Chitosanase Immobilization Using Composite Carrier of Sodium Alginate/Cellulose

2011 ◽  
Vol 236-238 ◽  
pp. 2371-2377 ◽  
Author(s):  
Yan Wang ◽  
Chen Lu Zhang ◽  
Ping Li ◽  
Pei Gen Zhou ◽  
Xiao Rong Pan

Sodium alginate and cellulose were combined to use as a composite carrier forPseudomonassp. CUY8 chitosanase immobilization. For free enzyme, immobilized chitosanase within different carriers of sodium alginate and composite carrier, Km values were 1.919, 9.27, and 5.91µM, respectively. The increase of Km value of immobilized chitosanase with composite carrier was lower than that of single carrier. This indicates that the composite carrier of sodium alginate/ cellulose improves the affinity of chitosanase to the substrate. Furthermore, chitosanase immobilization using composite carrier shows improved thermal stability ranging from 65 to 80°C, and enzyme residual activities were more than 75%. The effects of ratio of enzyme to substrate on chitooligosaccharides (COS) production were determined, and COS yields with composite carrier was 68% at optimum ratio of 1:1. Since the immobilization process using composite carrier is simple and effective, this method could be used for the industrial production of COS.

2022 ◽  
Vol 905 ◽  
pp. 271-276
Author(s):  
Hui Wang ◽  
Cong Ying Hou ◽  
Yan Bai

The effect of bentonite (BT) on the structure and performance of sodium alginate (SA) as microsphere carrier of essential oil is studied. The addition of BT can improve the performance of alginate gel microspheres through the study of the properties of single carrier SA and composite carrier SA/BT. The experimental results show that the viscosity of composite carrier SA/BT solution is higher than that of carrier SA solution, and the increasing rate of viscosity of composite solution with temperature is less than that of SA. The addition of BT can effectively inhibit the swelling of SA microspheres. The hydrogen bonding between SA and BT is shown in FTIR, and the interlayer spacing of BT crystal structure is not changed in XRD analysis. The mass loss rate of SA/BT microspheres is lower than that of SA in TGA analysis. The more dense structure of SA/BT microspheres than that of SA microspheres is confirmed by SEM. The release rate of cinnamon oil in SA/BT gel microspheres is significantly lower than that in SA gel microspheres under different temperature conditions. The addition of BT could better control the volatilization of essential oil encapsulated in SA gel microspheres.


Catalysts ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 983
Author(s):  
Wahhida Latip ◽  
Victor Feizal Knight ◽  
Ong Keat Khim ◽  
Noor Azilah Mohd Kasim ◽  
Wan Md Zin Wan Yunus ◽  
...  

Immobilization is a method for making an enzyme more robust in the environment, especially in terms of its stability and reusability. A mutant phosphotriesterase (YT PTE) isolated from Pseudomonas dimunita has been reported to have high proficiency in hydrolyzing the Sp and Rp-enantiomers of organophosphate chromophoric analogs and therefore has great potential as a decontamination agent and biosensor. This work aims to investigate the feasibility of using Fuller’s earth (FE) as a YT PTE immobilization support and characterize its biochemical features after immobilization. The immobilized YT PTE was found to show improvement in thermal stability with a half-life of 24 h compared to that of the free enzyme, which was only 8 h. The stability of the immobilized YT PTE allowed storage for up to 4 months and reuse for up to 6 times. The immobilized YT PTE showed high tolerance against all tested metal ions, Tween 40 and 80 surfactants and inorganic solvents. These findings showed that the immobilized YT PTE became more robust for use especially with regards to its stability and reusability. These features would enhance the future applicability of this enzyme as a decontamination agent and its use in other suitable industrial applications.


1974 ◽  
Vol 1 (4) ◽  
pp. 579 ◽  
Author(s):  
S Leblova

Alcohol dehydrogenase isolated from broad bean was found to have a Km value of 1.0 × 1.0 -2 M, a pH optimum of 8.7 and a molecular weight of 60 000 � 5000. The enzyme lost 55 % of its activity after being heated at 55�C, and was totally inactivated at 70°C. Thermal stability of the enzyme was not enhanced by NAD+ or ethanol. The substrate specificity of the enzyme is reported. Cysteine and mercaptoethanol activated the enzyme, whilep-chloromercuribenzoate, Cu2+, Hg2+, B4O72- -, Zn2+ and EDTA inhibited it. The influence of ethanol, acetaldehyde and growth substances on alcohol dehydrogenase activity in germinating broad bean seeds and plant tissues was also studied.


RSC Advances ◽  
2015 ◽  
Vol 5 (16) ◽  
pp. 11761-11765 ◽  
Author(s):  
Lu Liu ◽  
Yongqian Shi ◽  
Bin Yu ◽  
Qilong Tai ◽  
Bibo Wang ◽  
...  

Graphitic carbon nitride (g-C3N4)/montmorillonite (Na-MMT) nanohybrids were fabricated and introduced into a sodium alginate with different levels. The introduction of 4.0 wt% nanohybrids led to the maximal improvement by ca. 149 °C in thermal stability.


2021 ◽  
Vol 2 (1) ◽  
pp. 30-41
Author(s):  
Pooneh Kia ◽  
Mansor Bin Ahmad ◽  
Kamyar Shameli

Fluorapatite (FA) can be used as a bioactive substance in the body, especially the teeth implants. The FA nanoparticle was synthesized by adding the fluorine to the structure of HA using sol–gel method and the heat treatment of 700 °C. Being low costs, eco-friendly and safer features are obvious advantages of the green synthesis of FA nanoparticles by using bio stabilizer of sodium alginate. Calcium nitrate tetrahydrate, diammonium phosphate, ammonium fluoride were used as precursors of Ca, P and F respectively with the ratio of 1:67 Ca/P. The presence of crystal structure of HA and FA investigated by the results of XRD which confirmed the substitution of hydroxyl groups with the fluorine in the crystal structure of apatite. FTIR obtained that fluorine was substituted by hydroxyl groups in the structure of fluoridated hydroxyapatite by disappearing the hydroxyl groups at 3600 cm-1 in the FA. TGA investigated the thermal stability of the nanoparticles that showed the discrepancy of weight loss for HA and FA between 600?C to 800?C. By using TEM, average sizes of 35 and 49 nm were determined for HA and FA respectively. FESEM results confirmed the shapes and distribution of particles of HA and FA in that, round like for the former and rode like for the later. The overall performance of utilizing sodium alginate (SA) as a bio-stabilizer is to obtain better precipitate which leads to having better crystallinity and smaller particle size and thermal stability remarkably improved.


2012 ◽  
Vol 554-556 ◽  
pp. 1507-1510 ◽  
Author(s):  
Li Qing Zhao ◽  
Jia Mao Fang ◽  
Xiang Dong Xiao

A novel strain, Bacillus fusiformis CGMCC1347, was utilized successfully to transform isoeugenol to vanillin and the product inhibition could be well avoided by using immobilized cells in the isoeugenol/aqueous biphasic system. The Bacillus fusiformis CGMCC1347 cells were entrapped into sodium alginate under conditions of 2.5% sodium alginate, 10% cells and 0.1 mol l-1 CaCl2. The optimum pH for free cells and immobilized cells were 4.0 and 3.5, respectively, and the optimum reaction temperature for both free and immobilized cells was 37 °C. The pH stabilities of free cells and immobilized cells were good at all investigated pH levels. For thermal stability, free cells were stable at 50°C60°C and the immobilized cells were stable at 50°C 80°C. The half-life of the immobilized cells was more than 25 d, comparing with less than 14 d for the free cells at 4°C.


Biomolecules ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 904
Author(s):  
Rana Morsi ◽  
Khadega A. Al-Maqdi ◽  
Muhammad Bilal ◽  
Hafiz M. N. Iqbal ◽  
Abbas Khaleel ◽  
...  

In the present study, soybean peroxidase (SBP) was covalently immobilized onto two functionalized photocatalytic supports (TiO2 and ZnO) to create novel hybrid biocatalysts (TiO2-SBP and ZnO-SBP). Immobilization caused a slight shift in the pH optima of SBP activity (pH 5.0 to 4.0), whereas the free and TiO2-immobilized SBP showed similar thermal stability profiles. The newly developed hybrid biocatalysts were used for the degradation of 21 emerging pollutants in the presence and absence of 1-hydroxy benzotriazole (HOBT) as a redox mediator. Notably, all the tested pollutants were not equally degraded by the SBP treatment and some of the tested pollutants were either partially degraded or appeared to be recalcitrant to enzymatic degradation. The presence of HOBT enhanced the degradation of the pollutants, while it also inhibited the degradation of some contaminants. Interestingly, TiO2 and ZnO-immobilized SBP displayed better degradation efficiency of a few emerging pollutants than the free enzyme. Furthermore, a combined enzyme-chemical oxidation remediation strategy was employed to degrade two recalcitrant pollutants, which suggest a novel application of these novel hybrid peroxidase-photocatalysts. Lastly, the reusability profile indicated that the TiO2-SBP hybrid biocatalyst retained up to 95% degradation efficiency of a model pollutant (2-mercaptobenzothiazole) after four consecutive degradation cycles.


2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
G. Arabaci ◽  
A. Usluoglu

Catalase was partially purified fromMalva sylvestrisL. and immobilized onto chitosan. Then, its catalytic properties were investigated. (NH4)2SO4precipitation and dialysis were performed in the extracted enzyme. Further purification was performed with sephadex G-200 column. Kinetic studies of the purified enzyme activity were measured and characterized. The inhibitory effects of KCN, NaN3, CuSO4, and EDTA onM. sylvestrisL. catalase activity were observed except NaCl. Furthermore,M. sylvestrisL. catalase was immobilized covalently with glutaraldehyde onto chitosan particles. The pH and temperature optima as well as the changes in the kinetics (Km, Vmax) of the immobilized and freeM. sylvestrisL. catalase were determined. The Km value for immobilized catalase (23.4 mM) was higher than that of free enzyme (17.6 mM). Optimum temperature was observed higher than that of the free enzyme. The optimum pH was the same for both free and immobilized catalases (pH 7.50). Immobilized catalase showed higher storage and thermal stabilities than free catalases. Free catalase lost all its activity within 60 days whereas immobilized catalase lost 45% of its activity during the same incubation period at 4°C. The remaining immobilized catalase activity was about 70% after 8 cycles of batch operations.


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