Oxidation of lactose to lactobionic acid by a Microdochium nivale carbohydrate oxidase: Kinetics and operational stability

2006 ◽  
Vol 97 (4) ◽  
pp. 694-707 ◽  
Author(s):  
Mikkel Nordkvist ◽  
Per Munk Nielsen ◽  
John Villadsen
The Analyst ◽  
2000 ◽  
Vol 125 (9) ◽  
pp. 1587-1590 ◽  
Author(s):  
Juozas Kulys ◽  
Lidija Tetianec ◽  
Palle Schneider

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.


1982 ◽  
Vol 47 (10) ◽  
pp. 2716-2723 ◽  
Author(s):  
Lubomíra Rexová-Benková ◽  
Jiřina Omelková ◽  
Vladimír Kubánek

Endo-D-galacturonanase of Aspergillus sp. was irreversibly adsorbed on polyethyleneterephthalate in an acetate 0.1 mol l-1 buffer solution of pH 4.2. Immobilization of the enzyme resulted in lowering of its activity, the measure of which depended on the amount of the enzyme fixed on the carrier. The highest relative activity (42.4%) had the preparation containing 5.25 mg of the enzyme per 1 g of the carrier. The velocity and intensity of the sorption of the enzyme depended on the ionic strength of the medium, whilst pH, on the other hand, was of no influence. Endo-D-galacturonanase immobilized in a 0.1 mol l-1 buffer was characteristic a) of its fixation strength in salt solutions of various ionic strength and pH, in a 3 mol l-1 guanidine solution, and also in sodium pectate and pectin solutions, b) of its high stability during a long-lasting storage at 4 °C, c) of its operational stability. The immobilization led to a partial change of the action pattern onto the high-molecular substrate, manifested in lowering the decrease of viscosity to degradation degree ratio.


2014 ◽  
Vol 99 (1) ◽  
pp. 189-199 ◽  
Author(s):  
Jo De Vrieze ◽  
Sylvia Gildemyn ◽  
Ramiro Vilchez-Vargas ◽  
Ruy Jáuregui ◽  
Dietmar H. Pieper ◽  
...  

2021 ◽  
Vol 412 ◽  
pp. 128680
Author(s):  
Wenxiao Zhang ◽  
Xiaodong Li ◽  
Xiuxiu Feng ◽  
Xiaoyan Zhao ◽  
Junfeng Fang

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