“…Since this commercial enzyme is not pure, these phenomena may be due to the contamination of a small quantity of -glucosidase in the mixture. The cellulase from T. Viride was known to effectively degrade the newspaper material, 44 and T. reesei 45 was known to hydrolyze the crystalline form of cellulose. In general, the enzymatic hydrolysis on the ACG slide surface is more sitespecific but much slower than that in solution.…”
Section: Resultsmentioning
confidence: 99%
“…The cellulase from T. viride was known to effectively degrade the newspaper material, and T. reesei was known to hydrolyze the crystalline form of cellulose.…”
Section: Resultsmentioning
confidence: 99%
“…The cellulase from T. Viride was known to effectively degrade the newspaper material, 44 and T. reesei 45 was known to hydrolyze the crystalline form of cellulose. In general, the enzymatic hydrolysis on the ACG slide surface is more sitespecific but much slower than that in solution.…”
A new type of glycan array covalently or noncovalently attached to aluminum oxide-coated glass (ACG) slides has been developed for studies of enzymatic reactions and protein binding. To prepare the noncovalent array, glycans with a polyfluorinated hydrocarbon (-C(8)F(17)) tail are spotted robotically onto the ACG slide surface containing a layer of polyfluorinated hydrocarbon terminated with phosphonate. After incubation and washing, the noncovalent array can be characterized by MS-TOF via ionization/desorption at a low laser energy without addition of matrix. A representative cellotetraose array was developed to study the activity and specificity of different cellulases and to differentiate the exo- and endoglucanase activities. To prepare the covalent array, glycans with a phosphonic acid tail were synthesized and spotted robotically onto the ACG slide surface. After incubation, the slides can be used directly for quantitative protein binding analysis. Compared to the preparation of glycan arrays on glass slides and other surfaces, this method of arraying using phosphonic acid reacting with ACG is more direct, convenient, and effective and represents a new platform for the high-throughput analysis of protein-glycan interactions.
“…Since this commercial enzyme is not pure, these phenomena may be due to the contamination of a small quantity of -glucosidase in the mixture. The cellulase from T. Viride was known to effectively degrade the newspaper material, 44 and T. reesei 45 was known to hydrolyze the crystalline form of cellulose. In general, the enzymatic hydrolysis on the ACG slide surface is more sitespecific but much slower than that in solution.…”
Section: Resultsmentioning
confidence: 99%
“…The cellulase from T. viride was known to effectively degrade the newspaper material, and T. reesei was known to hydrolyze the crystalline form of cellulose.…”
Section: Resultsmentioning
confidence: 99%
“…The cellulase from T. Viride was known to effectively degrade the newspaper material, 44 and T. reesei 45 was known to hydrolyze the crystalline form of cellulose. In general, the enzymatic hydrolysis on the ACG slide surface is more sitespecific but much slower than that in solution.…”
A new type of glycan array covalently or noncovalently attached to aluminum oxide-coated glass (ACG) slides has been developed for studies of enzymatic reactions and protein binding. To prepare the noncovalent array, glycans with a polyfluorinated hydrocarbon (-C(8)F(17)) tail are spotted robotically onto the ACG slide surface containing a layer of polyfluorinated hydrocarbon terminated with phosphonate. After incubation and washing, the noncovalent array can be characterized by MS-TOF via ionization/desorption at a low laser energy without addition of matrix. A representative cellotetraose array was developed to study the activity and specificity of different cellulases and to differentiate the exo- and endoglucanase activities. To prepare the covalent array, glycans with a phosphonic acid tail were synthesized and spotted robotically onto the ACG slide surface. After incubation, the slides can be used directly for quantitative protein binding analysis. Compared to the preparation of glycan arrays on glass slides and other surfaces, this method of arraying using phosphonic acid reacting with ACG is more direct, convenient, and effective and represents a new platform for the high-throughput analysis of protein-glycan interactions.
“…Even though biowaste, as a major resource for bio-energy, is not being fully utilized the enzymatic catalyzed bioconversion of waste cellulose into fermentable sugars such as glucose can be illustrated by Figure . The bioconversion process can also be influenced by variables such as cellulose pretreatment, cellulase mixtures, and cellulase nature while the composition of biowaste would also determine the amount of sugar produced by a specific cellulase system. − 1 Cellulase-catalyzed biodegradation of cellulose into reducing sugars, glucose, and cellobiose.…”
Section: Resultsmentioning
confidence: 99%
“…Used paper materials have been identified as major components of biowaste and various aspects of office paper, foolscap paper, filterpaper, newspaper, and cardboard bioconversion with P. funiculosum cellulase have been described. , This investigation had as its aim to determine the optimum bioconversion when different paper amounts were bioconverted as well as maximum sugar production when changing enzyme concentrations were applied. Sugar-producing profiles have been constructed reflecting the influence of enzyme concentration and increasing paper amounts on the extent of bioconversion and efficiency of the degradation process.…”
Renewable energy would become more topical as natural energy resources are depleted. Also
a major global issue is the extent of solid waste generation of which biowaste is the main
component and development of its bio-energy potential can address issues such as renewable
energy and environmental pollution, simultaneously. Used paper is a primary component of
biowaste with cellulose its dominant structural biopolymer. Various used paper materials have
been treated with a cellulose hydrolyzing enzyme from Penicillium funiculosum to bioconvert
their cellulose component into sugars such as glucose that could be utilized as feedstock for the
synthesis of biodegradable products such as bio-ethanol. These paper materials exhibited
nonsimilar susceptibilities toward this cellulase enzyme and consequently different sugar releasing
and bioconversion efficiency patterns were obtained when changing quantities of each paper were
treated with a fixed amount of enzyme. When a fixed amount of each paper material was treated
with increasing enzyme concentrations, different bioconversion and efficiency profiles were also
constructed for each paper material biodegraded.
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