scholarly journals Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Bárbara M. Bonine ◽  
Patricia Peres Polizelli ◽  
Gustavo O. Bonilla-Rodriguez
Keyword(s):  
Calcium Alginate ◽  
Immobilized Lipase ◽  
Temperature Stability ◽  
Immobilized Enzymes ◽  
Free Enzyme ◽  
Poly Vinyl Alcohol ◽  
Optimum Temperature ◽  
Original Activity ◽  
Plant Lipase ◽  
Number Of Cycles

This study reports the immobilization of a new lipase isolated from oleaginous seeds of Pachira aquatica, using beads of calcium alginate (Alg) and poly(vinyl alcohol) (PVA). We evaluated the morphology, number of cycles of reuse, optimum temperature, and temperature stability of both immobilization methods compared to the free enzyme. The immobilized enzymes were more stable than the free enzyme, keeping 60% of the original activity after 4 h at 50°C. The immobilized lipase was reused several times, with activity decreasing to approximately 50% after 5 cycles. Both the free and immobilized enzymes were found to be optimally active between 30 and 40°C.

Use of chemically modified poly(ethylene terephthalate)-g- (acryl amide) fibers for α-amylase immobilization

e-Polymers ◽  
2007 ◽  
Vol 7 (1) ◽  
Author(s):  
Zülfikar Temoçin ◽  
Mustafa Yiğitoğlu
Keyword(s):  
Ethylene Terephthalate ◽  
Immobilized Enzymes ◽  
Storage Conditions ◽  
Maximum Activity ◽  
Free Enzyme ◽  
Original Activity ◽  
Poly Ethylene Terephthalate ◽  
Repeated Use ◽  
Amine Groups ◽  
Poly Ethylene

AbstractAcryl amide grafted Poly(ethylene terephthalate) (AAm-g-PET) fiber was used for covalent coupling of α-amylase. The amide groups of Poly(acryl amide) were converted to the amine groups by Hofmann degradation reaction. The amine groups were activated by glutaraldehyde, before coupling of the enzyme. The free α-amylase and immobilized α-amylase were characterized by determining the activity profile as function of pH, temperature, thermal stability and storage stability. For the immobilized α-amylase, operational stability was also determined. The immobilization of α-amylase on support caused the optimal reaction pH to shift from 5 to 6. The maximum activity of the free and immobilized enzymes occurred at 50 0C. Km for the immobilized system was higher than that for the free enzyme. The activity of the free enzyme ended in 30 days, whereas the activity of the immobilized enzyme lasted for 60 days at storage conditions. α-Amylase immobilized on matrix maintained 40% of its original activity after 30 times of repeated use.

scholarly journals PENGARUH SUHU INKUBASI TERHADAP AKTIVITAS LIPASE DAUN PEPAYA (Carica papaya L) YANG DIAMOBILISASI DALAM PASIR LAUT

KOVALEN ◽  
2019 ◽  
Vol 5 (2) ◽  
pp. 116-120
Author(s):  
Fisty Sumangkut ◽  
Nurhaeni ◽  
Ni Ketut Sumarni ◽  
Erwin Abdul Rahim
Keyword(s):  
Carica Papaya ◽  
Incubation Temperature ◽  
Immobilized Lipase ◽  
Temperature Stability ◽  
Silica Content ◽  
Immobilize Lipase ◽  
Optimum Temperature ◽  
Randomized Design ◽  
Sea Sand ◽  
Completely Randomized Design

The silica content in sea sand can be used to immobilize lipase from papaya leaf. Research on the influence  of  incubation temperature on sea sand immobilized lipase from papaya leaf (Carica papaya L) has been carried out. The aim of research is determining the influence of incubation temperature on sea sand immobilized lipase from papaya leaf (Carica papaya L). The method used in this study was a completely randomized design with temperature at 30, 40, 50, 60, 70°C.  The results show that lipase from papaya leaf (Carica papaya L) had successfully immobilized in the sea sand and the optimum temperature stability of lipase immobilized in sea sand at  50°C with an activity is 53.000 µmol/g.jam Keywords : immobilized, lipase, papaya leaf, sea sand.

scholarly journals Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae

2007 ◽  
Vol 72 (12) ◽  
pp. 1255-1263 ◽  
Author(s):  
Khaled Ahmed ◽  
Nenad Milosavic ◽  
Milica Popovic ◽  
Radivoje Prodanovic ◽  
Zorica Knezevic ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Thermal Stability ◽  
Immobilized Enzyme ◽  
Immobilized Enzymes ◽  
Optimum Temperature ◽  
Activity Profile ◽  
Original Activity ◽  
Yeast Saccharomyces Cerevisiae ◽  
Optimum Ph ◽  
Promising Solution

?-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of ?-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45 ?C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized ?-glucosidase.

scholarly journals Production of Aspartame by Immobilized Thermolysin

2019 ◽  
pp. 1232-1239
Author(s):  
Mohammed A Alsoufi ◽  
Raghad A. Aziz
Keyword(s):  
Reaction Time ◽  
Immobilized Enzyme ◽  
Bentonite Clay ◽  
Optimum Temperature ◽  
Initial Activity ◽  
Reaction Conditions ◽  
Original Activity ◽  
Ph Profile ◽  
Full Activity ◽  
Main Activity

The aim of this study was the production of aspartame by using immobilized thermolysin in bentonite clay. The yield of immobilized thermolysin in bentonite was 92% of the original enzyme amount. pH profile of free and immobilized enzyme was 7.0 and 7.5 respectively which was stable at 6.5-9.0 for 30min. The optimum temperature of both enzymes was 50°C, while they were stable at 65°C for 30min. however, they lost 52.73 and 61.72% from its main activity at 80°C respectively. Immobilized thermolysin has retained all activity within 27 days, but it kept 68.27% of initial activity when stored for 60 days at 4°C whereas, it retained a full activity after 20 continue usage. In addition, it retained 86.53% of its original activity after 30 continuing usages. The yield of produced aspartame was increased with reaction time; it was 9% after 1h and increased gradually to 100% after 10h at reaction conditions.

scholarly journals Application of β-glucosidase Immobilized on Chitosan microspheres in Degradation of Polydatin in Polygonum cuspidatum

2021 ◽  
Vol 233 ◽  
pp. 02034
Author(s):  
Wei Zong ◽  
Shan Liu ◽  
Jeonyun Yun ◽  
Xiong Xiao ◽  
Zujun Deng ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cost Reduction ◽  
Degradation Rate ◽  
Temperature Stability ◽  
Catalytic Efficiency ◽  
Efficient Production ◽  
Polygonum Cuspidatum ◽  
Optimum Temperature ◽  
Preparation Conditions ◽  
Hydrolysis Of

Resveratrol in Polygonum cuspidatum is a β-glycoside, which can be hydrolyzed to resveratrol by β-glucosidase. it is an efficient production process to degrade polydatin from Polygonum cuspidatum extract by immobilized β-glucosidase. It is of great significance to explore suitable immobilization conditions to improve the catalytic efficiency and reusability of β-glucosidase for polydatin degradation and cost reduction. In this paper, the recombinant Escherichia coli bgl2238, which was screened and constructed from corn soil of Heilongjiang Province in the early laboratory, was immobilized by chitosan adsorption and glutaraldehyde crosslinking. The preparation conditions and immobilization process of bgl2238 were determined by single factor method: the optimal crosslinking time was 1 h, the optimal crosslinking temperature was 20 °C, the recovery rate of enzyme activity of bgl2238 was 87 %, and the enzyme activity was 859.65 mU/g. The optimum temperature of the immobilized bgl2238 is 50 °C, which is 6 °C higher than that of the free bgl2238, and the temperature stability and pH stability are improved. After six consecutive hydrolysis of Polygonum cuspidatum, the degradation rate of polydatin is still over 70 %, which proves that the immobilized bgl2238 has good reusability. This will be helpful to evaluate the application prospect of β - glucosidase immobilized in this system and determine the best conditions for its production.

scholarly journals Purification and Characterization of Endoglucanase from local isolate of Aspergillus flavus

2013 ◽  
Vol 10 (3) ◽  
pp. 844-853
Author(s):  
Baghdad Science Journal
Keyword(s):  
Aspergillus Flavus ◽  
Specific Activity ◽  
Gel Filtration ◽  
Temperature Stability ◽  
Exchange Chromatography ◽  
Purification And Characterization ◽  
Original Activity ◽  
A Value ◽  
Optimum Ph

Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.

scholarly journals Immobilization of Isolated Lipase From Moldy Copra(Aspergillus Oryzae)

2011 ◽  
Vol 8 (2) ◽  
pp. 896-902
Author(s):  
Seniwati Dali ◽  
A. B. D. Rauf Patong ◽  
M. Noor Jalaluddin ◽  
Pirman ◽  
Baharuddin Hamzah
Keyword(s):  
Thermal Stability ◽  
Aspergillus Oryzae ◽  
Immobilized Lipase ◽  
Optimum Temperature ◽  
Adsorption Method ◽  
Ph Optimum ◽  
Optimum Ph ◽  
Recovery Technique ◽  
Free Lipase

Enzyme immobilization is a recovery technique that has been studied in several years, using support as a media to help enzyme dissolutions to the reaction substrate. Immobilization method used in this study was adsorption method, using specific lipase fromAspergillus oryzae. Lipase was partially purified from the culture supernatant ofAspergillus oryzae. Enzyme was immobilized by adsorbed on silica gel. Studies on free and immobilized lipase systems for determination of optimum pH, optimum temperature, thermal stability and reusability were carried out. The results showed that free lipase had optimum pH 8,2 and optimum temperature 35 °C while the immobilized lipase had optimum 8,2 and optimum temperature 45 °C. The thermal stability of the immobilized lipase, relative to that of the free lipase, was markedly increased. The immobilized lipase can be reused for at least six times.

Tailoring surface properties of functionalized graphene papers aiming to enzyme immobilization

2021 ◽  
Author(s):  
Jéssica Luzardo ◽  
Douglas Aguiar ◽  
Alexander Silva ◽  
Sanair Oliveira ◽  
Braulio Archanjo ◽  
...  
Keyword(s):  
Cyclic Voltammetry ◽  
Photoelectron Spectroscopy ◽  
Enzyme Stability ◽  
Immobilized Enzymes ◽  
Free Enzyme ◽  
X Ray ◽  
Force Microscopy ◽  
Enzyme Solution ◽  
Atomic Force ◽  
Composition And Structure

The use of enzymes as catalysts requires recovery and reuse to make the process viable. Enzymatic immobilization changes enzyme stability, activity, and specificity. It is very important to explore new substrates for immobilization with appropriate composition and structure to improve the efficiency of the immobilized enzymes. This work explores the use of two different graphene oxide papers, one produced by oxidation route (GO) and the other by electrochemical synthesis (EG), aiming for β-galactosidase immobilization. The chemical and structural properties of these two papers were characterized by Raman spectroscopy, X-ray photoelectron spectroscopy and X-ray diffraction. Atomic force microscopy images showed that EG paper ensured more efficient immobilization of the enzymes on the surface of the paper. Cyclic voltammetry was used to monitor the reaction of conversion of lactose to glucose in the free enzyme solution and graphene paper immobilized enzyme solutions. The cyclic voltammetry analysis showed that immobilized enzymes on GO paper showed an improvement in the activity of β-galactose when compared to free enzyme solution, as well as enzyme immobilized on a glassy carbon electrode.

scholarly journals Lipase-catalyzed transesterification of rendering plant fat – Short Communication

2010 ◽  
Vol 56 (No. 3) ◽  
pp. 122-125 ◽  
Author(s):  
A. Prošková ◽  
Z. Kopicová ◽  
J. Kučera ◽  
L. Škarková
Keyword(s):  
Short Communication ◽  
Immobilized Enzyme ◽  
Immobilized Lipase ◽  
Covalent Bond ◽  
Novozym 435 ◽  
Optimum Temperature ◽  
Optimum Conditions ◽  
Soluble Lipase ◽  
Good Accordance ◽  
Higher Temperature

Soluble lipase (Lipozyme CALB L) was immobilized by covalent bond to chitosan pellets prepared from Aspergillus niger mycelium. This immobilized enzyme was compared with commercial immobilized lipase of the same origin (Novozym 435). Novozym 435 is also lipase CALB L commercially immobilized by sorption on poly-(methyl acrylate). Novozym 435 shows much higher conversion of rendering plant fat in methanol under optimum conditions, having, at the same time, lower optimum temperature and lower stability at higher temperature. Lipozyme CALB L immobilized on chitosan leads to a low conversion, regardless its higher thermal stability. Novozym 435 gives conversion of about 50% of theoretical value, which is in good accordance with basically catalyzed transesterification of rendering plant fat described elsewhere. Lipozyme CALB L immobilized on chitosan gives conversion of about 10% of theoretical value only. The use of Novozym 435 in two-step system (enzyme-acid) seems to be more convenient compared with traditional two-step system (base-acid)

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