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Cellulase

Cellulase is a group of enzymes that catalyze the hydrolysis of cellulose, a major component of plant cell walls.
These enzymes play a crucial role in the breakdown of cellulosic biomass, making them valuable for applications in biofuel production, pulp and paper industry, textile processing, and animal feed.
Cellulases are produced by a variety of microorganisms, including bacteria, fungi, and protozoa, and their activity and specificity can vary widely depending on the source and environmental conditions.
Understanding the properties and optimization of cellulase enzymes is an active area of research, with potential for enhancing the efficiency and sustainability of cellulose utilization.
Reseachers can leverag AI-driven tools like PubCompare.ai to idntify the most effective cellulase protocols and products from scientific literature, preprints, and patents, accelerating advancements in this important field of study.

Most cited protocols related to «Cellulase»

1
Efficient Arabidopsis Protoplast Isolation
Cited 163 times
Leaves (width: 2 cm, length: 5 cm in optimal light condition; width: 0.5 cm; length: 2.5 cm in low light conditions) were collected from 3 to 5-week-old plants grown under optimal light (ca. 150 μE·m-2·s-1) or low light (ca. 50·μE m-2·s-1) conditions. Arabidopsis protoplasts were isolated in two ways. First, to recreate the current technique, protoplasts were made according to the procedure of Yoo et al. [4 (link)]. Second, in a new technique, selected leaves were used in a 'Tape-Arabidopsis Sandwich' experiment. The upper epidermal surface was stabilized by affixing a strip of Time tape (Time Med, Burr Ridge, IL) while the lower epidermal surface was affixed to a strip of Magic tape (3 M, St. Paul, MN). The Magic tape was then carefully pulled away from the Time tape, peeling away the lower epidermal surface cell layer. The peeled leaves (7 to 10 optimal-light-growth leaves, about 1-2 g, up to 5 g), still adhering to the Time tape, were transferred to a Petri dish containing 10 mL of enzyme solution [1% cellulase 'Onozuka' R10 (Yakult, Tokyo, Japan), 0.25% macerozyme 'Onozuka' R10 (Yakult), 0.4 M mannitol, 10 mM CaCl2, 20 mM KCl, 0.1% BSA and 20 mM MES, pH 5.7]. The leaves were gently shaken (40 rpm on a platform shaker) in light for 20 to 60 min until the protoplasts were released into the solution. The protoplasts were centrifuged at 100 × g for 3 min in an Eppendorff A-4-44 rotor (Hamburg, Germany), washed twice with 25 mL of pre-chilled modified W5 solution (154 mM NaCl, 125 mM CaCl2, 5 mM KCl, 5 mM glucose, and 2 mM MES, pH 5.7) and incubated on ice for 30 min. During the incubation period, protoplasts were counted using a hemocytometer under a light microscope. The protoplasts were then centrifuged and resuspended in modified MMg solution (0.4 M mannitol, 15 mM MgCl2, and 4 mM MES, pH 5.7) to a final concentration of 2 to 5 × 105 cells/mL.
Wu F.H., Shen S.C., Lee L.Y., Lee S.H., Chan M.T, & Lin C.S. (2009). Tape-Arabidopsis Sandwich - a simpler Arabidopsis protoplast isolation method. Plant Methods, 5, 16.
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Publication 2009
Arabidopsis Cells Cellulase Enzymes Epidermal Cells Epidermis Glucose Hyperostosis, Diffuse Idiopathic Skeletal Light Light Microscopy Magnesium Chloride Mannitol Plants Protoplasts Sodium Chloride
2
Rice Protoplast Isolation Protocol
Cited 64 times
Dehulled seeds of rice (Oryza sativa L.) cultivar Nipponbare were sterilized with 75% ethanol for 1 min. These seeds were further sterilized with 2.5% sodium hypochlorite for 20 min, washed at least five times with sterile water and then incubated on 1/2 MS medium with a photoperiod of 12 h light (about 150 μmol m-2 s-1) and 12 h dark at 26°C for 7-10 days. Green tissues from the stem and sheath of 40-60 rice seedlings were used. A bundle of rice plants (about 30 seedlings) were cut together into approximately 0.5 mm strips with propulsive force using sharp razors. The strips were immediately transferred into 0.6 M mannitol for 10 min in the dark. After discarding the mannitol, the strips were incubated in an enzyme solution (1.5% Cellulase RS, 0.75% Macerozyme R-10, 0.6 M mannitol, 10 mM MES at pH 5.7, 10 mM CaCl2 and 0.1% BSA) for 4-5 h in the dark with gentle shaking (60-80 rpm). After the enzymatic digestion, an equal volume of W5 solution (154 mM NaCl, 125 mM CaCl2, 5 mM KCl and 2 mM MES at pH 5.7) was added, followed by vigorous shaking by hand for 10 sec. Protoplasts were released by filtering through 40 μm nylon meshes into round bottom tubes with 3-5 washes of the strips using W5 solution. The pellets were collected by centrifugation at 1,500 rpm for 3 min with a swinging bucket. After washing once with W5 solution, the pellets were then resuspended in MMG solution (0.4 M mannitol, 15 mM MgCl2 and 4 mM MES at pH 5.7) at a concentration of 2 × 106 cells mL-1, determined by using a hematocytometer. The viability of protoplasts was determined by the FDA staining method as described [44 (link)]. All manipulations above were performed at room temperature.
For isolating protoplasts from etiolated rice seedlings, the sterilized seeds were germinated under light for 3 days, and then moved to the dark for another 4-7 days. The isolation procedure was the same as that for isolation of green tissue protoplasts described above.
Zhang Y., Su J., Duan S., Ao Y., Dai J., Liu J., Wang P., Li Y., Liu B., Feng D., Wang J, & Wang H. (2011). A highly efficient rice green tissue protoplast system for transient gene expression and studying light/chloroplast-related processes. Plant Methods, 7, 30.
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Publication 2011
Cells Cellulase Centrifugation Digestion Enzymes Ethanol isolation Light Magnesium Chloride Mannitol MS 1-2 Nylons Oryza sativa Pellets, Drug Plant Embryos Protoplasts Seedlings Sodium Chloride Sodium Hypochlorite Staining Stem, Plant Sterility, Reproductive Tissues
3
Rice Protoplast Isolation and Transformation
Cited 51 times
Our protoplast isolation protocol was based on the protocol for maize protoplasts provided online by J. Sheen's laboratory with several changes. Rice seeds were grown as stated above. Between 7 and 14 days post germination, plants were ~4–8 inches tall. Leaf and stem tissue was cut into 0.5 mm pieces using very sharp razors. Tissue was immediately incubated in enzyme solution (0.6 M mannitol, 10 mM MES (pH 5.7), 1.5% Cellulase RS, 0.75% Macerozyme, 0.1% BSA, 1 mM CaC12, 5 mM β-mercaptoethanol and 50 μg/ml carbenicillin) for 4 h in the dark under gentle shaking (40 rpm). After incubation, protoplasts were passed through a 35 μm nylon mesh filter. One volume of W5 solution (154 mM NaCl, 125 mM CaC12, 5 mM KC1, 2 mM MES (pH 5.7)) was added and the solution was centrifuged for 5 minutes at 1500 rpm to pellet the protoplasts. Cells were re-suspended in Mmg solution [13 (link)] (0.6 M mannitol, 15 mM MgC12, 4 mM MES (pH 5.7)) for PEG-mediated transformation at 106 cells/ml. Cells were quantified using a hemocytometer. For transformation, 40% PEG (0.6 M mannitol, 100 mM CaC12, 40% v/v PEG 3350) was added to the protoplasts for 15 minutes. Cells were washed 1× with 10 volumes of W5 and then re-suspended in incubation solution (0.6 M mannitol, 4 mM MES (pH 5.7), 4 mM KC1). Cells were incubated at 28°C in the dark overnight.
Bart R., Chern M., Park C.J., Bartley L, & Ronald P.C. (2006). A novel system for gene silencing using siRNAs in rice leaf and stem-derived protoplasts. Plant Methods, 2, 13.
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Publication 2006
2-Mercaptoethanol Carbenicillin Cells Cellulase Enzymes Germination isolation Maize Mannitol Nylons Oryza sativa Plant Embryos Plant Leaves Plants polyethylene glycol 3350 Precursor T-Cell Lymphoblastic Leukemia-Lymphoma Protoplasts Sodium Chloride Stem, Plant Tissues
4
Extracellular Protein and Enzyme Assays
Cited 29 times
Total extracellular protein contents in the culture supernatants were measured using a Bio-Rad DC protein assay kit (Bio-Rad) based on absorbance at 595 nm, with bovine serum albumin used as the standard. For protein gel electrophoresis, 30-µL aliquots of concentrated culture supernatants were subjected to sodium dodecylsulfate-polyacrylamide gel electrophoresis on Novex NuPAGE pre-cast protein gels (Thermo Fisher Scientific). Endoglucanase activity in the culture supernatants was determined using an azo-cm-cellulose assay kit (Megazyme, Wicklow, Ireland) according to the manufacturer’s protocol. Endo-1,4-β-xylanase activities were assayed with an azo-xylan kit (Megazyme) following the method specified by the manufacturer. FPA activities were assayed with Whatman No.1 filter paper as the substrate. The enzyme reactions were performed in 50 mM citrate buffer (pH 4.8) at 50 °C for 60 min, using the DNS method to quantify the released reducing sugar. Exoglucanase activity was assayed according to the method described by Zou et al. [60 (link)] and measured at 50 °C using 1.0 mg mL−1p-nitrophenyl-β-D-cellobioside (Sigma-Aldrich) as the substrate in 50 mM citrate buffer (pH 4.8) containing 1 mg mL−1d-glucono-1,5-σ-lactone. Each reaction mixture containing 250 µL of properly diluted enzyme and 250 µL of 1.0 mg mL−1 substrate in 50 mM citrate buffer (pH 4.8) was incubated for 10 min at 50 °C, and the reaction was terminated by adding 500 µL of 1 M Na2CO3. Released p-nitrophenol (pNP) was measured at an absorbance of 420 nm. Inactive enzyme, which was boiled at 100 °C for 10 min, was used as a control. pNP was used for the standard curve. In the exoglucanase activity analyses, one unit (U) of enzymatic activity was defined as the amount of 1 μmol glucose or pNP released by 1 mL of enzyme from the substrate per minute under the standard assay conditions. All estimates were performed in three repeated assays. The statistical significance of differences among WT and mutant strains was assessed by one-way analysis of variance.
Liu Q., Gao R., Li J., Lin L., Zhao J., Sun W, & Tian C. (2017). Development of a genome-editing CRISPR/Cas9 system in thermophilic fungal Myceliophthora species and its application to hyper-cellulase production strain engineering. Biotechnology for Biofuels, 10, 1.
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Publication 2017
4-nitrophenol Biological Assay Buffers Carbohydrates CD3EAP protein, human Cellulase Cellulose Citrates Electrophoresis endometriosis protein-1 enzyme activity Enzymes Gels Glucose Lactones Nitrophenols Proteins SDS-PAGE Serum Albumin, Bovine Strains Xylans
5
Screening Cellulase-Producing Microorganisms
Cited 13 times
The medium used for the second screening step using the Congo red test was similar to that described above (Section 2.2), except that the carbon source was low viscosity carboxymethylcellulose (CMC) (Sigma, USA). Only those strains that showed substantial growth in the initial screening with Avicel were selected for the Congo red test. Inoculation was carried out by using a platinum needle to transfer the spores from the PDA plate to the center of the plates containing the CMC medium [18 ]. The inoculated plates were incubated for 96 h at 30°C and the growth of the microorganism was measured by the diameter of the colony. A 10 mL aliquot of Congo red dye (2.5 g·L−1) was then added to each plate. After 15 min, the solution was discarded and the cultures were washed with 10 mL of 1 mol·L−1 NaCl. Cellulase production was indicated by the appearance of a pale halo with orange edges, indicative of areas of hydrolysis. This halo was measured for subsequent calculation of the enzymatic index (EI) using the expression:
EI=diameter  of  hydrolysis  zonediameter  of  colony.
The strains that showed an EI higher than 1.50 were considered to be potential producers of cellulases. Three independent experiments were performed for this screening step, with two replicates per strain. For each strain the average EI of the three experiments was calculated, together with the standard deviation.
Florencio C., Couri S, & Farinas C.S. (2012). Correlation between Agar Plate Screening and Solid-State Fermentation for the Prediction of Cellulase Production by Trichoderma Strains. Enzyme Research, 2012, 793708.
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Publication 2012
Avicel Carbon Carboxymethylcellulose Cellulase Cellulases Enzymes Hydrolysis Needles Platinum Sodium Chloride Spores Strains Vaccination Viscosity

Most recents protocols related to «Cellulase»

1
Sugar Snake Degradation by Surfactants
Not available on PMC !

Example 2

Another wider test was completed using a method in which a piece of sugar snake (weight previously recorded) was incubated in chemistry containing surfactant. After a set time, the remaining sugar snake was removed and quantified by water displacement in a graduated cylinder. After treatment, sugar snake degradation was determined by subtracting the volume (mL) of water displacement from the starting weight (grams). Each variation was compared to a control where the surfactant was omitted. The same three terms as above (synergistic, compatible, and less favorable) were used to identify the enzyme compatibility of each surfactant. Results are shown in Table 4.

TABLE 4
Concen-IncubationPercentCompat-
trationTimeDegra-ibility
Surfactant(wt. %)pH(hr)dationRating
Tergitol442461Less
NP-12Favorable
Ecosurf SA-944885Compatible
Amphosol CG44854Compatible
Mackam 50-SB44851Compatible
Bioterge44827Less
AS-40KFavorable
APG 325N44785Compatible
APG 325N410743Less
Favorable
Barlox 1244785Compatible
Barlox 12410716Less
Favorable
SXS44785Compatible
SXS24711Compatible
Pluronic 25R44858Compatible

US11859157B2. Synergistic cellulase-surfactant interactions for degradation of bacterial cellulose (2024-01-02). ECOLAB USA INC. [US]. Inventors: Jesse Ray Murphy [US], Lyndal Jensen [US].
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Patent 2024
Bacteria Carbohydrates Cellulase Cellulose Enzymes NP-27 Pluronics Snakes Surface-Active Agents Tergitol 4
2
Cellulase Compositions for Sugar Snake Degradation
Not available on PMC !

Example 3

Multiple enzyme compositions comprising a cellulase were evaluated to determine sugar snake degradation performance as a baseline without potential surfactant synergy to assess the role of the enzyme composition versus improvement based on surfactant synergy. Compositions were prepared with 0.5 wt. % enzyme composition, 1.7 wt. % sodium citrate buffer, and water at a pH of 4.25. The four enzyme compositions tested were obtained from Novozymes and included: DRAIN EASE FLOW™, CELLUCLEAN CLASSIC 700T®, CELLUCLAST CONCENTRATED BG®, and Cellulase C. A sugar snake of equal mass was measured and the cleaning compositions were applied to it. The percent degradation of the sugar snake (based on mass) was evaluated after 2 hours of contact and after 24 hours of contact. The percent degradation is shown in FIG. 2 where 100 indicates 100% degradation. As can be seen in FIG. 2, CELLUCLAST CONCENTRATED BG® provided the best sugar snake degradation at both the 2-hour time and 24-hour time. DRAIN EASE FLOW™ and Cellulase C performed substantially similar and CELLUCLEAN CLASSIC 700T® did not appear to degrade the sugar snake at all.

US11859157B2. Synergistic cellulase-surfactant interactions for degradation of bacterial cellulose (2024-01-02). ECOLAB USA INC. [US]. Inventors: Jesse Ray Murphy [US], Lyndal Jensen [US].
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Patent 2024
Bacteria Buffers Carbohydrates Cellulase Cellulose Endoglucanase C Enzymes Snakes Sodium Citrate Surface-Active Agents Vision
3
Enzyme Blend Enhances Waste Solubilization
Not available on PMC !

Example 4

Experiments were performed in 100 ml Kautex bottles. Model waste was mixed with water to a volume at 50 ml and at TS concentration of 7.5%. CBC and the selected blend (B.a protease:T.I pholip:A.a BG:CBC in ratio of 10:5:15:70) were added in amounts corresponding to 0%, 25%, 50%, 75%, 100% and 200% of the concentration that has been used as default during the previous experiments (2.4% enzymes protein/TS). Bottles were incubated on a Stuart Rotator SB3 and placed in a 50° C. oven for 24 hours.

A significant improvement in TS-solubilization was seen at all applied enzyme concentrations, when comparing the blend with CBC. The TS-solubilization at default settings (2.4% CBC/TS) was around 25%. This was obtained with only approximately 0.9% of the blend, which corresponds to a lowering in enzyme dosage of approximately 2.5 to 2.7 times (See FIG. 2). At the same time we found a clear increase in hydrolysis and fermentation products such as glucose, xylose, lactic acid (FIG. 3, and FIG. 5). This is a surprise since 15% of CBC (cellulase and xylanase activities) was replaced with the lipase and protease.

US11873522B2. Solubilization of MSW with blend enzymes (2024-01-16). Renescience A/S [DK]. Inventors: Hanne Risbjerg Soerensen [DK], Lisa Rosgaard [DK], Henrik B. Nielsen [DK], Lone Baekgaard [DK], Joanna Wawrzynczyk [DK].
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Patent 2024
Cellulase Enzymes Fermentation Glucose Hydrolysis Lactic Acid Lipase Peptide Hydrolases Proteins Xylose
4
Enzyme Stability in Cleaning Compositions
Not available on PMC !

Example 5

Enzyme stability was tested in cleaning compositions prepared with differing stabilizers. All test compositions were prepared containing 0.5% DRAIN EASE FLOW™ 2% Tween® 20, and 1.8% sodium citrate buffer in water prepared at a pH of about 4.5 Enzyme stability was assessed by an activity assay. The results are provided in FIG. 4. Formulations containing 20% PEG 400® and 20% glycerol showed 84% and 83% retention of DRAIN EASE FLOW™ activity after 8 weeks at 37° C. Formulations containing 20% propylene glycol showed 100% retention of DRAIN EASE FLOW™ activity under the same conditions. Indicating the stabilizers did provide enzyme stability and retention.

US11859157B2. Synergistic cellulase-surfactant interactions for degradation of bacterial cellulose (2024-01-02). ECOLAB USA INC. [US]. Inventors: Jesse Ray Murphy [US], Lyndal Jensen [US].
Full text: Click here
Patent 2024
Bacteria Biological Assay Buffers Cellulase Cellulose Enzyme Stability Glycerin polyethylene glycol 400 Propylene Glycol Retention (Psychology) Sodium Citrate Surface-Active Agents Tween 20
5
Endoglucanase Activity Quantification
The endoglucanase (EG) activity
was assessed by measuring the release of reducing sugars in a reaction
mixture containing the crude extract and carboxymethyl cellulose (0.5%
w/v) as a substrate in 50 mM Na acetate buffer (pH 5) at 50 °C
for 60 min (T. reesei) or 120 min (T. atroviride).27 (link) The
reducing sugars released were determined using the 3,5-dinitrosalicylic
acid (DNS) method. One unit (U) of endoglucanase activity was defined
as the amount of enzymes that released 1 μmol of glucose equimolar
per minute under the assay conditions27 (link) and normalized by grams of the fermented substrate (U/g).
Bulgari D., Alias C., Peron G., Ribaudo G., Gianoncelli A., Savino S., Boureghda H., Bouznad Z., Monti E, & Gobbi E. (2023). Solid-State Fermentation of Trichoderma spp.: A New Way to Valorize the Agricultural Digestate and Produce Value-Added Bioproducts. Journal of Agricultural and Food Chemistry, 71(9), 3994-4004.
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Publication 2023
Acetate Biological Assay Buffers Carboxymethylcellulose Cellulase Complex Extracts Enzymes Glucose Sugars

Top products related to «Cellulase»

1
Cellulase by Merck Group
Sourced in United States, Germany, Italy, United Kingdom, China, Spain, Ireland, France
Cellulase is a type of enzyme that catalyzes the hydrolysis of cellulose, a major structural component of plant cell walls. It is used in various industrial and research applications.
2
Cellic ctec2 by Novozymes
Sourced in Denmark, United States, China
Cellic® CTec2 is a commercial enzyme product developed by Novozymes. It is a cellulase enzyme complex designed for the hydrolysis of cellulosic biomass. The product contains a blend of cellulolytic enzymes that work synergistically to break down cellulose into fermentable sugars.
3
Pectinase by Merck Group
Sourced in United States, Germany, Japan, France
Pectinase is an enzyme used in laboratory applications. It functions to break down pectin, a complex carbohydrate found in plant cell walls.
4
Pectolyase by Merck Group
Sourced in United States, Japan, Spain
Pectolyase is a laboratory enzyme used to break down pectin, a structural component found in plant cell walls. It is commonly used in various biotechnology and plant science applications.
5
Cytohelicase by Merck Group
Sourced in Japan, United States
Cytohelicase is a laboratory equipment product developed by Merck Group. It is a specialized device designed for the analysis and study of cellular processes. The core function of Cytohelicase is to facilitate the investigation of DNA unwinding and replication activities within cells.
6
Onozuka r 10 by Serva Electrophoresis
Sourced in Germany, United States
Onozuka R-10 is a cellulase enzyme preparation derived from the fungus Trichoderma viride. It is commonly used in various biotechnology applications, including plant cell wall degradation and sample preparation for electrophoresis.
7
Celluclast 1.5 l by Merck Group
Sourced in United States, Germany, China
Celluclast 1.5 L is an enzymatic product from Merck Group. It is a liquid formulation containing cellulase enzyme complex.
8
Avicel ph 101 by Merck Group
Sourced in United States, Germany, China, France, United Kingdom, Sao Tome and Principe, Norway, Macao, Japan
Avicel PH-101 is a microcrystalline cellulose product manufactured by Merck Group. It is a white, odorless, and tasteless powder that is used as an excipient in the pharmaceutical and dietary supplement industries.
9
Cellic ctec2 cellulase by Novozymes
Sourced in United States, Denmark, China
Cellic CTec2 is a cellulase enzyme preparation produced by Novozymes. It is designed to hydrolyze cellulose into fermentable sugars. The core function of Cellic CTec2 is to break down cellulosic materials to facilitate the conversion of lignocellulosic biomass into biofuels and other bio-based products.
10
Xylanase by Merck Group
Sourced in United States, Germany, Italy
Xylanase is an enzyme that catalyzes the breakdown of xylan, a type of hemicellulose found in plant cell walls. It is commonly used in various industrial applications, such as the production of biofuels, food processing, and paper and pulp industries.

More about "Cellulase"

Cellulases are a group of enzymes that play a crucial role in the breakdown of cellulose, a major component of plant cell walls.
These hydrolytic enzymes catalyze the cleavage of cellulosic biomass, making them invaluable for a variety of industrial applications, including biofuel production, pulp and paper processing, textile manufacturing, and animal feed formulation.
Cellulases are produced by a diverse range of microorganisms, such as bacteria, fungi, and protozoa, and their specific activity and characteristics can vary depending on the source and environmental conditions.
Synonyms and related terms for cellulases include Cellic® CTec2, Pectinase, Pectolyase, Cytohelicase, and Onozuka R-10.
These enzymes are often used in combination with other hydrolytic enzymes, like Cellulclast 1.5 L and Xylanase, to enhance the efficiency of cellulose and hemicellulose degradation.
The substrate Avicel PH-101 is commonly used to assess the performance of cellulase enzymes.
Researchers and industry professionals are actively exploring ways to optimize the properties and performance of cellulase enzymes, leveraging advanced tools like PubCompare.ai to identify the most effective protocols and products from scientific literature, preprints, and patents.
By harnessing the power of AI-driven protocol optimization, they can accelerate advancements in this critical field of study, ultimately enhancing the sustainability and efficiency of cellulose utilization.