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PubMed2001

Baker's asthma due to xylanase and cellulase without sensitization to alpha-amylase and only weak sensitization to flour.

BACKGROUND: The baking additives xylanase and cellulase were described as baking additives causing baker's asthma. It is not known whether monosensitization to these enzymes may occur. METHODS: We present a case report of a baker with work-related asthma evaluated by skin prick test (SPT), enzyme-linked immunosorbent assay (EAST), immunoblot, EAST and immunoblot inhibition, and specific bronchial challenge. Fungal xylanase and alpha-amylase were measured by two-site enzyme immunoassays in products used by the patient at work. RESULTS: Allergy to xylanase and cellulase was demonstrated by SPT, EAST, immunoblot and specific bronchial challenge (for xylanase only). No sensitization to alpha-amylase could be demonstrated, but there was a weak flour allergy as documented by EAST and immunoblot and a positive occupational-type challenge with high concentrations of rye flour. Four baking additives contained measurable amounts of fungal alpha-amylase and xylanase, without a correlation between these enzymes. CONCLUSIONS: We conclude that occupational asthma due to the baking additives xylanase and cellulase may occur without concomitant sensitization to alpha-amylase and only weak sensitization to flour.

Adult↗
PubMed2005

A thin carboxymethyl cellulose culture substrate for the cellulase-induced harvesting of an endothelial cell sheet.

Engineered tissues constructed with two-dimensionally organized cells provide promising parts for reconstructing damaged tissues. Here we propose a new method for fabricating a 2D sheet made of an endothelial cell monolayer. First a culture substrate was prepared by treating the glass surface with an amine-terminated organosilicon derivative, followed by the covalent attachment of a thin carboxymethyl cellulose (CMC) layer. Fibronectin was immobilized onto the CMC-coated surface to promote cell adhesion. These surfaces were characterized step by step by means of contact angle measurement and X-ray photoelectron spectroscopy. Porcine aortic endothelial cells adhered to the culture substrate and consequently formed a confluent monolayer. When the substrate-cell composite was immersed in a cellulase solution, a cell sheet was spontaneously detached from the substrate due to enzymatic digestion of the CMC layer. The cell-cell connections were well preserved in the cell sheet, even after detachment from the substrate, most likely due to the fact that cellulase is harmless to mammalian cells. The cell sheet could be transferred to other culture dish with the aid of a hydrophilic membrane support, retaining the proliferation activity of the cells. The results obtained in this study demonstrate that cellulase treatment of the CMC layer is a rational and efficient method for obtaining a 2D cell sheet.

Animals↗
PubMed1996

Structures and activity of cellulase inhibitors enzymatically synthesized from cellooligosaccharides and 1-deoxynojirimycin.

Cellulase inhibitors were synthesized from cellooligosaccharides and 1-deoxynojirimycin (DNJ) by transglycosylation, using a commercial cellulase. The structures of these cellulase inhibitors were proved to be 4-O-beta-cellobiosyl-DNJ, 4-O-beta-D-glucopyranosyl-DNJ and 6-O-beta-cellobiosyl-DNJ by the results of 13C- and 1H-NMR analyses. The inhibitory activity of each inhibitor was investigated against several carboxymethylcellulases.

1-Deoxynojirimycin↗
PubMed2004

Characterization and performance of immobilized amylase and cellulase.

The performance of cellulase and amylase immobilized on siliceous supports was investigated. Enzyme uptake onto the support depended on the enzyme source and immobilization conditions. For amylase, the uptake ranged between 20 and 60%, and for cellulase, 7-10%. Immobilized amylase performance was assessed by batch kinetics in 100-300 g/L of corn flour at 65 degrees C. Depending on the substrate and enzyme loading, between 40 and 60% starch conversion was obtained. Immobilized amylase was more stable than soluble amylase. Enzyme samples were preincubated in a water bath at various temperatures, then tested for activity. At 105 degrees C, soluble amylase lost approximately 55% of its activity, compared with approximately 30% loss for immobilized amylase. The performance of immobilized cellulase was evaluated from batch kinetics in 10 g/L of substrate (shredded wastepaper) at 55 degrees C. Significant hydrolysis of the wastepaper was also observed, indicating that immobilization does not preclude access to and hydrolysis of insoluble cellulose.

Amylases↗
PubMed2004

Effects of sugar inhibition on cellulases and beta-glucosidase during enzymatic hydrolysis of softwood substrates.

A quantitative approach was taken to determine the inhibition effects of glucose and other sugar monomers during cellulase and beta-Glucosidase hydrolysis of two types of cellulosic material: Avicel and acetic acid-pretreated softwood. The increased glucose content in the hydrolysate resulted in a dramatic increase in the degrees of inhibition on both beta-Glucosidase and cellulase activities. Supplementation of mannose, xylose, and galactose during cellobiose hydrolysis did not show any inhibitory effects on beta-Glucosidase activity. However, these sugars were shown to have significant inhibitory effects on cellulase activity during cellulose hydrolysis. Our study suggests that high-substrate consistency hydrolysis with supplementation of hemicellulose is likely to be a practical solution to minimizing end-product inhibition effects while producing hydrolysate with high glucose concentration.

Acetic Acid↗
PubMed2006

Effect of beta-cyclodextrin in artificial chaperones assisted foam fractionation of cellulase.

Foam fractionation has the potential to be a low-cost protein separation process; however, it may cause protein denaturation during the foaming process. In previous work with cellulase, artificial chaperones were integrated into the foam fractionation process in order to reduce the loss of enzymatic activity. In this study, other factors were introduced to further reduce the loss of cellulase activity: type of cyclodextrin, cyclodextrin concentration, dilution ratio cyclodextrin to the foamate and holding time. alpha-Cyclodextrin was almost as effective as beta-cyclodextrin in refolding the foamed cellulase-Cetyltrimethylammonium bromide mixture. beta-Cyclodextrin (6.5 mM) was almost as effective as 13 mM beta-cyclodextrin in refolding. The dilution ratio, seven parts foamate and three parts beta-cyclodextrin solution, was found to be most effective among the three ratios tested (7:3, 1:1, and 3:7). The activity after refolding at this dilution ratio is around 0.14 unit/mL. The refolding time study showed that the refolding process was found to be most effective for the short refolding times (within 1 h).

Cellulase↗
PubMed2006

Evaluation of cellulase preparations for hydrolysis of hardwood substrates.

Seven cellulase preparations from Penicillium and Trichoderma spp. were evaluated for their ability to hydrolyze the cellulose fraction of hardwoods (yellow poplar and red maple) pretreated by organosolv extraction, as well as model cellulosic substrates such as filter paper. There was no significant correlation among hydrolytic performance on pretreated hardwood, based on glucose release, and filter paper activity. However, performance on pretreated hardwood showed significant correlations to the levels of endogenous beta-glucosidase and xylanase activities in the cellulase preparation. Accordingly, differences in performance were reduced or eliminated following supplementation with a crude beta-glucosidase preparation containing both activities. These results complement a previous investigation using softwoods pretreated by either organosolv extraction or steam explosion. Cellulase preparations that performed best on hardwood also showed superior performance on the softwood substrates.

Cellulase↗
PubMed2000

Successive construction of cellulase hyperproducers of Trichoderma using hyperpolyploids.

When the swollen conidia of Trichoderma reesei QM 6a are treated with 0.1% (w/v) colchicine solution, huge autopolyploid nuclei can be formed in those swollen conidia. When a mycelial mat derived from such a conidum is treated with a haploidizing reagent, benomyl, many fan-shaped sectors are produced from the colony, and cellulase hyperproducers are selected from conidia on the colony. When colchicine and benomyl treatments are repeated on cellulase hyperproducers, new hyperproducers can be constructed successively and systematically. Moreover, when conidia derived from autopolyploids are treated with ethylmethanesulfonate solution, another type of cellulase hyperproducers (polyploids) can be obtained.

Benomyl↗
PubMed2001

Influence of operating conditions and vessel size on oxygen transfer during cellulase production.

The production of low-cost cellulase enzyme is a key step in the development of an enzymatic-based process for conversion of lignocellulosic biomass to ethanol. Although abundant information is available on cellulase production, little of this work has examined oxygen transfer. We investigated oxygen transfer during the growth of Trichoderma reesei, a cellulase-producing microorganism, on soluble and insoluble substrates in vessel sizes from 7 to 9000 L. Oxygen uptake rates and volumetric mass transfer coefficients (kLa) were determined using mass spectroscopy to measure off gas composition. Experimentally measured kLa values were found to compare favorably with a kLa correlation available in the literature for a non-Newtonian fermentation broth during the period of heavy cell growth.

Biomass↗
PubMed2003

Regulation of Trichoderma cellulase formation: lessons in molecular biology from an industrial fungus. A review.

The present article reviews the current understanding of regulation of cellulase gene transcription in Hypocrea jecorina (= Trichoderma reesei). Special emphasis is put on the mechanism of action of low molecular weight inducers of cellulase formation, the presence and role of recently identified transactivating proteins (Ace1, Ace2, Hap2/3/5), and the role of the carbon catabolite repressor Cre1. We also report on some recent genomic approaches towards understanding how cellulase inducers signal their presence to the transcriptional apparatus.

Base Sequence↗
PubMed2001

New E. coli cloning vector using a cellulase gene (celA) as a screening marker.

The extracellular endoglucanase A gene of Clostridium thermocellum (celA) was used as a screening marker for E. coli cloning vector A 1.4-kb EcoRI fragment containing celA from pTvec/celA was isolated and cloned into a pUC18 deleting beta-galactosidase gene fragment. The constructed vectors, pCEL1, pCEL10, pCEL11, and pCEL20, have different multiple cloning sites within celA. If the cellulase, CelA, is inactivated by insertion of a foreign DNA fragment into multiple cloning sites, the recombinant transformants show no clear halos on an agar plate containing cellulose. This process overcomes the ambiguity of color screening in the X-gal/beta-galactosidase system, and over 90% of the recombinant transformants with no halos have foreign DNA inserts. Several E. coli strains were transformed successfully with pCEL series vectors regardless of mutation for alpha-complementation. Because E. coli strains do not have a cellulase gene, a vector using a cellulase gene screening marker can be used in any E. coli strain without limit. The new cloning system is very efficient, convenient, and cost effective.

Base Sequence↗
PubMed1997

In vitro determination of ruminal protein degradability of alfalfa and prairie hay via a commercial protease in the presence or absence of cellulase or driselase.

Ruminal protein degradation of alfalfa (2.62% N, 49.6% NDF, and in vivo undegradable intake protein [UIP] = 16.4% of CP) and prairie hay (.88% N, 69.4% NDF, and in vivo UIP = 44.5% of CP) was estimated using the Streptomyces griseus protease (SGP) in vitro method with or without pretreatment with two carbohydrases: cellulase from Penicillium funiculosum or driselase from Basidiomycetes. Driselase is a broad-spectrum carbohydrase. Incubating forage samples for 48 h with cellulase or driselase at a concentration of 800 mg/g per g of hay nearly maximized ADF and NDF disappearances. This concentration and incubation time then were used to pretreat hay samples. A 2-h pretreatment was included to evaluate the potential for reducing the analysis time. Other sets of samples were or were not pretreated with acetate buffer alone. Following pretreatment, samples were subjected to SGP for .25, .5, 1, 2, 4, 8, 12, 24, and 48 h. Pretreatment altered the sizes of protein pools and their degradation rates. When the UIP contents of the forages were estimated using SGP and a single-pool, first-order, kinetic model, cellulase (48 h) or driselase pretreatments yielded UIP predictions that were more similar to in vivo values. Some carbohydrase and protease combinations also yielded single time-point estimates of UIP that were similar to in vivo values. Similarly, when sufficient time was permitted for protease incubation, single time-point estimates derived from protease alone were similar to in vivo values.

Animals↗
PubMed1999

Treatment of gastric phytobezoars with cellulase.

BACKGROUND: The aim of our study was to analyze the efficacy of cellulase in dissolving gastric phytobezoars. METHODS: We carried out a prospective study over a period of 1 year. All patients (7 cases) diagnosed as having gastric phytobezoar on gastroscopy were treated with cellulase. RESULTS: Complete dissolution of the gastric phytobezoar was achieved in all 7 patients. No side effects or recurrences occurred during follow-up. DISCUSSION: We conclude that cellulase should be regarded as the treatment of choice for gastric phytobezoars because of its efficacy, and because of the lack of side effects or recurrences. However, further clinical trials are necessary to verify these findings.

Adult↗
PubMedDate not supplied

[Enzyme regeneration during hydrolysis of steam-pretreated willow and requirement for cellulase complex composition].

In order to reduce the total enzyme consumption in high-solids static hydrolysis of nonwashed steam-exploded willow Salix caprea by mixed cellulase of Trichoderma reesei + Aspergillus foetidus, two different approaches were proposed. In the first case, the enzyme activity adsorbed on residual solids after extended hydrolysis was used for hydrolysis of the newly added substrate. The initial mixing of fresh and hydrolyzed substrates was sufficient for the adsorbed enzyme redistribution and conversion of the new substrate portion, and permanent mechanical stirring was not required. Feeding of two additional portions of the exploded hardwood adjusted to pH 4 with dry caustic into the reactor with simultaneous replacement of accumulated sugars with fresh buffer (pH 4.5) resulted, on average, in a 90% conversion of cellulose at the final enzyme loading 8 IFPU per g ODM substrate, an average sugar concentration of 12%, and a glucose/xylose ratio of 5:1. In the second approach, weakly adsorbed cellulase fractions were used for static high-solids hydrolysis followed by their ultrafiltration recovery from the resultant sugar syrup. In contrast to the initial cellulase mixture whose residual activity in a syrup did not exceed 5-10% at the end of hydrolysis (48 h), up to 60% of weakly adsorbed enzyme fraction could be separated from sugar syrups by ultrafiltration and then reused. Weakly adsorbed enzymes displayed a hydrolysis efficiency of not less than 80% per IFPU enzyme consumed in extended hydrolysis of pretreated willow as compared to the original enzyme mixture. An electrophoretic study of the weakly adsorbed enzyme fraction identified T. reesei cellobiohydrolase II as the predominant component, whereas clear domination of T. reesei cellobiohydrolase I was found by electrophoresis of proteins tightly bound to hydrolysis residual solids.

Aspergillus↗
PubMed2002

[Effect of pectinase and cellulase addition on in vitro digestibility of common bean (Phaseolus vulgaris)].

Effect of commercial pectinase and cellulase addition on in vitro digestibility of two common bean (Phaseolus vulgaris) varieties, black (Brunca) and red (Chirripó), was measured. Constant conditions of pH (6.3-6.4), time (60 min), and temperature (40 degrees C) were held, and three enzyme concentrations were tested: 0.25%, 0.5% and 1.0% m/m. In vitro digestibility increases for black beans were 6.9%; 9.5% and 12.3% (p < 0.05), and for red beans were 8.9%; 10.2% and 12.9% (p < 0.05), with increasing pectinase concentration. Effects of cellulase were dependent upon both, enzyme concentration and bean variety. In vitro digestibility of red beans increased by 5.7%; 9.2% and 12.0% with increasing cellulase concentration; digestibility of black beans increased by less than 5%. No significant difference (p > 0.05) in general acceptance of enzyme treated beans (black or red) or nontreated beans was noted.

Cellulase↗
PubMedDate not supplied

[Cellulases from microorganisms].

Compositions of cellulase-hemicellulase systems of aerobic fungi (hyphomycetes, ascomycetes, and basidiomycetes), aerobic bacteria, actinomycetes, as well as anaerobic fungi and bacteria, are considered in the context of modern structural classification of glycosyl hydrolases. A new nomenclature of cellulases and relative enzymes based on their structural classification is reviewed. Some opportunities of cellulase improvement by means of protein engineering are discussed.

Bacteria, Aerobic↗
PubMed1975

Sugar production from agricultural woody wastes by saccharification with Trichoderma viride cellulase.

The saccharification of agricultural woody wastes was studied using a commercial enzyme preparation, Cellulase onozuka, derived from Trichoderma viride or the solid culture extracts of the fungus. With the intention of producing sugar at low cost, a simple procedure of enzymatic saccharification of rice straw, bagasse, and sawdust was studied. Delignifying methods of these wastes were investigated using dilute sodium hydroxide solution and dilute peracetic acid. Rice straw and bagasse were effectively delignified by boiling in a 1% sodium hydroxide solution for 3 hr or by autoclaving at 120 degrees C in a 1% sodium hydroxide solution for 1 hr. The sawdust from a broad leaved tree (Machilus thunbergii) was delignified by autoclaving at 120 degrees C in a 1% sodium hydroxide solution for 1 hr and by subsequent boiling in diluted 1/5 peracetic acid for 1 hr. This type of sawdust was also delignified by boiling in 1/5 peracetic acid for 1 hr and by subsequent autoclaving at 120 degrees C in a 1% sodium hydroxide solution for 1 hr. The sawdust from a coniferous tree (Cryptomeria japonica) was delignified by boiling in 1/5 peracetic acid for 1 hr and by subsequent autoclaving at 120 degrees C in a 1% sodium hydroxide solution for 1 hr; however, the successive treatment by autoclaving with alkali solution and subsequent boiling with diluted peracetic acid failed to bring about the desired effect. The saccharification of delignified rice straw, bagasse, and sawdust was examined using Cellulase onozuka, wheat bran or rice straw solid culture at various substrate concentrations, resulting in the formation of 5 to 10% sugar solutions after incubation at pH 5.0, 45 degrees C for 48 hr. The optimum substrate concentration existed at around 10%. Reuse of cellulase solution and resaccharification of residual sawdust were considered to be inadequate.

Candida↗
PubMed2003

[Expression of a thermostable bacterial cellulase in transgenic tobacco plants].

The bacterial gene of the thermostable endo-beta-1,4-glucanase (cellulase) was shown to retain its activity and substrate specificity when expressed in transgenic tobacco plants. The leader peptide of the carrot extensin was efficient in transferring the bacterial enzyme into the apoplast. The expression of the bacterial cellulase gene leads to changes in the plant tissue morphology. In the transgenic plant lines, regeneration of primary shoots from callus occurred at the three to five times higher cytokinin (6-BAP) concentration than in control plants. The transgenic plants that expressed the bacterial gene exhibited increased business and altered leaf shape. The transgenic plants developed can be used as models for studying the cellulases role and function in plants.

Bacterial Proteins↗