Screening of highly cellulolytic fungi and the action of their cellulase enzyme systems

1982 ◽  
Vol 4 (6) ◽  
pp. 414-418 ◽  
Author(s):  
J.N. Saddler
2021 ◽  
Vol 50 (4) ◽  
pp. 487
Author(s):  
S. K. Jayasekara ◽  
K. B. M. D. K. Karunarathna ◽  
K. L. W. Kumara ◽  
R. R. Ratnayake

2019 ◽  
Vol 73 (6) ◽  
pp. 550-553
Author(s):  
Kota Yoshimura ◽  
Masanobu Hatano

2019 ◽  
pp. 1-3
Author(s):  
Madhuri B ◽  
Narasimha G ◽  
Balaji M*

Areca palm (ChrysalidoCarpus lutescenes) a widely used plant having feathery arching brands with 100 leaflets. All these plants produce much of waste in additions to greeny and nuts. This waste of spade is used for the production of various molecules that are used in industry and pharma sector. Fermentation techniques are used to generate economically important enzymes for industrial and pharmaceutical purposes. Cellulase enzyme degrades the cellulose in between β-1, 4 glucosidic link found in lignocellulosic complex which under physical treatment is slower to degrade. The present study of Aspergillus niger for cellulose production was carried in solid state (SS) and submerged (SM) fermentations for production of cellulase enzyme. Cellulase production in SSF after 72 h of fermentation was 8.02 and in SMF activity was 2.98 per ml of cultured broth at H 6 and temperature at 30°C. Both SMF and SSF were supplemented with lactose and lactobionic acid, which acted as cellulase P production inducers. The aim of the present work was to study the effect of Areca palm spade as substrate for Aspergillus niger and its cellulase production under SMF and SSF.


2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai

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.


1962 ◽  
Vol 39 (1) ◽  
pp. 22-31 ◽  
Author(s):  
A. Vermeulen ◽  
J. Ferin

ABSTRACT The effect of prolonged 17α-methyl-nortestosterone (M. N. T.) administration on cortisol metabolism was studied in several patients. 1. A decreased urinary excretion of 17-hydroxycorticosteroids occurred regularly. 2. Chromatographic analysis of the urinary corticoids revealed that the decreased urinary excretion involved exclusively cortisol metabolites, whereas corticosterone metabolites were excreted at normal levels. This chromatographic study moreover showed an impairment in the conjugation of tetrahydrocorticoids. 3. Studies with 4-14C-cortisol in MNT treated patients showed increased transcortin levels, a normal cortisol pool, a reduced cortisol inactivation rate and a decreased cortisol production. 4. From these results it is concluded that the decreased 17-hydroxycorticoid excretion reflects a decreased cortisol production, at least partly secondary to a reduced cortisol-inactivation rate, which itself must be attributable either to an inhibition or a defect in the liver enzyme systems concerned in corticoid-inactivation.


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