scholarly journals Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry

2020 ◽  
Vol 2020 ◽  
pp. 1-12
Author(s):  
Esen Tasgin ◽  
Aynur Babagil ◽  
Hayrunnisa Nadaroglu ◽  
Patricia E. Allegretti
Keyword(s):  
Fe3o4 Nanoparticles ◽  
Carboxymethyl Cellulose ◽  
Food Industry ◽  
Acinetobacter Calcoaceticus ◽  
Immobilized Enzymes ◽  
Pectin Lyase ◽  
Three Phase ◽  
Optimum Ph ◽  
Ft Ir

An important component of the pectinase enzyme complex is pectin lyase (polymethylgalacturonate lyase; EC 4.2.2.10). In this study, extracellular pectin lyase enzyme was produced from Acinetobacter calcoaceticus bacteria. Pectin lyase was then purified using three-phase precipitation (TPP) technique with 25.5% yield. The pectin lyase was immobilized covalently via the L-glutaraldehyde spacer to the carboxymethyl cellulose. The immobilized pectin lyase was magnetized using Fe3O4 nanoparticles. Purified pectin lyase was connected to magnetized support material after 90 min at the rate of 80%. The most appropriate immobilization conditions were determined as pH 8 and 30°C. By characterizing the free and immobilized enzyme, KM, Vmax, and optimum pH and optimum temperature values were determined. It was optimum pH 8 and temperature 50°C for both free and immobilized pectin lyase. The structural characterization of the immobilized pectin lyase modified with Fe3O4 nanoparticles was carried out by SEM, FT-IR, and XRD chromatographic analyses. At the end of the study, free and immobilized enzymes were used for purification of some fruit juices and results were compared.

scholarly journals Immobilization of Purified Pectin Lyase from Pseudomonas putida onto Magnetic Lily Flowers (Lilium candidum L.) Nanoparticles and Applicability in Industrial Processes

Molecules ◽  
2020 ◽  
Vol 25 (11) ◽  
pp. 2671 ◽  
Author(s):  
Esen Tasgin ◽  
Hayrunnisa Nadaroglu ◽  
Aynur Babagil ◽  
Nazan Demir
Keyword(s):  
Pseudomonas Putida ◽  
Fe3o4 Nanoparticles ◽  
Higher Plants ◽  
Polyacrylamide Gel Electrophoresis ◽  
Industrial Applications ◽  
Pectin Lyase ◽  
Thermal Stabilities ◽  
Support Materials ◽  
Three Phase ◽  
Ft Ir

Pectinases are an important class of enzymes distributed in many higher plants and microorganisms. One of these enzymes is pectin lyase which has an important role in industrial applications such as clarification of fruit juices. Pectin lyase was purified with 73% yield from Pseudomonas putida bacteria and was 220.7-fold using three phase precipitation technique. Molecular weight of purified pectin lyase was determined as 32.88 kDa with SDS-polyacrylamide gel electrophoresis. The pectin lyase was immobilized covalently via the L-glutaraldehyde spacer to the cellulosic structures of lily flowers (Lilium candidum L.). The immobilized enzyme was then magnetized by modifying with γ-Fe3O4 nanoparticles and determined the most appropriate immobilization conditions as pH 6 and 30 °C. Purified pectin lyase was connected to magnetized support material after 60 min at the rate of 86.4%. The optimum pH and temperatures for the free and immobilized pectin lyase was found to be 6.0 and 40 °C. pH and thermal stabilities of the free and immobilized pectin lyase enzyme have been preserved at high-low temperatures and pH. The structural characterization of the immobilized pectin lyase was performed by SEM, FT-IR, and XRD chromatographic analyses and it was observed that the support materials structure was appropriated to immobilization with pectin lyase and to modify with Fe3O4 nanoparticles.

scholarly journals Characterization of Endogenous Transglutaminase Enzyme of Yellow Pike Conger’s Liver

2017 ◽  
Vol 20 (3) ◽  
pp. 582
Author(s):  
Santhy Wisuda Sidauruk ◽  
Tati Nurhayati ◽  
Untung Trimo Laksono
Keyword(s):  
Food Processing ◽  
Food Industry ◽  
Specific Activity ◽  
Living Organism ◽  
Fish Liver ◽  
Food Processing Industry ◽  
Food Properties ◽  
Optimum Ph ◽  
Pharmacological Application

Transglutaminases have been found in various living organism, such as mammals, plants, <br />microorganisms, and marine organisms including fishes. Transglutaminases have many various functions<br />such as food properties, non-food properties and pharmacologies. This research aimed to characterize<br />transglutaminase that obtained from byproducts of yellow pike conger (Congresox talabon) such as<br />catadromous fish of yellow pike conger’s liver. The characteristic of transglutaminase had the possibility<br />to know the optimum condition in application of transglutaminase from liver of yellow pike conger such<br />as food processing industry, non-food industry and pharmacological application. A yield of yellow pike<br />conger’s liver was 0.88±0.11%. Specific activity of remang fish liver weighing 10 grams was 1,375 U/mg.<br />Characteristic crude transglutaminase from liver of yellow pike conger had optimum pH at 7.5; optimum<br />temperature at 50°C, transglutaminase activity increased on Mg<br />2+<br /> ion dependent and crude transglutaminase <br />had molecular weight of 27.48; 37.00; 69.51; 78.89; 88.18; 108.45; 134.10; dan 172.12 kDa.<br /><br />

scholarly journals Purification of Pectin Lyase Enzyme from Bacillus pumilus Bacteria by Three-Phase Partitioning Method (TPP), Nanoflower Preparation and Investigation of Fruit Juice Clarification

2021 ◽  
Vol 12 (3) ◽  
pp. 3938-3955
Keyword(s):  
Bacillus Pumilus ◽  
Calcium Pyrophosphate ◽  
Fruit Juices ◽  
Pectin Lyase ◽  
Gel Chromatography ◽  
Cleavage Rate ◽  
Phase Partitioning ◽  
Three Phase ◽  
Solid Culture Medium ◽  
Ft Ir

In this study, firstly, Bacillus pumilus bacteria were isolated from tomato vegetables and identified. Then, the new pectin lyase enzyme was purified from B. pumilus, characterized, and hybrid nanoflower pectin lyase (hNF-PL) was synthesized the first time in this study. For this purpose, PL enzyme was produced in a solid culture medium using B. pumilus bacterium, and PL was purified in 191.8 folds with a yield of 78.2% using the three-phase partitioning (TPP) technique. Using SDS-PAGE, PL enzyme was determined to have a single subunit, and molecular weight was defined as 32.88 kDa with gel chromatography technique. This is the very first study to easily immobilize purified PL enzyme onto nanoflower chitosan/calcium pyrophosphate hybrid NPs. The synthesized nanoflower hNF-PL structure was characterized by SEM, FT-IR, XRD, and TEM chromatographic methods. In the final phase of the study, the effects of the pure PL and hNF-PL enzymes on the clarification and cleavage rate of fruit juices obtained from black grape, pomegranate, peach, red apple, and plum were investigated. Under the light shed by this study determined that the hNF-PL enzyme clarified the fruit juices more effectively than the pure PL enzyme.

scholarly journals Immobilization and Characterization of Bacillus Thuringiensis HCB6 Amylase in Calcium Alginate Matrix

Molekul ◽  
2017 ◽  
Vol 12 (1) ◽  
pp. 70 ◽  
Author(s):  
Zusfahair Zusfahair ◽  
Dian Riana Ningsih Dian Riana Ningsih ◽  
Dwi Kartika Dwi Kartika ◽  
Amin Fatoni Amin Fatoni ◽  
Indah Permatawati Indah Permatawati
Keyword(s):  
Incubation Time ◽  
Substrate Concentration ◽  
Contact Time ◽  
Alginate Bead ◽  
Residual Activity ◽  
Immobilized Enzymes ◽  
Optimum Ph ◽  
Km Value ◽  
Ca Alginate

Free enzyme in solution react with substrates to result in products which cannot be recovered for reuse. These problems can be overcome to a certain extent by the use of enzyme immobilization method. Immobilized enzymes are more robust and more resistant to condition changes. More importantly, the heterogeneous immobilized enzyme systems allow an easy recovery of both enzymes and products, multiple re-uses of enzymes, and continuous operation of enzymatic processes. Entrapment of enzymes in Ca-alginate is one of the simplest methods of immobilization. The aim of this research was to obtain the optimum condition of the making of immobilized amylase beads using a Ca-alginate bead and to determine its characteristics. The optimization of immobilized amylase beads includes variation of sodium alginates and variations of enzyme contact time with CaCl2. The characterization of immobilized amylase includes determination of optimum substrate concentration, optimum pH, and optimum incubation time as well as amylase stability test. Amylase activity was determined by using dinitro salicylic (DNS) method. The results showed that the optimum immobilized amylase obtained at alginate concentrations of 5% (w/v), contact time of 60 minutes and immobilization efficiency of 67.5%. Furthermore, immobilized amylase showed optimum substrate concentration of 1.5-2.5% (w/v), optimum pH of 6, an optimum incubation time of 20 minutes with the activity of 179.8 U/mL. The KM value for free amylase and immobilized amylases were 0.3 mM and 0.12 mM respectively. Vmax value for free amylase and immobilized amylases were 105.3 U/mL and 10.1 U/mL respectively. Immobilized Amylase can be used up to six times with the residual activity of 52.7%.

Novelty of Penicillium camembertii Lipase Supported on Glutaraldehyde Activated-SBA-15 Mesoporous Silica for Mono-Esterification of Bioglycerol in Non-Aqueous Media

2016 ◽  
Vol 14 (4) ◽  
pp. 919-928 ◽  
Author(s):  
Moreshwar P. Hude ◽  
Janusz Kozinski ◽  
Ajay K. Dalai ◽  
Ganapati D. Yadav
Keyword(s):  
Food Industry ◽  
Immobilized Lipase ◽  
Aqueous Media ◽  
Immobilized Enzymes ◽  
X Ray Diffraction ◽  
X Ray ◽  
Penicillium Camembertii ◽  
Ft Ir ◽  
Environmentally Friendly Approach ◽  
Ft Ir Spectroscopy

Abstract Hexagonal mesoporous type silica SBA-15 with pore sizes in the range 5.0–8.3 nm was synthesized using non-ionic triblock copolymer and characterized by Accelerated Surface Area Porosimetry (ASAP), FT-IR spectroscopy, X-ray diffraction (XRD) and Scanning Electron Microscopy (SEM). Different lipases were immobilized in glutaraldehyde activated mesoporous SBA-15 support. The resulting supported enzymes were shown to be active and stable catalysts for esterification of glycerol with oleic acid to produce monoglyceride (MG) which is commonly used in food industry. Various parameters were studied systematically to study kinetics. MG Synthesis using enzymatic process is an environmentally friendly approach. Enzyme immobilized on SBA-15 showed the best stability and catalytic activity in organic solvents. Out of various lipases studied penicillium camembertii (Lipase G) produced MG efficiently at low temperature. Reusability was studied on immobilized enzymes. Immobilized lipase maintained 90 % of its esterification activity in non-aqueous media even after 4 cycles of use. The selectivity of Lipase G is found to be 98 % for monoacylglyceride.

scholarly journals Characterization of a Pseudomonas putidaAllylic Alcohol Dehydrogenase Induced by Growth on 2-Methyl-3-Buten-2-ol

1999 ◽  
Vol 65 (6) ◽  
pp. 2622-2630 ◽  
Author(s):  
Vincent F. Malone ◽  
Amy J. Chastain ◽  
John T. Ohlsson ◽  
Loelle S. Poneleit ◽  
Michele Nemecek-Marshall ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Benzyl Alcohol ◽  
Acinetobacter Calcoaceticus ◽  
Reduction Reaction ◽  
Terminal Sequence ◽  
Alcohol Dehydrogenases ◽  
Optimum Ph ◽  
Aromatic Alcohols ◽  
A Subunit

ABSTRACT We have been working to develop an enzymatic assay for the alcohol 2-methyl-3-buten-2-ol (232-MB), which is produced and emitted by certain pines. To this end we have isolated the soil bacteriumPseudomonas putida MB-1, which uses 232-MB as a sole carbon source. Strain MB-1 contains inducible 3-methyl-2-buten-1-ol (321-MB) and 3-methyl-2-buten-1-al dehydrogenases, suggesting that 232-MB is metabolized by isomerization to 321-MB followed by oxidation. 321-MB dehydrogenase was purified to near-homogeneity and found to be a tetramer (151 kDa) with a subunit mass of 37,700 Da. It catalyzes NAD+-dependent, reversible oxidation of 321-MB to 3-methyl-2-buten-1-al. The optimum pH for the oxidation reaction was 10.0, while that for the reduction reaction was 5.4. 321-MB dehydrogenase oxidized a wide variety of aliphatic and aromatic alcohols but exhibited the highest catalytic specificity with allylic or benzylic substrates, including 321-MB, 3-chloro-2-buten-1-ol, and 3-aminobenzyl alcohol. The N-terminal sequence of the enzyme contained a region of 64% identity with the TOL plasmid-encoded benzyl alcohol dehydrogenase of P. putida. The latter enzyme and the chromosomally encoded benzyl alcohol dehydrogenase ofAcinetobacter calcoaceticus were also found to catalyze 321-MB oxidation. These findings suggest that 321-MB dehydrogenase and other bacterial benzyl alcohol dehydrogenases are broad-specificity allylic and benzylic alcohol dehydrogenases that, in conjunction with a 232-MB isomerase, might be useful in an enzyme-linked assay for 232-MB.

Spectral Investigation on the Growth and Characterization of NLO Crystals of Thiourea Succinic Acid Single Crystal.

2015 ◽  
Vol 2 (2) ◽  
pp. 70-73
Author(s):  
Kannan.P ◽  
Thambidurai.S ◽  
Suresh.N
Keyword(s):  
Single Crystal ◽  
Succinic Acid ◽  
Slow Evaporation Technique ◽  
Absorption Studies ◽  
Dta Analysis ◽  
Evaporation Technique ◽  
Ft Ir ◽  
Ir Spectroscopic ◽  
Thermal Stability Of

Growth of optically transparent single crystals of thiourea succinic acid (TUSA) was grown successfully from aqueous solution by slow evaporation technique. The crystal structure was elucidated using the single crystal XRD. The various functional groups and the modes of vibrations were identified by FT-IR spectroscopic analysis. The optical absorption studies indicate that the optical transparency window is quite wide making its suitable for NLO applications. Thermal stability of the crown crystal carried out by TGA-DTA analysis.

Characterization of Different Types of Biomass Wastes Using Thermogravimetric and ICP-MS Analyses

2020 ◽  
Vol 70 (12) ◽  
pp. 4594-4600
Keyword(s):  
Thermogravimetric Analysis ◽  
Food Industry ◽  
Wood Waste ◽  
Biomass Ash ◽  
Minor Elements ◽  
Ms Analysis ◽  
Icp Ms ◽  
Different Types

The purpose of this study was to characterize some types of biomass wastes resulted from different activities such as: agriculture, forestry and food industry using thermogravimetric and ICP-MS analyses. Also, it was optimized an ICP-MS method for the determination of As, Cd and Pb from biomass ash samples. The ICP-MS analysis revealed that the highest concentration of metals (As, Cd, Pb) was recorded in the wood waste ash sample, also the thermogravimetric analysis indicated that the highest amount of ash was obtained for the same sample (26.82%). The biomass wastes mentioned in this study are alternative recyclable materials, reusable as pellets and briquettes. Keywords: ash, biomass, ICP-MS, minor elements, TG

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