Results 171 to 180 of about 12,890 (218)
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Nature, 1964
THERE are only a few reports of enzymes from higher plants which can hydrolyse cellulose or water-soluble cellulose derivatives. Several reports show that malt extracts are capable of hydrolysing water-soluble cellulose derivatives1,3,11 and dispersed cellulose fibres1,7.
D B, DICKINSON, J P, MCCOLLUM
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THERE are only a few reports of enzymes from higher plants which can hydrolyse cellulose or water-soluble cellulose derivatives. Several reports show that malt extracts are capable of hydrolysing water-soluble cellulose derivatives1,3,11 and dispersed cellulose fibres1,7.
D B, DICKINSON, J P, MCCOLLUM
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Visualizing cellulase activity
Biotechnology and Bioengineering, 2013AbstractCommercial exploitation of lignocellulose for biotechnological production of fuels and commodity chemicals requires efficient—usually enzymatic—saccharification of the highly recalcitrant insoluble substrate. A key characteristic of cellulose conversion is that the actual hydrolysis of the polysaccharide chains is intrinsically entangled with ...
Patricia, Bubner +2 more
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Deactivation of cellulases by phenols
Enzyme and Microbial Technology, 2011Pretreatment of lignocellulosic materials may result in the release of inhibitors and deactivators of cellulose enzyme hydrolysis. We report the identification of phenols with major inhibition and/or deactivation effect on enzymes used for conversion of cellulose to ethanol.
Eduardo, Ximenes +4 more
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Cellulose, cellulases and cellulosomes
Current Opinion in Structural Biology, 1998The structural complexity and rigidity of cellulosic substrates have given rise to a phenomenal diversity of degradative enzymes--the cellulases. Cellulolytic microorganisms produce a wide variety of different catalytic and noncatalytic enzyme modules, which form the cellulases and act synergistically on their substrate. In some microbes, several types
Bayer, E.A. +3 more
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Nature, 1968
IN their communication about direct uptake of organic solutes, Chapman and Taylor1 commented on the contradictory published accounts of the food and feeding of the polychaete Nereis virens Sars. Verrill2 stated that it is carnivorous, while Gross3 suggested that it is almost entirely herbivorous. Turnbull4 regarded the animal as omnivorous.
D B, Lewis, P J, Whitney
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IN their communication about direct uptake of organic solutes, Chapman and Taylor1 commented on the contradictory published accounts of the food and feeding of the polychaete Nereis virens Sars. Verrill2 stated that it is carnivorous, while Gross3 suggested that it is almost entirely herbivorous. Turnbull4 regarded the animal as omnivorous.
D B, Lewis, P J, Whitney
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The distribution of cellulase in invertebrates
Comparative Biochemistry and Physiology, 1964Abstract 1. 1. Seventy-four species of animals were investigated to determine whether they have cellulase activity in their digestive glands. Cellulase activity, detected by noting the reduction in viscosity of a solution of sodium carboxymethylcellulose, was found in a number of annelids, molluscs and crustaceans.
Y, YOKOE, I, YASUMASU
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Nature, 1969
CELLULASES classified as Cx attack soluble derivatives of cellulose, such as carboxymethylcellulose or hydroxyethylcellulose, and also substrates such as alkali or acid swollen cellulose. Highly ordered cellulose as in the cotton fibre is, however, not attacked.
T M, Wood, D R, Phillips
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CELLULASES classified as Cx attack soluble derivatives of cellulose, such as carboxymethylcellulose or hydroxyethylcellulose, and also substrates such as alkali or acid swollen cellulose. Highly ordered cellulose as in the cotton fibre is, however, not attacked.
T M, Wood, D R, Phillips
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A kinetic assay for cellulases
Analytical Biochemistry, 1982Abstract Research on the mechanism of action of cellulases has been hampered by the lack of a rapid, continuous, or kinetic assay. A linked assay system that uses glucose oxidase and horseradish peroxidase has been coupled with β-glucosidase to yield an assay system that can be used for kinetic assays for cellobiase-producing enzymes as well as a ...
D F, Day, W E, Workman
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