scholarly journals Perspectives and applications of immobilised β-galactosidase in food industry – a review

2008 ◽  
Vol 26 (No. 1) ◽  
pp. 1-14 ◽  
Author(s):  
Z. Grosová ◽  
M. Rosenberg ◽  
M. Rebroš

β-Galactosidase is an important industrial enzyme in the hydrolysis of milk and whey lactose. The enzymatic hydrolysis of lactose allows to avoid health and environmental problems posed by this disaccharide. In addition, this enzyme catalyses the formation of galacto-oligosaccharides, which are prebiotic additives for the so-called “healthy foods”. β-Galactosidase is one of the relatively few enzymes that have been used in large-scale processes in both free and immobilised forms. This article presents a review of recent trends in immobilisation of β-galactosidase and their application in food industry.

2011 ◽  
Vol 5 (6) ◽  
pp. 609-620 ◽  
Author(s):  
S. Di Risio ◽  
C. S. Hu ◽  
B. A. Saville ◽  
D. Liao ◽  
J. Lortie

1992 ◽  
Vol 42 (3) ◽  
pp. 197-204 ◽  
Author(s):  
M. Ropars ◽  
R. Marchal ◽  
J. Pourquié ◽  
J.P. Vandecasteele

Author(s):  
Joni Agustian ◽  
Lilis Hermida

Enzymatic hydrolysis of starches using free glucoamylase to reducing sugars have difficulties in recovering and recycling of the enzyme, hence immobilisation on inert supports were widely studied. However, effectiveness of the immobilised glucoamylase were merely observed only on soluble starches. It was considered a valuable thing to know performance of glucoamylase on Mesostructured Cellular Foam (MCF) silica in hydrolysing of tapioca. An optimised study on enzymatic hydrolysis of tapioca using glucoamylase on MCF silica (9.2T-3D) and its kinetics were described including justification of the predicted model as it was required to develop in large scale operations. Central Composite Design was used to model the process by studying effects of three factors on DE values after enzyme immobilisation.  Immobilisation of glucoamylase on this support gave up to 82% efficiency with the specific activity of 1,856.78 U.g-1. Its used to hydrolysis of tapioca resulted DE values of 1.740-76.303% (w/w) where the highest DE was obtained at pH of 4.1, temperature of 70 ℃ and agitation speed of 140 rpm. The optimisation produced a polynomial quadratic model having insignificant lack-of-fit and low standard deviation, so that it was applicable and reliable in simulating the DE with only 0.80% of data were not described. Temperature affected the process highly, but the buffer pH, agitation speed and factorial interactions were considered not important. KM value for immobilised enzyme was better than the free glucoamylase, however, its reaction rate was slower than the free glucoamylase catalysis. Copyright © 2019 BCREC Group. All rights reserved 


1992 ◽  
Vol 42 (3) ◽  
pp. 205-217 ◽  
Author(s):  
R. Marchal ◽  
M. Ropars ◽  
J. Pourquié ◽  
F. Fayolle ◽  
J.P. Vandecasteele

Lignocellulosic biomass is one of the largest carbohydrate sources and has huge potential for biofuels production. However, the problem with lignocellulosic feedstock is that it has useful sugars locked in by lignin, hemicellulose, and cellulose. Some kind of pretreatment; therefore is needed to make carbohydrate accessible which later can be fermented to produce ethanol. The results from this research indicated that the yields of glucan (93%) and xylan (82.8%) were improved by using milling combined with ELLA pretreatment. The optimal enzymatic hydrolysis efficiencies were obtained under 10 min for ball milling time, pretreatment at 1 h, temperature at 150°C, S/L = 0.5 and ammonia loading at 0.25 g-NH3/g-biomass. This method reduced the pretreatment time and short milling time and thus has potential of reducing the energy consumption and promising the application in the large scale.


Author(s):  
Marcin Lukasiewicz ◽  
Anna Osowiec ◽  
Magdalena Marciniak

2018 ◽  
Author(s):  
Ángel Batallas ◽  
Erenio González ◽  
Carmen Salvador ◽  
Jonathan Villavicencio ◽  
Humberto González Gavilánez ◽  
...  

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