Enzymatic degradation of carboxymethyl cellulose hydrolyzed by the endoglucanases Cel5A, Cel7B, and Cel45A from <i>Humicola insolens</i> and Cel7B, Cel12A and Cel45Acore from <i>Trichoderma reesei</i>

Karlsson, Johan; Momcilovic, Dane; Wittgren, Bengt; Schülein, M.; Tjerneld, Folke; Brinkmalm, Gunnar

doi:10.1002/bip.1060

Cited by 81 publications

(78 citation statements)

References 33 publications

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“…2 it can be seen that cellotriose (3 0 ), cellotetraose (4 0 ) and cellopentaose (5 0 ) are enzyme products but not cellohexaose (6 0 ). This observation is in accordance with previous studies where CMC has been hydrolyzed by Tr Cel45A and indicates that the endoglucanase requires a substrate longer than five AGUs in order catalyze a cleavage (Karlsson et al 2002a). It is also seen that the main products are oligomers with few substituents, which is an indication on a high endoglucanase selectivity on the CMC.…”

Section: Maldi-tofmssupporting

confidence: 91%

“…Figure 7 illustrates the active site of an endoglucanase and the nomenclature of the sugar-binding subsites according to Davies et al (1997). The endoglucanase used in the present study (Tr Cel45A) has been suggested to be highly selective towards CMC (Karlsson et al 2002a). In addition, the endoglucanase must bind to a cellulose segment longer than five AGUs in order to hydrolyze the substrate (Karlsson et al 2002b).…”

Section: Monomer Analysismentioning

confidence: 98%

“…This implies that the active site of Tr Cel45A is insensitive to carboxymethyl substituents, which should lead to substantial hydrolysis of the CMC. However, according to their results from size-exclusion chromatography and reducing sugar analysis it was found that the CMC was not extensively hydrolyzed by Tr Cel45A, which has also been shown in another study (Karlsson et al 2002a).…”

Section: Introductionmentioning

confidence: 98%

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Investigation of endoglucanase selectivity on carboxymethyl cellulose by mass spectrometric techniques

et al. 2008

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The benefits of applying cellulose selective enzymes as analytical tools for chemical structure characterization of cellulose derivatives have been frequently addressed over the years. In a recent study the high selectivity of cellulase Cel45A from Trichoderma reesei (Tr Cel45A) was utilized for relating the chemical structure to the flow properties of carboxymethyl cellulose (CMC). However, in order to take full advantage of the enzymatic hydrolysis the enzyme selectivity on the cellulose substrate must be further investigated. Therefore, the selectivity of Tr Cel45A on CMC was studied by chemical sample preparation of the enzyme products followed by mass spectrometric chemical structure characterization. The results strongly suggest that, in accordance with recent studies, also this highly selective endoglucanase is able to catalyze hydrolysis of glucosidic bonds adjacent to mono-substituted anhydroglucose units (AGUs). Furthermore, the results also indicate that substituents on the nearby AGUs will affect the hydrolysis.

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Section: Maldi-tofmssupporting

confidence: 91%

Section: Monomer Analysismentioning

confidence: 98%

Section: Introductionmentioning

confidence: 98%

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Investigation of endoglucanase selectivity on carboxymethyl cellulose by mass spectrometric techniques

et al. 2008

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“…4). Correspondingly endoglucanase-initiated hydrolysis of cellulose derivatives is possible, the extent not only being dependent on the degree of substitution, but also on the substituent distribution along the cellulose chain [38] and the architecture of the enzyme protein [39]. For an effective hydrolysis of CA, endoglucanase would be the most favored especially if non-substituted or partly substituted anhydroglucose units are present (Table 2).…”

Section: Enzymology Of Cellulose Acetate Biodegradationmentioning

confidence: 99%

Degradation of Cellulose Acetate-Based Materials: A Review

Puls¹,

Wilson

Hölter³

2010

J Polym Environ

533

321

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Cellulose acetate polymer is used to make a variety of consumer products including textiles, plastic films, and cigarette filters. A review of degradation mechanisms, and the possible approaches to diminish the environmental persistence of these materials, will clarify the current and potential degradation rates of these products after disposal. Various studies have been conducted on the biodegradability of cellulose acetate, but no review has been compiled which includes biological, chemical, and photo chemical degradation mechanisms. Cellulose acetate is prepared by acetylating cellulose, the most abundant natural polymer. Cellulose is readily biodegraded by organisms that utilize cellulase enzymes, but due to the additional acetyl groups cellulose acetate requires the presence of esterases for the first step in biodegradation. Once partial deacetylation has been accomplished either by enzymes, or by partial chemical hydrolysis, the polymer's cellulose backbone is readily biodegraded. Cellulose acetate is photo chemically degraded by UV wavelengths shorter than 280 nm, but has limited photo degradability in sunlight due to the lack of chromophores for absorbing ultraviolet light. Photo degradability can be significantly enhanced by the addition of titanium dioxide, which is used as a whitening agent in many consumer products. Photo degradation with TiO 2 causes surface pitting, thus increasing a material's surface area which enhances biodegradation. The combination of both photo and biodegradation allows a synergy that enhances the overall degradation rate. The physical design of a consumer product can also facilitate enhanced degradation rate, since rates are highly influenced by the exposure to environmental conditions. The patent literature contains an abundance of ideas for designing consumer products that are less persistent in the outdoors environment, and this review will include insights into enhanced degradability designs.

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“…Use of size exclusion chromatography (SEC) in combination with MALLS or RI detection has been reported in various publications [15][16][17][18] for the determination of the extent of the hydrolysis, which causes a significant shift of the molecular mass distribution.…”

Section: Introductionmentioning

confidence: 99%

The Applicability of Enzymes in Cellulose Ether Analysis

Adden

Melander

Brinkmalm

et al. 2009

Macromolecular Symposia

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Summary: Six methyl cellulose (MC) samples, one with a DS of 1.32 and five with a DS between 1.83 and 1.88, were degraded with five different enzymes or enzyme preparations containing endoglucanases. The main goal was to investigate whether enzymes could be used for determination of heterogeneity of the substituent distribution along the cellulose chain. To obtain information about the heterogeneity it was necessary to gather information on how the enzymes affect hydrolysis. Monomer composition and methyl distribution in the polymer chain were analyzed after total or partial random hydrolysis and appropriate derivatization by GC and MS, respectively, and used as reference data for the evaluation of the enzymatic hydrolysis. Size exclusion chromatography with multi angle light scattering and refractive index detection (SEC-MALLS/RI) was used to estimate molar mass distribution of the MCs before and after hydrolysis. Electrospray and matrix assisted laser desorption/ionization (ESI and MALDI) in combination with various MS analyzers were compared with respect to quantification of the degradation products directly and after perdeuteromethylation. Methyl group distribution in the oligomeric fractions and the average DS/DP were calculated from ESI mass spectra. With help of the reference analysis, patterns could be corrected for the unspecific contribution of end groups. By labelling and ESI-MS n , our knowledge about the tolerance of the enzyme's sub-sites with respect to the number of methyl groups could be improved. A novel standard addition method in combination with electrospray ionization ion trap mass spectrometry (ESI-IT MS) was used to determine the amount of formed oligomers.

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Enzymatic degradation of carboxymethyl cellulose hydrolyzed by the endoglucanases Cel5A, Cel7B, and Cel45A from Humicola insolens and Cel7B, Cel12A and Cel45Acore from Trichoderma reesei

Cited by 81 publications

References 33 publications

Investigation of endoglucanase selectivity on carboxymethyl cellulose by mass spectrometric techniques

Investigation of endoglucanase selectivity on carboxymethyl cellulose by mass spectrometric techniques

Degradation of Cellulose Acetate-Based Materials: A Review

The Applicability of Enzymes in Cellulose Ether Analysis

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