form
liquid
specific activity
≥250 units/g
greener alternative product characteristics
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greener alternative category
storage temp.
2-8°C
General description
Cellobiase enzyme preparation obtained by submerged fermentation of an Aspergillus niger microorganism. The cellobiase hydrolyzes cellobiose to glucose.
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for waste prevention when used in cellulosic ethanol research. For more information see the article in biofiles.
Application
Cellobiase from Aspergillus niger has been used in a study to assess the targeted antifungal delivery system of a β-Glucosidase sensitive nystatin–star poly(ethylene glycol) conjugate. Cellobiase from Aspergillus niger has also been used in a study to investigate the influence of substrate particle size and wet oxidation on physical surface structures and enzymatic hydrolysis of wheat straw.
Legal Information
A product of Novozyme Corp.
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Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
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Jonathan R Mielenz et al.
Bioresource technology, 100(14), 3532-3539 (2009-03-31)
Soybean hulls were evaluated as a resource for production of ethanol by the simultaneous saccharification and fermentation (SSF) process, and no pretreatment of the hulls was found to be needed to realize high ethanol yields with Saccharomyces cerevisiae D(5)A. The
Jan Eric Jessen et al.
Journal of biomedicine & biotechnology, 2012, 186982-186982 (2012-11-03)
Thermophilic bacteria have gained increased attention as candidates for bioethanol production from lignocellulosic biomass. This study investigated ethanol production by Thermoanaerobacter strain J1 from hydrolysates made from lignocellulosic biomass in batch cultures. The effect of increased initial glucose concentration and
Jürgen Jalak et al.
PloS one, 9(9), e108181-e108181 (2014-09-30)
Enzymatic hydrolysis of recalcitrant polysaccharides like cellulose takes place on the solid-liquid interface. Therefore the adsorption of enzymes to the solid surface is a pre-requisite for catalysis. Here we used enzymatic activity measurements with fluorescent model-substrate 4-methyl-umbelliferyl-β-D-lactoside for sensitive monitoring