• Korean Journal of Food Science and Technology
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• v.25 no.5
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• pp.521-525
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• 1993

To elucidate adsorption of proteins and examine the molecular behavior of protein molecules at interfaces, various proteins at the air-water interface were studied. The adsorption data of bovine serum albumin intermediates indicated that the conformational state of a protein played an important role in adsorption of proteins at interfaces. The adsorption behavior of succinylated beta-lactoglobulin indicated that the increase in the net negative charge of the protein significantly inflenced both the kinetics and thermodynamics of adsorption. The adsorption kinetics of beta-casein showed that the salt that induced break-down of water structure decreased the rate of adsorption.

• International Journal of Industrial Entomology and Biomaterials
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• v.34 no.1
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• pp.6-10
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• 2017

Dissolution of Antheraea yamamai silkworm cocoon was carried out in various solvent systems with various dissolving conditions including dissolution salts, salt concentration, dissolving temperature, and time. General chaotropic salt for Bombyx mori silk fibroin does not work for A. yamamai silkworm cocoon. Lithium bromide 9.3 M at $100^{\circ}C$ also does not work to dissolve wild silkworm cocoon. However, 9 M of lithium thiocyanate treatment at $100^{\circ}C$ induced 100% dissolution of wild silkworm cocoon. But it could not be dissolved lower than $60^{\circ}C$. Like lithium thiocyanate, less than $60^{\circ}C$ treatment with molten calcium nitrate 4 hydrate could not dissolve wild silkworm cocoon. As the dissolution temperature increased up to $100^{\circ}C$, the solubility of wild one was reached over 90%. SDS-PAGE showed broad tailing stream pattern that means the molecule of wild silk was depolymerized with dissolution temperature and time. From the above results, the best chaotropic salt for A.yamamai silkworm cocoon is calcium nitrate 4 hydrate.

• Journal of Sericultural and Entomological Science
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• v.45 no.2
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• pp.121-125
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• 2003

Dissolution of Antheraea pernyi silk fiber was carried out in a zinc nitrate 6 hydrate (Zn(NO$_3$)$_2$ㆍ6$H_2O$) solution with various dissolving conditions. The solubility was significantly dependent on the concentration of zinc nitrate, dissolving temperature and time. Regenerated A. pernyi silk fibroin powder was obtained through dialysis process to remove chaotropic salt. FTIR and X-ray diffractometer showed that the conformation of regenerated A. pernyi silk powder was sheet structure.

• Clean Technology
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• v.22 no.3
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• pp.175-180
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• 2016

Tyrosinases catalyze the hydroxylation of a monophenol (monophenolase activity) and the conversion of an o-diphenol to o-quinone (diphenolase activity), which are mainly involved in the modification of tyrosine residues into 3,4-dihydroxyphenyl-alanine (DOPA) and DOPA/DOPAquinone-derived intermolecular cross-linking. Previously, we obtained a slightly acidic and cold-active tyrosinase, tyrosinase-CNK, by our recombinant protein approach. The enzyme showed optimal activity at pH 6.0 and 20 ℃ with an abnormally high monophenolase/diphenolase activity ratio and still had approximately 50% activity compared with the highest activity even in ice water. Here, we investigated reaction stability of the recombinant tyrosinase-CNK as a psychrophilic enzyme. The enzyme showed remarkable thermal stability at 0 ℃ and the activity was well conserved in repeated freeze-thaw cycles. Although water-miscible organic solvent as reaction media caused the activity decrease of tyrosinase-CNK as expected, the enzyme activity was not additionally decreased with increased concentration in organic solvents such as ethanol and acetonitrile. Also, the enzyme showed high salt tolerance in chaotropic salts. It was remarkably considered that 2⁺ metal ions might inhibit the incorporation of Cu²⁺ into the active site. We expect that these results could be used to design tyrosinase-mediated enzymatic reaction at low temperature for the production of catechols through minimizing unwanted self-oxidation and enzyme inactivation.