Blue Jean expt 2005

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Information about Blue Jean expt 2005

Published on September 18, 2007

Author: Malbern


Textile: Enzyme Applications:  Textile: Enzyme Applications Amylase Cellulase Laccase Get the Look You Want with Enzymes Novozymes Biotech, Inc. is the Leading Industrial Enzyme Producer in the world. The Enzyme, Laccase is a Tool for creating new looks in Blue Jeans:  The Enzyme, Laccase is a Tool for creating new looks in Blue Jeans See Biotimes [ Novozymes Biotech, formerly Novo Nordisk) pg 10-11 Laccase (produced through genetic engineering) can help to create the 'Cool Jeans' Abrasion Desizing Bleaching Conventional bleaching agents brighten every thread of denium, whereas this enzyme only goes for indigo! Unlike most other fabrics, denium is dyed before being woven. In fact only the vertical yarn is dyed. Blue Jean Experiment Protocol(Dye Transfer Inhibition) Laccase-catalyzed :  Blue Jean Experiment Protocol (Dye Transfer Inhibition) Laccase-catalyzed Materials (compliments of Novozymes Biotech) Reagent 1 = Chicago sky blue 6B (textile dye)[.03 mM in H2O] Reagent 2= methyl syringate [0.2 M in ETOH] is an accelerator Reagent 3 = laccase (recombinant enzyme: 38U/ml in H2O] deionized water pipettors, tips, microfuge tubes Protocol 1: (Dye Formation) Takes ~1 minute for RXN Test: 1ml water +20 micro liter '1' + 1micro liter '2' --- ---andgt;Blue Protocol 2: (Dye Bleaching) observe reaction for ~4 minutes Test: Add 1micro liter of '3' to tube with blue solution -andgt;pink-andgt;pale yellow -andgt; clear Slide4:  Dye Transfer Inhibition at work Has laccase NO Laccase Laccase Enzymes:  Laccase Enzymes Laccases are a family of multicopper oxidases that bear a close resemblance, particularly in amino acid sequence, to ascorbate oxidase (found in cucumbers) and mammalian plasma protein ceruloplasmin. First isolated in 1883 from Rhus venicifera, the Japanese lacquer tree, laccases are also commonly found in fungi such as the lignolytic white-rot fungus Trametes versicolor. They have also recently been discovered in bacteria. Their physiological function is still under intense investigation although they are implicated in the synthesis and/or degradation of the biopolymer lignin, wound response mechanisms and the morphogenesis of microorganisms. They have a broad specificity that enables them to catalyse the one electron oxidation of a range of substrates. These substrates, usually phenolic in nature, provide electrons for the concomitant four electron reduction of atmospheric O2 to water. Catalysis takes place via the four copper centres which are classified according to their electronic properties. Laccase Enzymes:  Laccase Enzymes Currently the catalytic properties of laccases are being exploited for a range of technological applications such as the bioremediation of soils and water and the development of environmentally friendly processes in the pulp and paper industry. Much work has gone into the sequencing, cloning and mutagenesis of laccase genes from microrganisms. Recently several crystal structures containing the full complement of Cu atoms have been reported. Ribbon representation of the X-Ray crystallographic structure of Trametes versicolor laccase reported by Piontek and coworkers in 2002.

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