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Cellulase

About: Cellulase is a research topic. Over the lifetime, 16172 publications have been published within this topic receiving 479592 citations. The topic is also known as: cellulase.


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Book ChapterDOI
TL;DR: This chapter discusses an alternative method for purifying a carboxymethylcellulase from the fungus Sclerotium rolfsii using a modification of the improved Somogyi–Nelson method.
Abstract: Publisher Summary Carboxymethylcellulases are predominantly endoglucanases able to catalyze the hydrolysis of glycosidic bonds in the soluble, substituted cellulose, carboxymethylcellulose (CMC). These enzymes, formerly called C x , are important components of the cellulase complex that catalyzes the degradation of crystalline cellulose. This chapter discusses an alternative method for purifying a carboxymethylcellulase from the fungus Sclerotium rolfsii . During hydrolysis of CMC, reducing sugars are generated. Timed samples are withdrawn from the reaction mixture and assayed for reducing sugar using a modification of the improved Somogyi–Nelson method. Samples assayed in this way are used to construct a linear progress curve for the measurement of initial velocity.

6 citations

Journal Article
TL;DR: A positive relation between phenol oxidase activity, lign in degradation on lignin agar plate and growth on paddy straw was evident.
Abstract: Fresh dung, dung cakes, decomposed straw and rice husk were collected in polythene bags, distilled water was sprinkled to bring the moisture level to 50% and the material exposed to atmospheric temperature (16-20°C). The fruiting bodies of the fungus developed in a week’s time and these fungi were isolated by spore drop, direct streak and tissue culture methods. The qualitative screening of the various fungi was done by determining the cellulase and the phenol oxidase activities. The lignin degradation activity was determined on lignin agar plates. Growth studies were done using CMC as a sole source of carbon. Twelve fungi belonging to the genera Coprinus, Aspergillus, Panaeolus, Eupenicillium, Cladosporium and Fusarium were collected. One of the isolates was identified as Actinomycete. The lignin degradation was highest (37.62%) in case of Cladosporium followed by Actinomycete (34.21%) and Fusarium (31.28%). Other isolates showed a low lignin degradation in a range of 2.86% (Aspergillus) to 18.57% (Eupenicillium). Cellulose azure activity was also highest (0.349 OD) in case of Coprinus cinereus which showed 11.27% lignin degradation. All the isolates were positive for phenol oxidase activity except Eupenicillium, Aspergillus and Actinomycete. The biomass on CMC broth was more in case of Aspergillus (79. 30 mg) followed by Cladosporium (78.00 mg), Panaeolus (77.00 mg) and Coprinus cinereus (53.00 mg). These fungi manifested growth on paddy straw. A positive relation between phenol oxidase activity, lignin degradation on lignin agar plate and growth on paddy straw was evident.

6 citations

Journal ArticleDOI
TL;DR: Pre-treatment milling of paper proved to effectively increase the sugar formation under all incubation conditions and Pretreated foolscap paper was the most susceptible substrate with maximum bioconversion when exposed to both forms of successive cellulase treatment.

6 citations

Journal Article
Hanlin Chen1, J Zhu, Gemei Liang, Z Yan, S Zhang 
TL;DR: From 150 fungal strains, the authors found 8 strains contained mainly of xylan enzyme activity over 100 U/mL in which the No. 149 strain was the highest xylanase producer, tentatively identified as Aspergillas niger.
Abstract: From 150 fungal strains, the authors found 8 strains contained mainly of xylanase activity over 100 U/mL in which the No 149 strain was the highest xylanase producer Which tentatively identified as Aspergillas niger The appropriate medium composition was as follows: wheat bran hemicellulose 4%; NaNO3 1%; wheat bran 1% prepared in Mandels nutritional solution without (NH4)2SO4 and urea After cultivated in shake-flask at 28 degrees C-32 degrees C for 60 h, the activity reached the highest value of 3572 U/mL The optimum pH of xylanase was 46 and it was stable at pH3-11 The fermented broth of strain 149 contained in addition to xylanase (relative activity 100) also included amylase(18), mannanase(098), beta-xylosidase(094) and cellulase(017)

6 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023549
20221,155
2021574
2020650
2019681
2018716