retains 55.8% of the original activity of the native enzyme. The optimal pH of SS–ASNase derivatives shifts considerably, to 5.0 in comparison with pH 6.0–8.0 of the native form. The thermostability and resistance to trypsin digestion of the modified enzyme are greatly enhanced as compared with ASNase alone. The Michaelis constant (Km) of SS–ASNase is 65 times lower than that of the enzyme alone. This suggests that the affinity of the enzyme to its substrate L-asparagine greatly increases when bioconjugated with silk sericin. The in vivo experiments also show that the silk sericin peptides have no immunogenicity, and the antigenicity of the enzyme is obviously decreased when coupled covalently with the silk sericin peptides. Copyright © 2005 Society of Chemical Industry

Synthesis of silk sericin peptides-L-asparaginase bioconjugates and their characterization

The method for preparing water soluble sericin with different molecular weights by using cocoon as raw material includes the following steps: soaking cleaned cocoon crust and waste silk in water or alkalescency solution, regulating pH value of said solution to 8-12 and making high-temp. high-pressure degrading treatment, regulating temp. or pressure, treatment time and pH value of boiling solution and controlling requirement molecular weight of water soluble sericin so as to prepare water soluble sericin solution or powder. The product can be extensively used in the fields of biological material, textile finishing agent.

Mei-Lin Tao

Papers

Immobilization of L-asparaginase on the microparticles of the natural silk sericin protein and its characters.

Synthesis of silk sericin peptides-L-asparaginase bioconjugates and their characterization

Production method of water soluble sericin