immobilization enzyme
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2020 ◽  
Vol 1615 ◽  
pp. 460711 ◽  
Author(s):  
Jia Liu ◽  
Run-Tian Ma ◽  
Yan-Ping Shi


2020 ◽  
Vol 27 (9) ◽  
pp. 9979-9986 ◽  
Author(s):  
Song Li ◽  
Xiangyang Sun ◽  
Yuanxin Liu ◽  
Suyan Li ◽  
Wenjie Zhou ◽  
...  


Author(s):  
Yu. Golovin ◽  
F. Secundo ◽  
N. Klyachko

PAMO was immobilized onto Ni-NTA modified hybrid magnetite-gold nanoparticles through polyhistidinemotife. As a result of immobilization, enzyme has become fully inactive. Under the expose to 50 Hz 100 mT magnetic field,catalyzed by enzyme reaction rate increases 1,5 times due to PAMO desorption from nanoparticles.



Author(s):  
Wanderley Pereira Oliveira ◽  
Tales Alexandre Costa-Silva ◽  
Ana Karine Furtado Carvalho ◽  
Claudia Regina Fernandes Souza ◽  
Larissa De Freitas ◽  
...  

Candida rugosa lipase (LCR) was immobilized on low-cost supports (by-products) and dried using a spouted-bed system. The yields of immobilized derivatives were in the range 61.5–78.7%. Lipase immobilized on rice husk showed the best results, presenting 94.1% of the original activity, followed by sugarcane bagasse (90.3%) and green coconut fiber (87.3%). Moisture content in the obtained powders varied between 4.7 and 5.6% and the water activities were in the range 0.21–0.35. Among all the tested biocatalysts for aroma production the lipase immobilized on rice husk showed the highest activity towards the formation of isoamyl caprylate (62.40 g.L-1). Keywords: Spouted bed dryer; Enzyme dehydration; Enzyme immobilization; Enzyme stabilization; Aroma production. 



2018 ◽  
Vol 91 ◽  
pp. 793-801 ◽  
Author(s):  
Yingli Hu ◽  
Lingmei Dai ◽  
Dehua Liu ◽  
Wei Du ◽  
Yujun Wang


2018 ◽  
Vol 101 (2) ◽  
pp. 243-249 ◽  
Author(s):  
Shiping Shan ◽  
Zhaohui Guo ◽  
Ping Lei ◽  
Wei Cheng ◽  
Minxi Wu ◽  
...  


2017 ◽  
Vol 184 (2) ◽  
pp. 453-470 ◽  
Author(s):  
Hua Hang ◽  
Changbao Wang ◽  
Yiqun Cheng ◽  
Ning Li ◽  
Liuli Song


2016 ◽  
Vol 4 (35) ◽  
pp. 5873-5882 ◽  
Author(s):  
Jiayi Song ◽  
Ping Su ◽  
Ye Yang ◽  
Ting Wang ◽  
Yi Yang

A novel enzyme immobilization procedure was developed. The immobilized enzyme composites exhibited significantly improved digestion performance, excellent reusability, stability and dynamic reversible reproducibility.



2015 ◽  
Vol 5 (1) ◽  
pp. 79
Author(s):  
Upita Septiani ◽  
Agrina Lisma

 ABSTRACT The utilization of natural zeolite as supporting media of α-amylase enzyme has been done. Natural zeolite which is activated with 3M HCl can remove impurities in the surface natural zeolite, uncover and widen the pores of the zeolite and activate functional groups to interact with α-amylase enzyme in the process of immobilization enzyme process. The mass of activated natural zeolite which is used as a material immobilized to get the optimal activity of α-amylase enzyme was 0.3 gram. Based on the measurement result of optimization of α-amylase enzyme were obtained optimum temperature of 35 oC, pH 5.6 and incubation time of 35 minutes with 0.04845 units/mL of the unit activity. And for α-amylase immobilized enzyme will be stable at the optimum temperature of 50 oC, pH 5.6 and incubation time of 45 minutes with 0.030 units/mL of the unit activity. SEM-EDX pattern shows the differences in surface morphology between natural zeolite and activated natural zeolites which contain α-amylase enzyme. A mobilization technique can increase the stability utilized in a α-amylase enzyme. Keywords : Zeolite, amobilization, α-amylase enzyme



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