Hydrolysis of cellulose by a mixture of Trichoderma reesei cellobiohydrolase and Aspergillus niger endoglucanase

1988 ◽  
Vol 967 (3) ◽  
pp. 437-440 ◽  
Author(s):  
Norman E. Lee ◽  
Marybeth Lima ◽  
Jonathan Woodward
Keyword(s):  
Aspergillus Niger ◽  
Trichoderma Reesei ◽  
Hydrolysis Of Cellulose ◽  
Hydrolysis Of

scholarly journals Production of Recombinant Trichoderma reesei Cellobiohydrolase II in a New Expression System Based on Wickerhamomyces anomalus

2017 ◽  
Vol 2017 ◽  
pp. 1-8 ◽  
Author(s):  
Dennis J. Díaz-Rincón ◽  
Ivonne Duque ◽  
Erika Osorio ◽  
Alexander Rodríguez-López ◽  
Angela Espejo-Mojica ◽  
...  
Keyword(s):  
Trichoderma Reesei ◽  
Recombinant Expression ◽  
Expression System ◽  
Enzymatic Extract ◽  
Native Strain ◽  
Wickerhamomyces Anomalus ◽  
Optimum Ph ◽  
Hydrolysis Of Cellulose ◽  
Cellobiohydrolase Ii ◽  
Hydrolysis Of

Cellulase is a family of at least three groups of enzymes that participate in the sequential hydrolysis of cellulose. Recombinant expression of cellulases might allow reducing their production times and increasing the low proteins concentrations obtained with filamentous fungi. In this study, we describe the production of Trichoderma reesei cellobiohydrolase II (CBHII) in a native strain of Wickerhamomyces anomalus. Recombinant CBHII was expressed in W. anomalus 54-A reaching enzyme activity values of up to 14.5 U L−1. The enzyme extract showed optimum pH and temperature of 5.0–6.0 and 40°C, respectively. Enzyme kinetic parameters (KM of 2.73 mM and Vmax of 23.1 µM min−1) were between the ranges of values reported for other CBHII enzymes. Finally, the results showed that an enzymatic extract of W. anomalus 54-A carrying the recombinant T. reesei CBHII allows production of reducing sugars similar to that of a crude extract from cellulolytic fungi. These results show the first report on the use of W. anomalus as a host to produce recombinant proteins. In addition, recombinant T. reesei CBHII enzyme could potentially be used in the degradation of lignocellulosic residues to produce bioethanol, based on its pH and temperature activity profile.

scholarly journals KINERJA MIKROBA Zymomonas mobilis DAN Saccharomyces cerevisiae UNTUK MENGURAIKAN HIDROLISAT TONGKOL JAGUNG MENJADI BIOETANOL DENGAN PENGARUH WAKTU FERMENTASI DAN RASIO PENAMBAHAN MIKROBA

2017 ◽  
Vol 6 (2) ◽  
pp. 1-6
Author(s):  
Fatimah ◽  
Deralisa Ginting ◽  
Veronica Sirait
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Gas Chromatography ◽  
Aspergillus Niger ◽  
Trichoderma Reesei ◽  
Zymomonas Mobilis ◽  
Alternative Fuel ◽  
Fermentation Time ◽  
Corn Cobs ◽  
Hydrolysis Of ◽  
Bioethanol Yield

Bioethanol from biomass is one of energy which  has a  potential as  alternative fuel. Bioethanol can be produced by using fungi or bacteria. The research was about  the performance of Zymomonas mobilis and Saccharomyces cerevisiae to change corn cobs hydrolyzate into bioethanol by adding microbes to the influence of time and ratio of  fermentation had been done. The hydrolyzate  were decomposition of corn cobs using Trichoderma reesei and Aspergillus niger. The purpose of this study was to know the conversion of  hydrolysis of corn cobs into bioethanol with variation time of fermentation (1 day, 3 days, 5 days, and 7 days) and rate of adding microbes  (Zymomonas mobilis : Saccharomyces cerevisiae = 1:1; 1:2 and 2:1) (v/v). The glucose from corn cobs hydrolyzate was 5,869 g/ml. Fermentation wass carried out at 25 0C. Bioethanol which obtained from this study was investigated using gas chromatography. The optimum bioethanol yield was equal to 6,31% by using Zymomonas mobilis : Saccharomyces cerevisiae (2:1) and at the 3 days  fermentation time.

scholarly journals Microbial oil production byMortierella isabellinafrom corn stover under different pretreatments

RSC Advances ◽  
2017 ◽  
Vol 7 (89) ◽  
pp. 56239-56246 ◽  
Author(s):  
Chen Zhao ◽  
Lu Deng ◽  
Hao Fang ◽  
Shaolin Chen
Keyword(s):  
Enzymatic Hydrolysis ◽  
Aspergillus Niger ◽  
Mixed Culture ◽  
Corn Stover ◽  
Trichoderma Reesei ◽  
Oil Production ◽  
Cellulase Production ◽  
Microbial Oil ◽  
Pretreated Corn Stover ◽  
Hydrolysis Of

Mixed culture ofTrichoderma reeseiandAspergillus nigerwas employed to accomplish on-site cellulase production where cellulases were applied directly to the enzymatic hydrolysis of pretreated corn stover.

scholarly journals Hydrolysis of Cellulose from Oil Palm Empty Fruit Bunch using Aspergillus niger

2021 ◽  
Vol 226 ◽  
pp. 00042
Author(s):  
Sri Sugiwati ◽  
Suaidah Suaidah ◽  
Eka Triwahyuni ◽  
Muryanto Muryanto ◽  
Yosie Andriani ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Oil Palm ◽  
Hydrolytic Activity ◽  
Reducing Sugar ◽  
Empty Fruit Bunch ◽  
Hydrolysis Time ◽  
Glucose Assay ◽  
Optimum Ph ◽  
Hydrolysis Of Cellulose ◽  
Hydrolysis Of

Oil palm empty fruit bunch (OPEFB) constitutes a great source of lignocellulosic biomass, mainly comprising of 66.97 % of holocellulose (cellulose and hemicellulose) and 24.45 % of lignin. This present work aimed to hydrolyze cellulose present in OPEFB to form glucose with the aid of Aspergillus niger. A. niger is a type of filamentous fungi able to produce cellulase, a multi-enzyme complex consisting of an endoglucanase, exoglucanase, and β-glucosidase, able to converting cellulose into glucose. The glucose produced is then fermented to produce bioethanol. The present study compared hydrolytic activity of cellulose between OPEFB with pretreatment using NaOH 10 % and OPEFB without pretreatment, concerning temperature, pH, and hydrolysis time. The concentration of reducing sugar derived from cellulosic hydrolysis was determined by using a glucose assay of 3.5-dinitrosalicylic acid. The results showed that the optimum temperature for hydrolysis of cellulose OPEFB (pretreated and untreated) was at 40 °C and the optimum pH was 5.0 for OPEFB-untreated and 5.5 for OPEFB-pretreated. Hydrolysis of cellulose at 40 °C and 3 d yielded reducing sugar 13.01 mg mL−1 and 1.16 mg mL−1 for OPEFB-untreated and OPEFB-pretreated, respectively.

scholarly journals Cellobiohydrolase from Trichoderma reesei

1983 ◽  
Vol 215 (3) ◽  
pp. 677-683 ◽  
Author(s):  
M Nummi ◽  
M L Niku-Paavola ◽  
A Lappalainen ◽  
T M Enari ◽  
V Raunio
Keyword(s):  
Trichoderma Reesei ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Culture Liquid ◽  
Protein Band ◽  
Immunoaffinity Chromatography ◽  
Amorphous Cellulose ◽  
Single Protein ◽  
Hydrolysis Of Cellulose ◽  
Hydrolysis Of

A 1,4-beta-D-glucan cellobiohydrolase (EC 3.2.1.91) was purified from the culture liquid of Trichoderma reesei by using biospecific sorption on amorphous cellulose and immunoaffinity chromatography. A single protein band in polyacrylamide-gel electrophoresis and one arc in immunoelectrophoresis corresponded to the enzyme activity. The Mr was 65 000. The pI was 4.2-3.6. The purified enzyme contained about 10% hexose. The enzyme differs from previously described cellobiohydrolases in being more effective in the hydrolysis of cellulose.

Immobilized Nanoparticles-Mediated Enzymatic Hydrolysis of Cellulose for Clean Sugar Production: A Novel Approach

2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai
Keyword(s):  
Catalytic Activity ◽  
Enzymatic Hydrolysis ◽  
Immobilized Enzyme ◽  
Free Enzyme ◽  
Magnetic Nanomaterials ◽  
Sugar Production ◽  
Cellulase Enzyme ◽  
Enzymatic Hydrolysis Of Cellulose ◽  
Hydrolysis Of Cellulose ◽  
Hydrolysis Of

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.

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