scholarly journals Survival of Bifidobacterium longumImmobilized in Calcium Alginate Beads in Simulated Gastric Juices and Bile Salt Solution

2000 ◽  
Vol 66 (2) ◽  
pp. 869-873 ◽  
Author(s):  
Ki-Yong Lee ◽  
Tae-Ryeon Heo

ABSTRACT Bifidobacterium longum KCTC 3128 and HLC 3742 were independently immobilized (entrapped) in calcium alginate beads containing 2, 3, and 4% sodium alginate. When the bifidobacteria entrapped in calcium alginate beads were exposed to simulated gastric juices and a bile salt solution, the death rate of the cells in the beads decreased proportionally with an increase in both the alginate gel concentration and bead size. The initial cell numbers in the beads affected the numbers of survivors after exposure to these solutions; however, the death rates of the viable cells were not affected. Accordingly, a mathematical model was formulated which expressed the influences of several parameters (gel concentration, bead size, and initial cell numbers) on the survival of entrapped bifidobacteria after sequential exposure to simulated gastric juices followed by a bile salt solution. The model proposed in this paper may be useful for estimating the survival of bifidobacteria in beads and establishing optimal entrapment conditions.

2014 ◽  
Vol 2014 ◽  
pp. 1-5 ◽  
Author(s):  
Gulnur Arabaci ◽  
Ayse Usluoglu

Water pollution due to release of industrial wastewater has already become a serious problem in almost every industry using dyes to color its products. In this work, polyphenol oxidase enzyme from quince (Cydonia Oblonga) leaves immobilized on calcium alginate beads was used for the successful and effective decolorization of textile industrial effluent. Polyphenol oxidase (PPO) enzyme was extracted from quince (Cydonia Oblonga) leaves and immobilized on calcium alginate beads. The kinetic properties of free and immobilized PPO were determined. Quince leaf PPO enzyme stability was increased after immobilization. The immobilized and free enzymes were employed for the decolorization of textile dyes. The dye solutions were prepared in the concentration of 100 mg/L in distilled water and incubated with free and immobilized quince (Cydonia Oblonga) leaf PPO for one hour. The percent decolorization was calculated by taking untreated dye solution. Immobilized PPO was significantly more effective in decolorizing the dyes as compared to free enzyme. Our results showed that the immobilized quince leaf PPO enzyme could be efficiently used for the removal of synthetic dyes from industrial effluents.


PLoS ONE ◽  
2016 ◽  
Vol 11 (4) ◽  
pp. e0153685 ◽  
Author(s):  
Shen-Fu Lin ◽  
Ying-Chen Chen ◽  
Ray-Neng Chen ◽  
Ling-Chun Chen ◽  
Hsiu-O Ho ◽  
...  

2017 ◽  
Vol 324 ◽  
pp. 358-369 ◽  
Author(s):  
Gabriel Salierno ◽  
Mauricio Maestri ◽  
Stella Piovano ◽  
Miryan Cassanello ◽  
María Angélica Cardona ◽  
...  

Biomaterials ◽  
2005 ◽  
Vol 26 (16) ◽  
pp. 3327-3331 ◽  
Author(s):  
Shinji Sugiura ◽  
Tatsuya Oda ◽  
Yasuhiko Izumida ◽  
Yasuyuki Aoyagi ◽  
Mitsuo Satake ◽  
...  

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.


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