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.

scholarly journals IMMOBILIZATION OF PAPAIN ON CHITOSAN

2010 ◽  
Vol 8 (3) ◽  
pp. 372-376
Author(s):  
Sari Edi Cahyaningrum ◽  
Narsito Narsito ◽  
Sri Juari Santoso ◽  
Rudiana Agustini
Keyword(s):  
Thermal Stability ◽  
Optimum Temperature ◽  
Ph Optimum ◽  
Optimum Ph ◽  
Thermal Stability Of

In this study, papain was immobilized on chitosan with Mg(II) cosslinked agent. Studies on free and immobilized papain systems for determination of optimum pH, optimum temperatur, thermal stability and reusability were carried out. The results showed that free papain had optimum pH 6.5 and optimum temperature 55 °C while the immobile papain hadoptimum pH 8 and optimum temperature 80 °C. The thermal stability of the immobilized papain, relative to that of the free papain, was markedly increased. The immobilized papain can be reused for at least six times.   Keywords: papain, immobilization, chitosan

scholarly journals SCREENING DAN KARAKTERISASI PEKTINESTERASE SEBAGAI ENZIM POTENSIAL DALAM KLARIFIKASI SARI BUAH JERUK KEPROK GARUT (Citrus nobilis var.chrysocarpa)

2015 ◽  
Vol 35 (04) ◽  
pp. 422
Author(s):  
Rohula Utami ◽  
Esti Widowati ◽  
Arifah Rahayu
Keyword(s):  
Thermal Stability ◽  
Optimum Temperature ◽  
Citrus Pectin ◽  
Ph Optimum ◽  
Citrus Juice ◽  
Optimum Ph ◽  
Km Value ◽  
Screening Result ◽  
Optimum Ph And Temperature

The objective of this research was screening of pectinesterase (PE) producing bacteria which are potential in clarification of keprok garut citrus juice (Citrus nobilis var microcarpa) and characterization of the resulted pectinesterase (optimum pH and temperature, pH and thermal stability, KM and Vmaks). The screening result showed that enzyme of isolates AR2, AR 4, AR 6, and KK 2 was found to be a potential enzyme for clarification of keprok garut citrus juice. Enzyme pektinesterase of isolates AR 2, AR 4, AR 6, and KK 2 had optimum pH at 8; 7.5; 8.5; and 6.5 and stable at pH 4-9, 4-9, 6-9, and 3-8. The optimum temperature enzyme of isolates AR 2 and AR 6 were 55ºC and that of AR 4 and KK 2 were 60ºC. Enzyme of isolate AR 2 was stable at 30-50ºC and inactive at 80ºC, AR 4 and KK 2 were stable at 30-60ºC and inactive at 90ºC whereas AR6 was stable at 30-60ºC and still wasn’t inactive at 90ºC. KM value of isolates AR 2, AR 4, AR 6, and KK 2 were 0.604; 0.338; 0.971; and 0.392 mg/ml. Vmaks value of isolates AR 2, AR 4, AR 6, and KK 2 were 1.218; 0.826; 0.969; and 1.080 u/ml. Pectinesterase enzyme of isolates KK 2 was found to be the most potential enzyme for clarification of keprok garut citrus juice.Keywords: Clarification, enzyme, keprok garut citrus, pectin, pectinesterase ABSTRAKTujuan dari penelitian ini adalah untuk melakukan screening bakteri penghasil enzim pektinesterase (PE) yang berpotensi dalam proses klarifikasi sari buah jeruk keprok garut (Citrus nobilis var microcarpa) serta mengetahui karakteristik enzim pektinesterase yang dihasilkan (pH optimum, suhu optimum, kestabilan pH dan suhu, serta nilai KMdan Vmaks). Hasil screening didapatkan isolat AR 2, AR 4, AR 6, dan KK 2 sebagai isolat penghasil enzim pektinesterase yang berpotensi dalam proses klarifikasi sari buah jeruk keprok garut. Aktivitas enzim pektinesterase isolat AR 2, AR 4, AR 6 dan KK 2 berturut-turut optimum pada pH 8; pH 7,5; pH 8,5; dan pH 6,5, serta stabil pada pH 4-9, pH4-9, pH 6-9, dan pH 3-8. Suhu optimum enzim pektinesterase isolat AR 2, AR 4, AR 6, dan KK 2 berturut-turut adalah 55ºC, 60ºC, 55ºC, dan 60ºC. Enzim pektinesterase isolat AR 2 stabil pada suhu 30-50ºC dan inaktif pada suhu 80ºC, enzim pektinesterase isolat AR 4 dan KK 2 stabil pada suhu 30-60ºC dan inaktif pada suhu 90ºC, sedangkan enzim pektinesterase isolat AR 6 stabil pada suhu 30-60ºC namun belum inaktif pada suhu 90ºC. Nilai konstanta Michaelis-Menten (KM) enzim pektinesterase isolat AR 2, AR 4, AR 6, dan KK 2 berturut-turut adalah 0,604; 0,338; 0,971; dan 0,392 mg/ml. Sedangkan nilai kecepatan maksimum (Vmaks) enzim pektinesterase isolat AR 2, AR 4, AR6, dan KK 2 berturut-turut adalah 1,218; 0,826; 0,969; dan 1,080 U/ml. Enzim pektinesterase isolat KK 2 memiliki karakteristik yang paling sesuai untuk aplikasi dalam klarifikasi sari buah jeruk keprok garut dibandingkan dengan enzim pektinesterase isolat lainnya.Kata kunci: Enzim, klarifikasi, pektin, pektinesterase, jeruk keprok garut

Rat liver L-threonine deaminase: Properties and purification

1985 ◽  
Vol 5 (6) ◽  
pp. 499-508 ◽  
Author(s):  
R. Leoncini ◽  
R. Pagani ◽  
A. Casella ◽  
E. Marinello
Keyword(s):  
Thermal Stability ◽  
Rat Liver ◽  
Competitive Inhibitor ◽  
New Method ◽  
Optimum Temperature ◽  
Temperature Optimum ◽  
Threonine Deaminase ◽  
Ph Optimum ◽  
Carbonate Ions

A new method of purification of rat liver L-threonine deaminase has been developed, and the results obtained are compared with values obtained by other authors. Some properties of this enzyme (pH optimum, temperature optimum, thermal stability, specificity, etc.) have been examined and we found that the enzyme is inhibited by carbonate ions, that L-cysteine (a competitive inhibitor) is also an inactivator of the enzyme and that it is bound to the enzyme in a ratio of 0.25 mole of cysteine per mole of enzyme, supporting the hypothesis that the enzyme consists of 4 subunits.

Regulation of acetyl-CoA carboxylase by glucagon in HeLa cells

1985 ◽  
Vol 5 (6) ◽  
pp. 491-497
Author(s):  
R. P. Bhullar ◽  
K. Dakshinamurti
Keyword(s):  
Thermal Stability ◽  
Rat Liver ◽  
Hela Cells ◽  
Competitive Inhibitor ◽  
Acetyl Coa Carboxylase ◽  
Optimum Temperature ◽  
Temperature Optimum ◽  
Threonine Deaminase ◽  
Ph Optimum ◽  
Carbonate Ions

A new method of purification of rat liver L-threonine deaminase has been developed, and the results obtained are compared with values obtained by other authors. Some properties of this enzyme (pH optimum, temperature optimum, thermal stability, specificity, etc.) have been examined and we found that the enzyme is inhibited by carbonate ions, that L-cysteine (a competitive inhibitor) is also an inactivator of the enzyme and that it is bound to the enzyme in a ratio of 0.25 mole of cysteine per mole of enzyme, supporting the hypothesis that the enzyme consists of 4 subunits.

scholarly journals Imobilisasi Enzim Lipase Dedak Padi (Oryza Sativa L.) Pada Karbon Aktif: Karakterisasi, dan Uji Stabilitas Kerja Enzim Imobil

2017 ◽  
Vol 5 (1) ◽  
pp. 32-36 ◽  
Author(s):  
Firdaus Firdaus ◽  
Seniwati Dali ◽  
Hendra J. Rusman
Keyword(s):  
Thermal Stability ◽  
Oryza Sativa L ◽  
Carbon Matrix ◽  
Enzyme Characterization ◽  
Relative Activity ◽  
Ph Optimum ◽  
Repeated Use ◽  
The Stability ◽  
Matrix Enzyme

This research aims to immobilization; characterize the enzyme of immobilized, test the effectiveness of the enzyme of immobilized. This research begins with the immobilization to process of enzyme lipase using activated carbon matrix, enzyme characterization covering of immobile determination of temperature and pH optimum of the enzyme of immobilized, as well as test the stability of work covering immobilized of enzyme the test thermal stability and repeated use. The results showed that the immobile of enzyme work optimally at 50oC of temperature and pH 6.5 with each activity 0.040 U/mL; research results also showed that the immobile of enzyme has higher thermal stability in comparison with the free enzyme: with the relative activity of 57.50% at the time of 45 minutes of exposure and the exposure time at 47.50% at 75-105 minutes and it can be used as many as six times with the relative activity of 52.5% in 6 times of use.

scholarly journals Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes

2019 ◽  
Vol 42 ◽  
pp. e44498
Author(s):  
Fernanda Martins de Souza ◽  
Cleide Mara Faria Soares ◽  
Alvaro Silva Lima ◽  
Luciana Cristina Lins de Aquino Santana
Keyword(s):  
Thermal Stability ◽  
Aspergillus Niger ◽  
Thermal Inactivation ◽  
Physical Adsorption ◽  
Covalent Bonding ◽  
Point Of View ◽  
Thermal Stabilities ◽  
Optimum Ph ◽  
Hancornia Speciosa ◽  
Free Lipase

In this work, a “green” Aspergillus niger lipase obtained from the solid-state fermentation of Hancornia speciosa (“mangaba”) seeds was efficiently immobilised on polyethersulfone membranes (PES) by physical adsorption (PES-ADS-lipase) and covalent bonding (PES-COV-lipase) (immobilisation yields of 92 and 81%, respectively). The free lipase showed an optimum pH close to neutrality, while the biocatalysts displaced the pH to the alkaline region (optimum pH 9.0 and 11.0 for PES-ADS-lipase and PES-COV-lipase, respectively). The optimum temperature of free lipase was 55°C; however, a higher thermal stability occurred at 37°C. The PES-ADS-lipase and PES-COV-lipase showed lower optimum temperatures (37 and 45°C, respectively) but higher thermal stabilities at 45 and 55°C, respectively. The lower thermal inactivation constant and higher half-life of PES-COV-lipase at 55°C confirmed the efficiency of covalent bonding in maintaining the thermal stability of the enzyme. The Michaelis–Menten constant (Km) and maximum rate of reaction (Vmax) were also determined, and the biocatalysts showed higher affinities to substrates (lower Km values) than free lipase. In this work, the biocatalysts showed good catalytic properties with future potential applications in hydrolysis reactions. The use of a “green” lipase obtained from agroindustrial residue makes this product economically attractive from an industrial point of view.

Determination of Plasminogen by Means of a Chroniogenic Peptide Substrate

1975 ◽  
Author(s):  
P. Friberger ◽  
G. Axelsson ◽  
K. Korsan-Bengtsen
Keyword(s):  
Ionic Strength ◽  
Linear Relationship ◽  
Reaction Rate ◽  
High Rate ◽  
Chromogenic Substrate ◽  
Peptide Substrate ◽  
Ph Optimum ◽  
Optimum Ph ◽  
Slight Inhibition

Plasmin splits the chromogenic substrate B2-Phe-Val-Arg-pNA (S-2160, Bofors) at a relatively high rate. Standard plasmin in glycerol obtained from Nat. Inst, for Biol. Stand, and Contr., London, was tested in a system with Tris buffer of varying pH and ionic strength. The pH optimum for the reaction was found to be 7.4. Variations in ionic strength between 0.05–0.1 had insignificant influence but at higher ionic strength there was a slight inhibition. A linear relationship was found between plasmin and AOD/min. At optimum pH and a final substrate concentration of 0.2 mM 0.1 CTA unit corresponds to approximately 0.10 nkat. Purified plasminogen (AB Kabi, Stockholm, Sweden) in the concentrations 0.02–0.2 CU/ml was activated optimally with streptokinase (Kabikinase® ) in the concentrations 500–2000 IU/ml. Higher concentration gave inhibition. The activity of streptokinase activated plasminogen increased with a decreasing ionic strength. A linear relationship was found between streptokinase activated plasminogen and AOD/min. Approximately 3,000 Plong/units per ml of urokinase was needed to obtain the same activation as with optimal streptokinase concentration. The method has been used for determination of plasminogen in plasma. With final dilution of plasma in the range 1/20–1/200 activated by streptokinase (2000 IU/ml) in a system of pH 8.2, I = 0.05, a linear relationship was found between plasma dilution and AOD/min. The reproducibility in a series of tests is good (variation coefficient < 3%) and with insignificant interference by inhibitors. The determinations were easily carried out in a simple spectrometer (405 nm) and in an automatic reaction rate analyzer (LKB 8600, 410 nm).

scholarly journals A simple and reliable method for determination of optimum pH in coupled enzyme assays

BioTechniques ◽  
2020 ◽  
Vol 68 (4) ◽  
pp. 200-203
Author(s):  
Lee Bowman ◽  
Rachael Motamed ◽  
Paul Lee ◽  
Kadijah Aleem ◽  
Astha S Berawala ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Pyruvate Kinase ◽  
Enzyme Assay ◽  
Reliable Method ◽  
Enzyme Assays ◽  
Ph Optimum ◽  
Optimum Ph

Determination of the optimum pH in a coupled enzyme assay poses significant challenges because altering the pH of the reaction mixture can affect the performance of both enzymes. Here, we demonstrate a simple and reliable method to determine the pH optimum for pyruvate kinase using the pyruvate kinase/lactate dehydrogenase coupled enzyme assay. This simple and reliable method can be broadly adapted to determine the pH optimum for various enzymes that are assayed using a coupled enzyme assay.

scholarly journals SIFAT-SIFAT BIOKIMIAWI EKSTRAK KASAR LIPASE EKSTRASELULER DARI BAKTERI Azospirillum sp. JG3

Molekul ◽  
2009 ◽  
Vol 4 (2) ◽  
pp. 73 ◽  
Author(s):  
Puji Lestari ◽  
Santi Nur Handayani ◽  
Oedjijono Oedjijono
Keyword(s):  
Organic Solvents ◽  
Crude Extract ◽  
Biochemical Properties ◽  
Microbiology Laboratory ◽  
Optimum Temperature ◽  
Mild Conditions ◽  
Optimum Ph ◽  
Optimum Production ◽  
High Stereoselectivity

Lipases are valuable biocatalysts because they act under extremely mild conditions, are stable in organic solvents, show broad substrate specificity and exhibit high stereoselectivity. Lipases play important role in various industries such as detergent, cosmetics, flavor, pharmacy and synthesis of organic compounds. The increasing of lipases requirements in industries is goading research to get new lipases resources commited. One of potential lipase resource is Azospirillum sp.JG3 bacteria from Microbiology Laboratory of Biology Faculty University of Jenderal Soedirman. The specific targets of this research are to get crude extract of lipase and investigate its biochemical characteristics. The method used were rejuvenation of Azospirillum sp.JG3 bacteria, inoculum production, determination of optimum production time and bacterium growth phase, extraction and production of lipase to get crude extract, and characterization the biochemical properties of lipase crude extract. The research resulted that crude extract of lipase from Azospirillum sp.JG3 had optimum temperature at 40 °C and optimum pH at pH 7. The lipase was a metalloenzyme with Ca2+ as its cofactor. The lipase was stable in three organic solvents tested, (chloroform, n-hexane and ether).

scholarly journals Isolasi dan Karakterisasi Fitase dari Mikroba yang Terdapat pada Pupuk Kompos, Rumen Sapi, Ragi dan Tanah Sawah

2016 ◽  
Vol 7 (1) ◽  
pp. 14
Author(s):  
Prof. Dr.rer.nat. Sajidan
Keyword(s):  
Key Words ◽  
Complex Compound ◽  
Relative Activity ◽  
Luria Bertani ◽  
Crude Enzyme ◽  
Soy Sauce ◽  
Optimum Temperature ◽  
Ph Optimum ◽  
Optimum Ph

<div class="WordSection1"><p><em> </em></p><p><em>            This research was aimed to isolate and characterize  phytase from different source</em><em>s</em><em> of higger phosphat complex compound</em><em>s</em><em> (compost, cattle rumen, and yeast). Bacteria of phytase was isolated on Luria Bertani (LB) medium and it was incubated on 37 <sup>o</sup>C for 16 hours. Microbe from yeast was isolated on Pottato Dextrose Agar (PDA) medium. Crude enzyme from supernatant was extracted with centrifuge on 5.000 rpm for 5 minutes. Crude enzyme was characterized for optimum pH, temperature, and influence of matalo ion efector on relative activity of enzyme. B1 isolate from P88 compost had optimum relative activity on pH 5, temperature 50 <sup>o</sup>C and activator Zn<sup>2+</sup> (10<sup>-3</sup> and 10<sup>-4</sup> M). B2 Isolate from cattle rumen had optimum relative activity on pH 5, temperature 50 <sup>o</sup>C and activator Zn<sup>2+</sup> (10<sup>-3</sup> M) and Mg<sup>2+</sup> (10<sup>-4</sup> M). B3 isolated from soy sauce yeast had optimum relative activity on pH 5, temperature 60 <sup>o</sup>C, and  activators Mg<sup>2+</sup> (10<sup>-3 </sup>M) and, Fe<sup>2+</sup> (10<sup>-4</sup> M). B4 isolated from tempeh yeast had optimum relative activity on pH 5, temperature 50 <sup>o</sup>C and activators Mg<sup>2+</sup> (10<sup>-3 </sup>M) and Ca<sup>2+</sup> (10<sup>-4</sup> M).</em></p><p><strong><em> </em></strong></p><p><strong><em>Key words</em></strong><em>: phytase, optimum pH, optimum temperature, metalo ion efector, isolate.</em></p></div><strong><br clear="all" /> </strong>

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