scholarly journals Kinetic Characterization and Effect of Immobilized Thermostable β-Glucosidase in Alginate Gel Beads on Sugarcane Juice

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Keerti ◽  
Anuradha Gupta ◽  
Vinod Kumar ◽  
Ashutosh Dubey ◽  
A. K. Verma
Keyword(s):  
Storage Stability ◽  
Immobilized Enzyme ◽  
Residual Activity ◽  
Sugarcane Juice ◽  
Ph Stability ◽  
Gel Beads ◽  
Optimum Ph ◽  
Enzyme Change ◽  
Ph Range ◽  
And Storage

A thermostable β-glucosidase was effectively immobilized on alginate by the method of gel entrapment. After optimization of immobilized conditions, recovered enzyme activity was 60%. Optimum pH, temperature, kinetic parameters, thermal and pH stability, reusability, and storage stability were investigated. The Km and Vmax for immobilized β-glucosidase were estimated to be 5.0 mM and 0.64 U/ml, respectively. When comparing, free and immobilized enzyme, change was observed in optimum pH and temperature from 5.0 to 6.0 and 60°C to 80°C, respectively. Immobilized enzyme showed an increase in pH stability over the studied pH range (3.0–10.0) and stability at temperature up to 80°C. The storage stability and reusability of the immobilized β-glucosidase were improved significantly, with 12.09% activity retention at 30°C after being stored for 25 d and 17.85% residual activity after being repeatedly used for 4 times. The effect of both free and immobilized β-glucosidase enzyme on physicochemical properties of sugarcane juice was also analyzed.

Immobilization and Characterization of Tannase and its Haze-removing

2009 ◽  
Vol 15 (6) ◽  
pp. 545-552 ◽  
Author(s):  
Erzheng Su ◽  
Tao Xia ◽  
Liping Gao ◽  
Qianying Dai ◽  
Zhengzhu Zhang
Keyword(s):  
Kinetic Parameter ◽  
High Activity ◽  
Green Tea ◽  
Storage Stability ◽  
Residual Activity ◽  
Black Tea ◽  
Optimum Temperature ◽  
Oolong Tea ◽  
Optimum Ph

Tannase was effectively immobilized on alginate by the method of crosslinking-entrapment-crosslinking with a high activity recovery of 76.6%. The properties of immobilized tannase were investigated. Its optimum temperature was determined to be 35 ° C, decreasing 10 °C compared with that of free enzyme, whereas the optimum pH of 5.0 did not change. The thermal and pH stabilities of immobilized tannase increased to some degree. The kinetic parameter, Km, for immobilized tannase was estimated to be 11.6 × 10-4 mol/L. Fe2+ and Mn2+ could activate the activity of immobilized tannase. The immobilized tannase was also applied to treat the tea beverage to investigate its haze-removing effect. The content of non-estern catechins in green tea, black tea and oolong tea increased by 52.17%, 12.94% and 8.83%, respectively. The content of estern catechins in green tea, oolong tea and black tea decreased by 20.0%, 16.68% and 5.04%, respectively. The anti-sediment effect of green tea infusion treated with immobilized tannase was significantly increased. The storage stability and reusability of the immobilized tannase were improved greatly, with 72.5% activity retention after stored for 42 days and 86.9% residual activity after repeatedly used for 30 times.

scholarly journals Digestive Proteases From Fish Processing Wastes: Their Partial Characterization and Comparison

2020 ◽  
Author(s):  
Ivana Soledad Friedman ◽  
Leonel Agustín Behrens ◽  
Nair A Pereira ◽  
Edgardo Contreras ◽  
Analia Verónica Fernández-Gimenez
Keyword(s):  
Residual Activity ◽  
Fish Processing ◽  
Intestinal Enzymes ◽  
Optimum Ph ◽  
Digestive Proteinases ◽  
Wide Ph Range ◽  
Processing Wastes ◽  
Reducing Costs ◽  
Ph Range ◽  
Percophis Brasiliensis

Abstract Fish processing generates a lot of wastes which are discarded resulting in environmental problems. However, this material represents a significant source of high-value bioproducts with potential biotechnological applications. The objective of this study was to characterize and to compare specific activities of acid and alkaline proteases recovered from the viscera of Merluccius hubbsi (Mh), Percophis brasiliensis (Pb), Urophyis brasiliensis (Ub), and Cynoscion guatucupa (Cg) under different pH and temperature conditions. Stomach proteinases from four species had a higher activity at pH 2, with stability in the range of pH 2-4. Optimum pH from intestinal enzymes of Cg was 11.5, while for the crude extract of Mh, Pb, and Ub catalytic activity was registered over a wide pH range range from 7 to 11.5. Stomach proteinases from four studied species had a higher activity at 30 °C and 50 °C, with stability at 10 °C and 30 °C. Optimum temperature from intestinal enzymes of the four tested species was 50 °C with high stability at 10 °C and 30 °C. Alkaline proteinase from all species and acid proteinases from Cg was inactivated at 70ºC, while stomach enzymes of Mh, Pb, and Ub had a residual activity lower than 5% at 80 °C after 5, 10 y 20 minutes of pre-incubation, respectively. Digestive proteinases recovered in this study could be used as biocatalysts in industrial processes, reducing costs, adding value to the fishery waste, and contributing to the reduction of environmental pollution.

scholarly journals Optimization of Processing Parameters for Extraction of Amylase Enzyme from Dragon (Hylocereus polyrhizus) Peel Using Response Surface Methodology

2014 ◽  
Vol 2014 ◽  
pp. 1-12 ◽  
Author(s):  
Mehrnoush Amid ◽  
Mohd Yazid Abdul Manap ◽  
Norkhanani Zohdi
Keyword(s):  
Storage Stability ◽  
Specific Activity ◽  
Mixing Time ◽  
Temperature Stability ◽  
Processing Parameters ◽  
Ph Stability ◽  
Extraction Condition ◽  
Main Effect ◽  
And Storage ◽  
Optimum Extraction

The main goal of this study was to investigate the effect of extraction conditions on the enzymatic properties of thermoacidic amylase enzyme derived from dragon peel. The studied extraction variables were the buffer-to-sample (B/S) ratio (1 : 2 to 1 : 6, w/w), temperature (−18°C to 25°), mixing time (60 to 180 seconds), and the pH of the buffer (2.0 to 8.0). The results indicate that the enzyme extraction conditions exhibited the least significant (P<0.05) effect on temperature stability. Conversely, the extraction conditions had the most significant (P<0.05) effect on the specific activity and pH stability. The results also reveal that the main effect of the B/S ratio, followed by its interaction with the pH of the buffer, was significant (P<0.05) among most of the response variables studied. The optimum extraction condition caused the amylase to achieve high enzyme activity (648.4 U), specific activity (14.2 U/mg), temperature stability (88.4%), pH stability (85.2%), surfactant agent stability (87.2%), and storage stability (90.3%).

scholarly journals The Properties of Immobilized Invertase Onto a New Support Material; Poly(Methacrylamide/Maleic Acid) Copolymeric Hydrogel

2018 ◽  
Vol 26 (2) ◽  
pp. 307-328 ◽  
Author(s):  
Hesna Nursevin Öztop ◽  
Fatma Banu Çatmaz ◽  
Dursun Saraydin
Keyword(s):  
Maleic Acid ◽  
Storage Stability ◽  
Maximum Velocity ◽  
Optimum Temperature ◽  
Michaelis Constant ◽  
Ph Values ◽  
Optimum Ph ◽  
And Storage ◽  
And Diffusion

Abstract Poly (methacrylamide / maleic acid) PM/MA and poly (methacrylamide) PM hydrogels were prepared aiming to be used as a support for invertase. Spectrophotometric, thermal analysis methods, swelling and diffusion experiments were used for the characterization of hydrogels. The swelling of PM/MA was higher than that of PM in water. The diffusion of water within the hydrogel was found to be non-Fickian. Invertase was immobilized onto PM and PM/MA (samples named PM-I and PM/MA-I respectively). The optimum pH values were found to be; 6.0, 5.0 and 5.5 for free invertase, PM-I and PM/MA-I respectively. The optimum temperature values were found to be 30 °C, 35 °C and 40 °C for free invertase, PM-I and PM/MA-I respectively. The Michaelis constant (Km) and maximum velocity of the enzymes (Vmax) were Km: 11,75 mM, Vmax: 1,95 μmol min−1 for free invertase, Km: 67,24 mM, Vmax: 60,6 μmol min−1 for PM-I and Km: 74,55 mM, Vmax: 18,12 μmol min−1 for PM/MA-I. PM/MA-I showed excellent thermal, operational and storage stability.

scholarly journals Activity and stability of immobilized Candida rugosa lipase on chitosan coated Fe3O4 nanoparticles in aqueous and organic media

2014 ◽  
Vol 10 (3) ◽  
pp. 2478-2483 ◽  
Author(s):  
Mohamed A. Abd-Elhakeem ◽  
Ahmed M. Elsayed ◽  
Taher A. Alkhulaqi
Keyword(s):  
Storage Stability ◽  
Immobilized Enzyme ◽  
Candida Rugosa ◽  
Chitosan Nanoparticles ◽  
Candida Rugosa Lipase ◽  
Initial Activity ◽  
Lipase Immobilization ◽  
Lipase Enzyme ◽  
Immobilized Candida Rugosa Lipase ◽  
And Storage

Fe3O4 (magnetite) nanoparticles were prepared by coprecipitation method, coated by chitosan and functionalized by glutaraldehyde. Lipase enzyme from Candida rugosa was immobilized on the prepared particles via cross linking reaction. Synthesis steps and characterization were examined by XRD, TEM, and FTIR.  The immobilization conditions were 10 mL of phosphate buffer (0.1 M, pH 6.5) containing 30 mg of  functionalized magnetic chitosan nanoparticles and 2.0 mg·mL-1 of lipase, immobilization temperature of 4 ℃ and immobilization time of 1 h. Under these conditions, lipase was successfully immobilized with loading capacity of 87 mg/g. The immobilized enzyme showed good operational and storage stability, where it remained stable after 30 days of storage at 4◦C.and retained about 61% of its initial activity after twenty repeated uses. Finally enzymatic catalyze synthesis of butyl and hexyl oleate at 40 ◦C with shaking (200 rpm) was realized in n-hexane and confirmed by GC analysis.

Studies on Penicillium M2 Chitosanase Immobilized on CSG Hybrid Material by Cross-Linking Reaction

2012 ◽  
Vol 512-515 ◽  
pp. 2419-2423
Author(s):  
Yan Jun Wang ◽  
Shao Ling Zhuo ◽  
Sheng Chen
Keyword(s):  
Kinetic Parameter ◽  
Hybrid Material ◽  
Storage Stability ◽  
Immobilized Enzyme ◽  
Cross Linking ◽  
Optimal Conditions ◽  
Optimal Temperature ◽  
Carrier Material ◽  
And Storage

Chitosanase was immobilized on CSG hybrid material by cross-linking reaction and the immobilization conditions and characterization of the immobilized enzyme were carried out. The optimal conditions for immobilization were as follows: 0.1 g carrier material was treated with 2.5 ml 5% solution of glutaraldehyde and 2 ml chitosanase was immobilized on the carrier. Optimal temperature and pH for the immobilized enzyme were 60°C and 7.0, respectively. Kinetic parameter Km was10.64 g/l. The immobilized enzyme showed better operation and storage stability than the free enzyme.

Optimum pH and pH Stability of Crude Polyphenol Oxidase (PPO) Extracted from Five Fruit Samples Commonly Consumed in Kano State, Nigeria

1970 ◽  
Vol 4 (1) ◽  
pp. 26-31
Author(s):  
AB Bello ◽  
MS Sule ◽  
AJ Alhassan
Keyword(s):  
Polyphenol Oxidase ◽  
Cucurbita Pepo ◽  
Carica Papaya ◽  
Psidium Guajava ◽  
Ph Stability ◽  
Effect Of Ph ◽  
Solanum Aethiopicum ◽  
Optimum Ph ◽  
Bush Mango ◽  
Ph Range

The effect of pH on the activity and stability of crude polyphenol oxidase (PPO) extracted from garden egg (Solanum aethiopicum), pawpaw (Carica papaya), pumpkin (Cucurbita pepo), guava (Psidium guajava) and bush mango (Irvingia gabonnensis) fruits were studied. Catechol at concentration of 20 mM was used as a substrate while sodium acetate buffer (0.2 M), pH range between 3.0– 5.5 and sodium phosphate buffer(0.2 M) , pH range between 6.0– 8.5 were used to determine the effect of pH on the PPO activity. Optimum pH values were found to be 6.0,6.5,6.0, 4.5 and 4.0/or 8.0 for the enzyme extracted from Solanum aethiopicum, Carica papaya, Cucurbita pepo, Psidium guajava and Irvingia gabonnensis respectively. The enzyme was found to be stable at the pH range of 5.0-7.5 for the enzyme extracted from garden egg, 6.0-8.0 for that from pawpaw, 4.5-7.0 for that from pumpkin, 4.0-6.5 for that from guava and 3.5-5.5 and 7.0-8.0 for that from bush mango respectively. Increase or decrease of pH from the ranges would cause decrease in the activity of the enzyme, and can be a good way of controlling undesirable changes caused by it in foods. Keywords: Optimum pH, pH stability, Polyphenol oxidase, Common fruits.

scholarly journals Immobilization and Characterization of a Recombinant Thermostable Lipase (Pf2001) from Pyrococcus furiosus on Supports with Different Degrees of Hydrophobicity

2010 ◽  
Vol 2010 ◽  
pp. 1-8 ◽  
Author(s):  
Roberta Vieira Branco ◽  
Melissa Limoeiro Estrada Gutarra ◽  
Denise Maria Guimarães Freire ◽  
Rodrigo Volcan Almeida
Keyword(s):  
Storage Stability ◽  
Immobilized Enzyme ◽  
Pyrococcus Furiosus ◽  
Residual Activity ◽  
Maximum Activity ◽  
Thermostable Lipase ◽  
Hyperthermophilic Archaeon ◽  
Biotechnological Processes

We studied the immobilization of a recombinant thermostable lipase (Pf2001) from the hyperthermophilic archaeon Pyrococcus furiosus on supports with different degrees of hydrophobicity: butyl Sepabeads and octadecyl Sepabeads. The enzyme was strongly adsorbed in both supports. When it was adsorbed on these supports, the enzyme showed 140 and 237% hyperactivation, respectively. The assessment of storage stability showed that the octadecyl Sepabeads immobilized enzyme showed 100% of residual activity after 30 days of storage. However, the greatest stability at was obtained in butyl Sepabeads immobilized enzyme, which retained 77% activity after 1 hour incubation. The maximum activity of the immobilized preparations was obtained with the pH between 6 and 7, at . Thus, this study achieved a new extremophilic biocatalyst with greater stability, for use in several biotechnological processes.

scholarly journals Optimization and Immobilization of Purified Labeo rohita Visceral Protease by Entrapment Method

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
S. Geethanjali ◽  
Anitha Subash
Keyword(s):  
Sodium Alginate ◽  
Calcium Chloride ◽  
Storage Stability ◽  
Labeo Rohita ◽  
Residual Activity ◽  
The Third ◽  
Protease Enzyme ◽  
Optimum Ph ◽  
Before And After ◽  
Temperature Storage

The purified fish visceral protease enzyme was immobilized by using various concentrations of sodium alginate and calcium chloride to optimize the best concentration for the formation of the beads. Then it was characterized by assaying the optimal pH, temperature, storage stability and reusability. The results on immobilization with sodium alginate and calcium chloride showed that a combination of 2% sodium alginate and 0.3 M calcium chloride weas found to be the optimum concentration for the formation of spherical and stable beads, this gave a maximal entrapped activity of 48.31%, and there was no change in the optimum pH 8.0 and temperature 40°C of protease before and after entrapment. The results on stability and reusability indicated that it was stable at 4°C retaining 100% residual activity after 5 days of storage and 67% loss of activity after ten days of storage and it retained 100% residual activity on the first reuse, 75% residual activity on the second reuse, 25% residual activity on the third use and complete loss in the activity on the fourth reuse.

On the Preparation of Bovine α-Thrombin

1978 ◽  
Vol 39 (01) ◽  
pp. 193-200 ◽  
Author(s):  
Erwin F Workman ◽  
Roger L Lundblad
Keyword(s):  
Immobilized Enzyme ◽  
Catalytic Properties ◽  
Specific Activity ◽  
Guanidine Hydrochloride ◽  
Low Molecular Weight ◽  
Reversible Process ◽  
Gel Beads ◽  
Tissue Thromboplastin ◽  
C 50 ◽  
Hydrolysis Of

SummaryAn improved method for the preparation of bovine α-thrombin is described. The procedure involves the activation of partially purified prothrombin with tissue thromboplastin followed by chromatography on Sulfopropyl-Sephadex C-50. The purified enzyme is homogeneous on polyacrylamide discontinuous gel electrophoresis and has a specific activity toward fibrinogen of 2,200–2,700 N.I.H. U/mg. Its stability on storage in liquid media is dependent on both ionic strenght and temperature. Increasing ionic strength and decreasing temperature result in optimal stability. The denaturation of α-thrombin by guanidine hydrochloride was found to be a partially reversible process with the renatured species possessing properties similar to “aged” thrombin. In addition, the catalytic properties of a-thrombin covalently attached to agarose gel beads were also examined. The activity of the immobilized enzyme toward fibrinogen was affected to a much greater extent than was the hydrolysis of low molecular weight, synthetic substrates.

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