scholarly journals PENGARUH EKSTRAK METANOL DAUN PEPAYA (Carica papaya L.) TERHADAP AKTIVITAS ENZIM LIPASE

KOVALEN ◽  
2017 ◽  
Vol 3 (3) ◽  
pp. 211
Author(s):  
Nurhaeni Nurhaeni ◽  
Ahmad Ridhay ◽  
Magfira Magfira
Keyword(s):  
Enzyme Activity ◽  
Lipase Activity ◽  
Incubation Time ◽  
Substrate Concentration ◽  
Goal Attainment ◽  
Carica Papaya ◽  
Methanol Extract ◽  
Ph Optimum ◽  
Lipase Enzyme ◽  
Optimum Ph

Has conducted research on the effects of methanol extract of leaves papaya (Carica papaya L.) Against Lipase Enzyme Activity. This study aimed to obtain information in a methanol extract inhibits lipase activity. The method used is Complete Random Design (RAL), with goal attainment is done by determining the incubation time lipase enzyme, pH optimum lipase enzyme, and maximum substrate concentration lipase enzyme. And determining the effect of the methanol extract to inhibit the lipase enzyme activity. The results showed that the best incubation time of lipase obtained by time of 120 minutes, the optimum pH 7 and the maximum substrate concentration of 4%. With the highest activity were obtained 16.94 mol /ml.menit, 13.33 mol / ml.menit, and 12.89 mol / ml.menit. The methanol extract of papaya leaves can inhibit the lipase enzyme activity the best concentration of 2% with the acquisition activity of 3.67 mol/ml.menit.Keyword: papaya, lipase, incubation time, optimum pH, substrate concentration.

β-GLUCURONIDASE OF RABBIT POLYMORPHONUCLEAR LEUCOCYTES

1950 ◽  
Vol 28e (3) ◽  
pp. 69-79 ◽  
Author(s):  
R. J. Rossiter ◽  
Esther Wong
Keyword(s):  
Enzyme Activity ◽  
Blood Plasma ◽  
Substrate Concentration ◽  
Final Concentration ◽  
White Cell ◽  
Polymorphonuclear Leucocytes ◽  
Michaelis Constant ◽  
Glucuronidase Activity ◽  
Arsanilic Acid ◽  
Optimum Ph

Rabbit polymorphonuclear leucocytes contain an enzyme capable of hydrolyzing biosynthetic phenolphthalein mono-β-glucuronide. The concentration of the enzyme in the white cell is some 2000 times the concentration of the enzyme in the blood plasma. Under the conditions of study, the β-glucuronidase activity was proportional to the concentration of the enzyme. The effect of substrate concentration on the enzyme activity was studied and the Michaelis constant, Ks, determined. The course of the reaction was linear with time for the first 12 hr. and then fell off slightly during the next 12 hr. The optimum pH of the enzyme was 4.45 in either 0.2 M acetate or 0.2 M phthalate buffer. It was not inhibited by cyanide, azide, iodoacetate, fluoride, glycine, thiourea, urethane, arsanilic acid, acetophenone, o-cresol or m-cresol, in a final concentration of 0.01 M. The possible function of β-glucuronidase in rabbit polymorphonuclear leucocytes is discussed.

scholarly journals Optimasi produksi diasilgliserol dari crude palm oil menggunakan lipase spesifik 1,3-gliserida dari Rhizopus oryzae TP-2 Optimation of diacylglycerol production from crude palm oil using specific lipase of 1,3-glyceride from Rhizopus oryzae TP-2

2016 ◽  
Vol 79 (1) ◽  
Author(s):  
. SUHARYANTO ◽  
. TRI-PANJI ◽  
Urip PERWITASARI
Keyword(s):  
Diabetes Mellitus ◽  
Palm Oil ◽  
Crude Extract ◽  
Incubation Time ◽  
Rhizopus Oryzae ◽  
High Price ◽  
Crude Palm Oil ◽  
Ph Optimum ◽  
Lipase Enzyme ◽  
Daily Food

AbstractModern lifestyle caused the increasing prevalence ofobesity that precedes degenerative disease such as coronarycardiovascular disease, hypercholesterolemia, stroke, anddiabetes mellitus. Use of healthy oil in the daily food diet couldreduce the risk of the disease. One of healthy oils that proved tobe useful for human health is diacylglycerol (DAG).Unfortunately, production of DAG in Indonesia is hampered bythe relatively high price of the lipase enzyme. To overcome theprovision of costly imported lipase in producing DAG, aresearch was conducted by employing crude extract of lipaseenzyme from an indigenous mold namely Rhizopus oryzaeTP-2. Crude extract of lipase enzyme from mycelium culturefiltrate was freeze dryed and used for crude palm oil (CPO)bioconversion through glycerolysis at various processcondition. The objective of this research was to determineoptimum variable of temperature, incubation time, amount ofsubstrate and pH in producing DAG from CPO using lipase ofR. oryzae TP-2. The reseach result showed that lipase fromR. oryzae TP-2 was proved to be specific at position of 1,3-glyceride as indicated by glycerolysis products i.e DAG/TAGratio 0.48 higher than that of FFA/TAG ratio 0.06. Optimumconditions for glycerolysis were at temperature 37 o C, pH 7,3 g of CPO substrate, and 18 hours of incubation time. DAGyield by this optimum condition reach as much as 20.76 % w/w.The lipase derived from this experiment produced DAG betterthan that of using imported commercially lipase enzyme ofRhizomucor meihei.AbstrakGaya hidup modern telah menyebabkan meningkatnyakasus kegemukan yang berdampak timbulnya berbagaipenyakit degeneratif seperti jantung koroner, hiper-kolesterolemia, stroke dan diabetes mellitus. Penggunaanminyak sehat (healthy oil) sebagai menu diet sehari-hari dapatmengurangi faktor risiko penyakit tersebut. Salah satu jenisminyak sehat yang terbukti berdampak positif pada kesehatanmanusia adalah diasilgliserol (DAG). Sayangnya, produksiDAG di Indonesia terkendala oleh mahalnya enzim lipasespesifik 1,3-gliserida yang masih harus diimpor. Untukmengatasi mahalnya enzim lipase impor dalam produksi DAGdari CPO, penelitian penggunaan ekstrak kasar lipase darikapang lokal Rhizopus oryzae TP-2 telah dilakukan. Ekstrakkasar lipase dari filtrat kultur miselium R. oryzae TP-2dikeringbekukan dan digunakan untuk biokonversi CPOmelalui proses gliserolisis pada berbagai kondisi reaksi.Penelitian bertujuan menetapkan peubah suhu, waktu, jumlahsubstrat dan pH optimum dalam produksi DAG menggunakanlipase dari R. oryzae TP-2. Hasil penelitian menunjukkanbahwa enzim lipase R. oryzae TP-2 bersifat spesifik1,3-gliserida yang ditunjukkan oleh nisbah DAG/TAG, yaitu0,48 lebih besar dari nisbah ALB/TAG yaitu sebesar 0,06.Kondisi optimum untuk gliserolisis CPO adalah waktu inkubasiselama 18 jam, suhu reaksi 37°C, jumlah substrat CPO 3 g, danpH reaksi 7. Hasil DAG pada kondisi optimum gliserolisisadalah 20,76 %. (b/b). Lipase R. oryzae TP-2 yang digunakandalam penelitian ini menghasilkan DAG lebih tinggi dari padalipase impor asal Rhizomucor meihei.

scholarly journals Valorisasi Pankreas Ikan Tongkol (Eutynnus Affinis) Untuk Produksi Enzim Lipase

Elkawnie ◽  
2018 ◽  
Vol 4 (2) ◽  
Author(s):  
Vivi Mardina ◽  
Fitriani Fitriani ◽  
Tisna Harmawan ◽  
Goldha Maulla Hildayani
Keyword(s):  
Environmental Pollution ◽  
Protein Concentration ◽  
Ph Optimum ◽  
Promising Technology ◽  
Fisheries Resources ◽  
Lipase Enzyme ◽  
Optimum Ph ◽  
Euthynnus Affinis

Indonesia khususnya Aceh kaya dengan sumber daya kelautan dan perikanan seperti ikan tongkol (Euthynnus affinis). Valorisasi jeroan ikan tongkol sebagai sumber enzim lipase menjadi teknologi yang menjanjikan pada bidang bioteknolgi. Pada penelitian ini, pankreas dari jeroan ikan tongkol diekstraksi sebagai sumber kasar enzim cair lipase dan dikarakterisasi pH optimumnya. Hasil penelitian menunjukkan bahwa konsentrasi protein pada pankreas ikan tongkol adalah 4.615 mg/ml. Enzim lipase yang diperoleh memiliki aktivitas berkisar antara pH 4 -  9, dengan pH optimum pada pH 9 dan nilainya mencapai 11.962 U/ml. Dengan demikian, penelitian ini diharapkan menjadi salah satu cara untuk mengkonversi jeroan ikan tongkol menjadi produk yang bernilai ekonomi dan aplikatif serta meminimalisir pencemaran lingkungan yang disebabkan oleh limbah perikanan.Indonesia particularly Aceh, is rich in marine and fisheries resources such as tongkol (Euthynnus affinis). Valorization of tuna’s viscera as a source of lipase enzymes is a promising technology in biotechnology. In this study, the pancreas from tuna’s viscera was extracted for the production of lipase enzyme and characterized by its optimum pH. The results showed that the protein concentration of pancreas was 4,615 mg/ml. The lipase enzyme has activity ranging from pH 4 - 9, with an optimum at pH 9 and reaches 11.962 U/ml. Thus, this research is expected to be one way to convert tuna’s viscera into the product that was economic, applicative and minimize environmental pollution caused by fishery waste.

scholarly journals Fermentasi Kelapa Parut Bebas Protein dengan Aspergillus niger untuk Menghasilkan Lipase

KOVALEN ◽  
2020 ◽  
Vol 6 (1) ◽  
pp. 45-52
Author(s):  
Rifka Aulia ◽  
Syaiful Bahri ◽  
Meryany Ananda
Keyword(s):  
Enzyme Activity ◽  
Aspergillus Niger ◽  
Water Content ◽  
Incubation Time ◽  
Fermentation Medium ◽  
Enzyme Extract ◽  
Enzyme Protein ◽  
Lipase Enzyme ◽  
Randomized Design ◽  
Completely Randomized Design

The research about the fermentation of protein-free grated coconut with Aspergillus niger to produce of crude lipase enzyme has been carried out. This study aims to determine the effect of water content on fermentation medium and the incubation time which results lipase enzyme extract with the highest activity. This study used a Completely Randomized Design (CRD) consisting of 2 factors, i.e. variations of water content in medium of 40%, 50%, 60%, and 70% and incubation times of 48, 96, 144, and 192 hours. The parameters observed were lipase enzyme activity produced in each treatment. The results showed that the highest medium water content was 70% with the lipase enzyme activity 4.33 µmol/mL.minute and the best incubation time was 96 hours with the lipase enzyme activity of 0.83 µmol/mL.minute. Keywords: Lipase enzyme, protein-free grated coconut, Aspergillus niger

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%.

scholarly journals PRODUKSI DAN PENENTUAN KONDISI OPTIMUM ENZIM XILANASE Bacillus amyloliquefaciens FUKUMOTO PADA SUBSTRAT XILAN JERAMI

2015 ◽  
Vol 2 (1) ◽  
pp. 74
Author(s):  
Widiyanti Sekatresna ◽  
Abdi Dharma ◽  
Periadnadi
Keyword(s):  
Enzyme Activity ◽  
Rice Straw ◽  
Incubation Time ◽  
Substrate Concentration ◽  
Bacillus Amyloliquefaciens ◽  
Specific Activity ◽  
Enzymatic Reaction ◽  
Optimal Conditions ◽  
Enzyme Specific Activity

 ABSTRACT The production and determination of  optimal condition of xylanase produced by Bacillus amyloliquefaciens on rice straw xylan were investigated in this study. The parameters to be observed were optimal conditions of pH, temperature, substrate concentration and incubation time. Xilanase activity was determined by measuring the amount of reducing sugar formed in the enzymatic reaction based on Somogyi Nelson method. Optimal conditions needed for the production of xylanase were at pH 7, temperature 27°C and six days of incubation time. While optimal conditions of xylanase action were reached at pH 8.2, temperature 45°C, substrate concentration 3.5%(w/w) and 15 minutes of incubation time with enzyme activity and enzyme specific activity of 1.285 U/mL and 0.738 U/mg respectively. As a comparison, xylanase was also produced on pure xylan  (birchwood), enzyme activity and enzyme specific activity obtained were 2.701 U/mL and 1.658 U/mg respectively. Cellulase content in enzyme produced on rice straw xilan showed the enzyme activity of 0.094 U/mL.  Keywords : xylanase, Bacillus amyloliquefaciens, rice straw xilan

scholarly journals Optimasi produksi diasilgliserol dari crude palm oil menggunakan lipase spesifik 1,3-gliserida dari Rhizopus oryzae TP-2 Optimation of diacylglycerol production from crude palm oil using specific lipase of 1,3-glyceride from Rhizopus oryzae TP-2

2016 ◽  
Vol 79 (1) ◽  
Author(s):  
. SUHARYANTO ◽  
. TRI-PANJI ◽  
Urip PERWITASARI
Keyword(s):  
Diabetes Mellitus ◽  
Palm Oil ◽  
Crude Extract ◽  
Incubation Time ◽  
Rhizopus Oryzae ◽  
High Price ◽  
Crude Palm Oil ◽  
Ph Optimum ◽  
Lipase Enzyme ◽  
Daily Food

AbstractModern lifestyle caused the increasing prevalence ofobesity that precedes degenerative disease such as coronarycardiovascular disease, hypercholesterolemia, stroke, anddiabetes mellitus. Use of healthy oil in the daily food diet couldreduce the risk of the disease. One of healthy oils that proved tobe useful for human health is diacylglycerol (DAG).Unfortunately, production of DAG in Indonesia is hampered bythe relatively high price of the lipase enzyme. To overcome theprovision of costly imported lipase in producing DAG, aresearch was conducted by employing crude extract of lipaseenzyme from an indigenous mold namely Rhizopus oryzaeTP-2. Crude extract of lipase enzyme from mycelium culturefiltrate was freeze dryed and used for crude palm oil (CPO)bioconversion through glycerolysis at various processcondition. The objective of this research was to determineoptimum variable of temperature, incubation time, amount ofsubstrate and pH in producing DAG from CPO using lipase ofR. oryzae TP-2. The reseach result showed that lipase fromR. oryzae TP-2 was proved to be specific at position of 1,3-glyceride as indicated by glycerolysis products i.e DAG/TAGratio 0.48 higher than that of FFA/TAG ratio 0.06. Optimumconditions for glycerolysis were at temperature 37 o C, pH 7,3 g of CPO substrate, and 18 hours of incubation time. DAGyield by this optimum condition reach as much as 20.76 % w/w.The lipase derived from this experiment produced DAG betterthan that of using imported commercially lipase enzyme ofRhizomucor meihei.AbstrakGaya hidup modern telah menyebabkan meningkatnyakasus kegemukan yang berdampak timbulnya berbagaipenyakit degeneratif seperti jantung koroner, hiper-kolesterolemia, stroke dan diabetes mellitus. Penggunaanminyak sehat (healthy oil) sebagai menu diet sehari-hari dapatmengurangi faktor risiko penyakit tersebut. Salah satu jenisminyak sehat yang terbukti berdampak positif pada kesehatanmanusia adalah diasilgliserol (DAG). Sayangnya, produksiDAG di Indonesia terkendala oleh mahalnya enzim lipasespesifik 1,3-gliserida yang masih harus diimpor. Untukmengatasi mahalnya enzim lipase impor dalam produksi DAGdari CPO, penelitian penggunaan ekstrak kasar lipase darikapang lokal Rhizopus oryzae TP-2 telah dilakukan. Ekstrakkasar lipase dari filtrat kultur miselium R. oryzae TP-2dikeringbekukan dan digunakan untuk biokonversi CPOmelalui proses gliserolisis pada berbagai kondisi reaksi.Penelitian bertujuan menetapkan peubah suhu, waktu, jumlahsubstrat dan pH optimum dalam produksi DAG menggunakanlipase dari R. oryzae TP-2. Hasil penelitian menunjukkanbahwa enzim lipase R. oryzae TP-2 bersifat spesifik1,3-gliserida yang ditunjukkan oleh nisbah DAG/TAG, yaitu0,48 lebih besar dari nisbah ALB/TAG yaitu sebesar 0,06.Kondisi optimum untuk gliserolisis CPO adalah waktu inkubasiselama 18 jam, suhu reaksi 37°C, jumlah substrat CPO 3 g, danpH reaksi 7. Hasil DAG pada kondisi optimum gliserolisisadalah 20,76 %. (b/b). Lipase R. oryzae TP-2 yang digunakandalam penelitian ini menghasilkan DAG lebih tinggi dari padalipase impor asal Rhizomucor meihei.

scholarly journals LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE

2019 ◽  
Vol 20 (1) ◽  
pp. 12-23
Author(s):  
Maan Alkhatib ◽  
Nik Adlin Bahrudin ◽  
HAMZAH M. SALLEH ◽  
Mohamed M. E. Nasef ◽  
Teo M. Ting
Keyword(s):  
Enzyme Activity ◽  
Storage Stability ◽  
Immobilized Enzyme ◽  
Immobilized Lipase ◽  
Enzyme Concentration ◽  
Free Enzyme ◽  
Effect Of Temperature ◽  
Ph Optimum ◽  
Lipase Enzyme ◽  
Central Composite

ABSTRACT: Lipase enzyme originated from wheat germ was immobilized on nylon -6- grafted with polyglycidyl methachrylate (PGMA). The immobilization of enzyme experiments were designed and studied using face centred central composite design (FCCCD) under response surface methodology (RSM). Prior to immobilization, the polymer was activated with diethyl amine/ethanol to introduce an amine functional group to facilitate covalent bonding with the enzyme. The immobilized and free enzymes were characterized for effect of temperature and pH on enzyme activity, stability, storage and reusability as well as kinetics studies. ANOVA revealed that optimum lipase activity of 0.287 U/ml was achieved at immobilization time of 5 h, pH of 6 and 1.0 mg/ml for enzyme concentration. The optimum temperatures and pH for immobilized and free enzymes were 45 °C and 35 °C, and 8 and 7, respectively. The immobilized enzyme showed higher stability compared to free enzyme. The immobilized enzyme retained 18% of its activity after being recycled 8 times. In a storage stability test, immobilized lipase was able to retain 70% of its activity after being stored for 30 days, while free enzyme activity dropped to 15 % after 20 days of storage. ABSTRAK:Enzim Lipase telah dihasilkan daripada mikroorganisma pegun gandum di atas nilon -6- dan digraf bersama poliglisidel methakrilet (PGMA). Enzim pegun ini direka dan dikaji secara eksperimen menggunakan reka bentuk campuran pusat pada permukaan (FCCCD) di bawah kaedah tindak balas permukaan (RSM). Sebelum menjadi pegun, polimer ini telah diaktifkan dengan dietil amine/ethanol bagi menghasilkan kumpulan fungsi amine bagi membantu ikatan kovalen atom pada enzim. Enzim pegun dan bebas ini telah dikategorikan mengikut kesan enzim ke atas suhu, aktiviti enzim ke atas kesan pH, kestabilan, keboleh-simpanan dan keboleh-gunaan balik, serta ujian tindak balas kinetik. ANOVA membuktikan bahawa aktiviti optimum enzim lipase ini adalah sebanyak 0.287 U/ml telah terhasil selama 5 jam pegun, pada pH 6 dan kepekatan enzim sebanyak 1.0 mg/ml. Suhu dan pH optimum, pada enzim pegun dan enzim bebas ini adalah pada 45 °C dan 35 °C, dan pH 8 dan 7, masing-masing. Enzim pegun ini menunjukkan lebih stabil daripada enzim bebas. Enzim pegun dilihat kekal 18% daripada aktivitinya selepas 8 kali ulangan. Melalui ujian kestabilan simpanan, enzim lipase pegun dapat mengekalkan 70% daripada aktivinya selepas disimpan selama 30 hari, manakala aktiviti enzim bebas telah menurun kepada 15% selepas 20 hari dalam simpanan.

scholarly journals PRODUKSI ENZIM LIPASE DARI Aspergillus niger ISOLAT KAPANG KOPRA DENGAN MENGGUNAKAN MEDIUM KELAPA PARUT

KOVALEN ◽  
2017 ◽  
Vol 3 (3) ◽  
pp. 269
Author(s):  
Indah Indah ◽  
Mappiratu Mappiratu ◽  
Musafira Musafira
Keyword(s):  
Enzyme Activity ◽  
Aspergillus Niger ◽  
Water Content ◽  
High Activity ◽  
Incubation Time ◽  
Enzyme Production ◽  
Block Design ◽  
Lipase Enzyme ◽  
Randomized Block Design

The investigation about the lipase enzyme production from Aspergillus niger using grated coconut as a medium has been done. The aim of the study is to determine the best incubation time, pH and water content which produced lipase enzyme with high activity. Randomized Block Design (RBD) with 2 factorial pattern (incubation time and pH of the medium) was used in this research. Each factor consists of three levels and it was done in the triple. The level of incubation time and of pH were 48, 60, 72 hours and pH 5, 6, and 7, respectively. The observed parameter was the obtained lipase enzyme activity. The result showed that the highest activity was achieved at pH 7 for 48 hours of incubation time with 45% of water content. The amount of lipase enzyme activity was 1.70 µmol/ml.minutes.Keywords: mold coconut, Aspergillus niger, lipase

Dibutyryl cAMP-induced Increases in triacylglycerol lipase activity in developing L8 myotube cultures

1990 ◽  
Vol 68 (6) ◽  
pp. 689-693 ◽  
Author(s):  
Warren K. Palmer ◽  
Lawrence B. Oscai ◽  
Peter J. Bechtel ◽  
Glenn A. Fisher
Keyword(s):  
Enzyme Activity ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Culture Medium ◽  
Cultured Cells ◽  
Muscle Cells ◽  
Cell Types ◽  
Dibutyryl Camp ◽  
Ph Optimum ◽  
Triacylglycerol Lipase

Triacylglycerol (TG) lipase activity, with an alkaline pH optimum, has been identified in the cellular fraction of L8 myotube cultures. This TG lipase activity was stimulated by serum and inhibited by NaCl and protamine sulfate. These characteristics have been classically described for lipoprotein lipase. It was possible to increase the activity of this TG lipase three- to fivefold by incubating the cells with dibutyryl cAMP Maximal enzyme activity was observed 16 h following the addition of 10–100 μM dibutyryl cAMP to the cultured cells. Enzyme activity returned to control levels 24 h after removal of the nucleotide from the culture medium. Serum-sensitive alkaline TG lipase activity was also identified in five other myotube preparations of cultured muscle cells. The highest levels of activity were found in rat skeletal muscle primary, H9, and L6 cell types. The finding that dibutyryl cAMP is an effective inducer of alkaline TG lipase activity provides us with a valuable model to investigate mechanisms regulating synthesis, compartmentalization, and transport of lipoprotein lipase in muscle.Key words: lipoprotein lipase, cultured muscle cells, enzyme induction.

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