Aspen, poplar and corn stover substrates used for lignin extraction were obtained from a local industry in Chengdu, Sichuan province, China. Bleached Kraft bamboo pulp was kindly donated by a local paper industry (Chengdu, China). It had a cellulose content of 78.3% and xylan content of 15.5%. Cyclohexanol and 2-chloro-4,4,5,5-tetramethyl-1,3,2-dioxaphospholane (TMDP, Product No. 447536) were purchased from Sigma-Aldrich (Shanghai, China). Cellic CTec2 enzyme was kindly provided by Novozymes in Beijing of China (protein concentration was 228.7 mg mL−1, enzyme activity was 144 FPU mL−1). Other reagents and solvents were purchased from Kelong Chemical Regent Co., Ltd. (Chengdu, China) and used as received.
Cellic ctec2 enzyme
Manufactured by Novozymes
Sourced in Denmark
Cellic CTec2 is an enzyme product developed by Novozymes. It is designed to enhance the efficiency of biomass conversion processes. The core function of Cellic CTec2 is to break down cellulose and hemicellulose, the main components of plant cell walls, into fermentable sugars.
Automatically generated - may contain errors
6 protocols using cellic ctec2 enzyme
1
Lignin Extraction from Diverse Lignocellulosic Feedstocks
2
Arabidopsis Biomass Saccharification
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Milled Arabidopsis biomass samples were individually hand weighed to 5 mg (+/−3%) and then placed into a 96-well Hastelloy reactor plate. The wells were filled with 200 µL of deionized water, sealed with 3 M brand Teflon tape and left to incubate at 50 °C overnight for approximately 16 to 17 h to fully hydrate. The Hastelloy plates were then taken out and cooled to room temperature before being heated to 180 °C at 130 psi for 12.5 min in a 2 gallon Parr rector (model 2550). These sample plates were then rapidly cooled with water and centrifuged at 1700 rpm for 20 min. Following centrifugation, 40 µL of Novozymes Cellic CTEC2 enzyme diluted to 8.75 mg/mL was added, and the sample plates were incubated for 70 h at 50 °C. Samples were then removed, allowed to cool to RT before centrifuging again at 1700 rpm for 20 min. The samples were then prepared at a 1:100 final dilution into Megazyme Gopod (glucose oxidase/peroxidase) and XDH (xylose dehydrogenase) colorimetric assays to determine their D-glucose and by UV spectrophotometry. Calculation of glucose conversion yield was determined by taking the average mass of biomass measured in each sample well, calculating the mg glucan content by multiplication, and then taking the glucan liberated by the digestion and diving by the glucan present in the sample to yield a percent conversion.
3
Wheat Bran Bioconversion Protocol
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Wheat bran (WB) (0.5–2 mm) was a generous gift by the company BioWanze (Wanze, Belgium).
Acetonitrile (>99.9%) was purchased from Carlo Erba Reagents (Dasit Group S.p.A, Cornaredo, Italy). 2-methylbutan-2-ol (2M2B, 99%), pentan-1-ol (>99%), lauric acid (99%), methyl laurate (99%), molecular sieves (3 and 5 Å) and the enzyme Novozym 435 (immobilized lipase on acrylic resin from Candida antarctica) were purchased from Sigma-Aldrich Corp. (St. Louis, United States). CellicCtec2 enzyme was a generous gift from Novozymes.
Acetonitrile (>99.9%) was purchased from Carlo Erba Reagents (Dasit Group S.p.A, Cornaredo, Italy). 2-methylbutan-2-ol (2M2B, 99%), pentan-1-ol (>99%), lauric acid (99%), methyl laurate (99%), molecular sieves (3 and 5 Å) and the enzyme Novozym 435 (immobilized lipase on acrylic resin from Candida antarctica) were purchased from Sigma-Aldrich Corp. (St. Louis, United States). CellicCtec2 enzyme was a generous gift from Novozymes.
4
Enzymatic Hydrolysis of Pretreated Corn Stover
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CellicCtec2 enzyme (Novozymes, Denmark) was used in the enzymatic hydrolysis of pretreated corn stover. It was purchased from Sigma Aldrich with an activity of 199.7 FPU/mL and protein number of 114.8 mg protein/mL. Pretreated samples (0.5 g dry basis) and citrate buffer (pH 4.8) were mixed in a 1:20 (w/v) ratio and were kept at 200 rpm and 50 °C for 72 h in a shaking incubator. Tetracycline hydrochloride (0.08 g/L) was added and the enzyme loading was 20 FPU/g solid, according to the method of NREL/TP-510-42623 [43 ]. Each sample was measured in duplicates. The glucose and xylose yield were calculated by Eq. (3 ) and (4 ), respectively [44 ]:
5
Alkaline Pretreatment and Enzymatic Hydrolysis of Aspen Wood
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For the alkaline pre-treatment, a 2% aqueous NaOH solution was used in the proportions of 100 cm3 of sodium hydroxide per 5 g of dry aspen wood powder from the fraction of 0.43 mm to 1.02 mm. The alkaline pre-treatment was performed in an autoclave under the following conditions: 121 °C, p = 0.1 MPa, 30 min. Afterward the activated material was subjected to enzymatic hydrolysis according to the procedure described by us previously [30 (link)] with some changes specified below. The hydrolysis Cellic CTec2 enzyme (Novozymes, Krogshoejvej, Denmark) was used and activity was 148 FPU/cm3 determined by the NREL method [31 ]. The enzymatic hydrolysis process was carried out in the Erlenmeyer flasks and the total volume of the mixture was 100 cm3. In the process 50 cm3 of 0.1 M citrate buffer solution at pH = 4. was used and due to the use of yeast in the next step, no sodium azide was added during the hydrolysis. In the hydrolysis process, 3.325 cm3 of 25% (v/v) Cellic CTec2 enzyme solution on each sample was used in the ratio of 1 g of concentrated enzyme to 1 g of absolutely dry biomass. The hydrolysis proceeded in an incubator IKA KS 3000i control (IKA, Warsaw, Poland) with shaking of 150 rpm at 50 °C. The total time of enzymatic hydrolysis was 72 h. After the very process, glucose and xylose concentrations in the supernatant were analyzed by the HPLC method.
6
Enzymatic Hydrolysis of Oil Palm Empty Fruit Bunches
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The oil palm empty fruit bunches (OPEFB) were obtained from Condong Co., Ltd., Garut, West Java, Indonesia. All parts of the OPEFB material were cleaned under running water and then oven dried at 60 °C for 24 h. The dry material was reduced to particle size using a disc mill and then sieved with 60 mesh or 0.25 mm size. After preparation, the material was kept at room temperature in sealed bags until use.
The xylanase and cellulase used in the enzymatic hydrolysis were the Cellic HTec2 enzyme and Cellic CTec2 enzyme (Novozymes, Copenhagen, Denmark) with the activity of 75 IU/mL and 130 FPU/mL, respectively. Debaryomyces hansenii ITBCCR85 was obtained from ITB culture collection (Institut Teknologi Bandung, Bandung, Indonesia), while purified Saccharomyces cerevisiae was obtained from commercial yeast for the bakery. Four ways streaking method was conducted several times to obtain a single cell colony.
All supplemental chemicals obtained from Sigma Aldrich (St. Louis, MO, USA) were aerobicof analytical grade and were utilized directly. An 18.2 MΩ·cm Milli-Q water (Millipore, St. Louis, MO, USA) was used to prepare all solutions.
The xylanase and cellulase used in the enzymatic hydrolysis were the Cellic HTec2 enzyme and Cellic CTec2 enzyme (Novozymes, Copenhagen, Denmark) with the activity of 75 IU/mL and 130 FPU/mL, respectively. Debaryomyces hansenii ITBCCR85 was obtained from ITB culture collection (Institut Teknologi Bandung, Bandung, Indonesia), while purified Saccharomyces cerevisiae was obtained from commercial yeast for the bakery. Four ways streaking method was conducted several times to obtain a single cell colony.
All supplemental chemicals obtained from Sigma Aldrich (St. Louis, MO, USA) were aerobicof analytical grade and were utilized directly. An 18.2 MΩ·cm Milli-Q water (Millipore, St. Louis, MO, USA) was used to prepare all solutions.
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