Mannooligosaccharide production by β‐mannanase enzyme application from coffee extract

Author(s):  
Selime Benemir Erkan ◽  
Selin Basmak ◽  
Ali Ozcan ◽  
Cansu Yılmazer ◽  
Hilal Nur Gürler ◽  
...  
Keyword(s):  
TAPPI Journal ◽  
2009 ◽  
Vol 8 (5) ◽  
pp. 19-25 ◽  
Author(s):  
PETER W. HART ◽  
DARRELL M. WAITE ◽  
LUC THIBAULT, ◽  
JOHN TOMASHEK ◽  
MARIE-EVE ROUSSEAU ◽  
...  

Eucalyptus wood chips were subjected to impregnation with various blends of novel fiber modify-ing enzymes before chemical pretreatment and two stages of refining using the preconditioning refiner chemical–alkaline peroxide mechanical pulping (PRC-APMP) process. Wood chip impregnation and pulp processing was con-ducted at a pilot plant in the United States. When compared under constant chemical application and at a constant 350 mL CSF, enzyme treatment reduced specific refining energy by at least 24%. The effect of one versus two stages of impregnation and of enzyme action upon several physical pulp properties was determined.


2018 ◽  
pp. 138-146 ◽  
Author(s):  
Karin Abraham ◽  
Eckhard Flöter

The presence of polysaccharides in cane and beet raw juices causes several negative effects during the sugar manufacture. These are usually mitigated by enzymatic decomposition of dextrans. Such effects not only depend on the content, but also on the molecular mass distribution. This means that the different dextran fractions specifically affect the process. An accurate process control hence requires the most precise knowledge about the existing content and the molecular mass distribution present. A detailed understanding of the specific processing problems and also a targeted enzyme application hence requires the determination of a total dextran content and also its characterization including the differentiation between the different dextran fractions. An accurate analytical tool which equally satisfies industrial applicability is still lacking. To improve on this situation, two new approaches for the determination of dextran were developed and benchmarked against the commonly used and established Haze Method, which is rather inaccurate and also sensitive to molecular mass variation. The two new approaches are both based on polarimetry. These two methods indicate to be superior over the Haze Method with respect two molecular mass variation and hence enable the determination of a broader molecular size range including also low molecular mass dextrans.


2015 ◽  
Vol 10 (5) ◽  
pp. 226-236 ◽  
Author(s):  
N.E. El-Bordeny ◽  
A.A. Abedo ◽  
H.M. El-Sayed ◽  
E.N. Daoud ◽  
H.S. Soliman ◽  
...  

BioResources ◽  
2015 ◽  
Vol 10 (3) ◽  
Author(s):  
Mohammad Ali Hossein ◽  
Mohammad Talaeipour ◽  
AmirHooman Hemmasi ◽  
Behzad Bazyar ◽  
Saeed Mahdavi

2011 ◽  
Vol 25 (1) ◽  
pp. 66-74 ◽  
Author(s):  
Y. Wang ◽  
J. E. Ramirez-Bribiesca ◽  
L. J. Yanke ◽  
A. Tsang ◽  
T. A. McAllister

1987 ◽  
Vol 65 (6) ◽  
pp. 1220-1225 ◽  
Author(s):  
C. L. Schauf

The effects of pronase and the anticonvulsant drugs diphenylhydantoin, bepridil, and sodium valproate on fast and slow Na+ inactivation were examined in cut-open Myxicola giant axons with loose patch-clamp electrodes applied to the internal surface. Pronase completely eliminated fast Na+ inactivation without affecting the kinetics of Na+ activation or the maximum Na+ conductance. The time and voltage dependences of slow inactivation following pronase treatment were identical to those measured before enzyme application in the same axons. All three anticonvulsants slowed the time course of recovery from fast Na+ inactivation in untreated axons, and shifted the steady-state fast inactivation curve in the hyperpolarizing direction along the voltage axis. Anticonvulsants enhanced steady-state slow inactivation and retarded recovery from slow inactivation in both untreated and pronase-treated axons. Although some quantitative differences were seen, the order of potency of the anticonvulsants on slow Na+ inactivation was the same as that for recovery from fast inactivation.


2017 ◽  
Vol 2017 ◽  
pp. 1-18 ◽  
Author(s):  
D. F. Silva ◽  
A. F. A. Carvalho ◽  
T. Y. Shinya ◽  
G. S. Mazali ◽  
R. D. Herculano ◽  
...  

The immobilization of cellulases could be an economical alternative for cost reduction of enzyme application. The derivatives obtained in the immobilization derivatives were evaluated in recycles of paper filter hydrolysis. The immobilization process showed that the enzyme recycles were influenced by the shape (drop or sheet) and type of the mixture. The enzyme was recycled 28 times for sheets E′ and 13 times for drops B′. The derivative E′ showed the highest stability in the recycle obtaining 0.05 FPU/g, RA of 10%, and FPU Yield of 1.64 times, higher than FPU spent or Net FPU Yield of 5.3 times, saving more active enzymes. The derivative B showed stability in recycles reaching 0.15 FPU/g of derivative, yield of Recovered Activity (RA) of 25%, and FPU Yield of 1.57 times, higher than FPU spent on immobilization or Net PFU Yield of 2.81 times. The latex increased stability and resistance of the drops but did not improve the FPU/gram of derivative.


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