scholarly journals Catalytical Properties of Free and Immobilized Aspergillus niger Tannase

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Abril Flores-Maltos ◽  
Luis V. Rodríguez-Durán ◽  
Jacqueline Renovato ◽  
Juan C. Contreras ◽  
Raúl Rodríguez ◽  
...  

A fungal tannase was produced, recovered, and immobilized by entrapment in calcium alginate beads. Catalytical properties of the immobilized enzyme were compared with those of the free one. Tannase was produced intracellularly by the xerophilic fungus Aspergillus niger GH1 in a submerged fermentation system. Enzyme was recovered by cell disruption and the crude extract was partially purified. The catalytical properties of free and immobilized tannase were evaluated using tannic acid and methyl gallate as substrates. KM and Vmax values for free enzyme were very similar for both substrates. But, after immobilization, KM and Vmax values increased drastically using tannic acid as substrate. These results indicated that immobilized tannase is a better biocatalyst than free enzyme for applications on liquid systems with high tannin content, such as bioremediation of tannery or olive-mill wastewater.

2003 ◽  
Vol 46 (2) ◽  
pp. 167-176 ◽  
Author(s):  
Gargi Dey ◽  
Singh Bhupinder ◽  
Rintu Banerjee

A maltooligosaccharide-forming amylase from B circulans GRS 313 was immobilized by entrapment in calcium alginate beads. The immobilized activity was affected by the size of the bead and bead size of 2mm was found to be most effective for hydrolysis. Kinetics constants, Km and Vmax were estimated and were found to be affected by the bead size. The catalytic activity of the enzyme was studied in presence of various starchy residues and metal ions. HgCl2, CuSO4 and FeCl3 caused inhibition of the enzyme. The reaction conditions, pH and temperature, was optimized using response surface methodology. At the optimum pH and temperature of 4.9 and 57ºC, the apparent activity was 25.6U/g of beads, resulting in almost 2-fold increase in activity. The immobilized enzyme showed a high operational stability by retaining almost 85% of the initial activity after seventh use.


2005 ◽  
Vol 21 (4) ◽  
pp. 609-614 ◽  
Author(s):  
H. Aissam ◽  
F. Errachidi ◽  
M. J. Penninckx ◽  
M. Merzouki ◽  
M. Benlemlih

2013 ◽  
Vol 05 (08) ◽  
pp. 768-774 ◽  
Author(s):  
Fatiha Hanafi ◽  
Mohammed Mountadar ◽  
Samira Etahiri ◽  
Mohamed Fekhaoui ◽  
Omar Assobhei

2000 ◽  
Vol 35 (8) ◽  
pp. 751-758 ◽  
Author(s):  
I. Garcı́a Garcı́a ◽  
P.R. Jiménez Peña ◽  
J.L. Bonilla Venceslada ◽  
A. Martı́n Martı́n ◽  
M.A. Martı́n Santos ◽  
...  

2020 ◽  
Author(s):  
Ian Mallov ◽  
Fiona Jeeva ◽  
Chris Caputo

Food is often wasted due to real or perceived concerns about preservation and shelf life. Thus, precise, accurate and consumer-friendly methods of indicating whether food is safe for consumers are drawing great interest. The colorimetric sensing of biogenic amines released as food degrades is a potential way of determining the quality of the food. Herein, we report the use of genipin, a naturally occurring iridoid, as a dual colorimetric sensor for both oxygen and biogenic amines. Immobilization of genipin in edible calcium alginate beads demonstrates that it is a capable sensor for amine vapors and can be immobilized in a non-toxic, food-friendly matrix.


1987 ◽  
Vol 19 (1-2) ◽  
pp. 175-182 ◽  
Author(s):  
Z. Lewandowski ◽  
R. Bakke ◽  
W. G. Characklis

Immobilization of nitrifiers and autotrophic denitrifiers (Thiobacillus denitrificans) within calcium alginate gel was demonstrated. Calcium carbonate reagent was immobilized along with bacteria as the stabilizing agent. Protons released as a result of microbial respiration reacted with calcium carbonate producing calcium ions which internally stabilized the calcium alginate gel. The microbially active gel beads were mechanically stable and active for three months in a continuous flow system without addition of calcium.


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.


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