scholarly journals AKTIVITAS AMILASE, LIPASE DAN PROTEASE DARI CACING Peryonix excavatus

Molekul ◽  
2009 ◽  
Vol 4 (2) ◽  
pp. 115
Author(s):  
Ari Asnani ◽  
Puji Lestari
Keyword(s):  
Enzymatic Activity ◽  
Ammonium Sulphate ◽  
Crude Extract ◽  
Isolation Procedure ◽  
Optimum Temperature ◽  
Enzymes Activities ◽  
Optimum Ph ◽  
Ammonium Sulphate Fractionation

The ability of Peryonix excavatus to live in extremely dirty area indicates that P. excavatus secretes distinctive enzymes which might be useful for industry. Thus, this research were aimed to isolate amylase, lipase and protease from P. excavatus, and to characterize the enzymes to know the optimum temperature and pH. The isolation procedure consisted of extraction and ammonium sulphate fractionation. The results showed that crude extract and ammonium sulphate fractions of P.excavatus had amylase, lipase, and protease enzymes activities. Among the three enzymes, amylase had the highest enzymatic activity whereas lipase was the least. The optimum temperature of amylase, lipase and protease were 60, 40, and 60 oC, respectively. The optimum pH of amylase, lipase and protease were 7, 7, and 8, respectively.

STUDIES ON 17β-HYDROXYSTEROID DEHYDROGENASE IN HUMAN ENDOMETRIUM AND ENDOMETRIAL CARCINOMA

1975 ◽  
Vol 80 (2) ◽  
pp. 355-364 ◽  
Author(s):  
K. Pollow ◽  
H. Lübbert ◽  
B. Pollow
Keyword(s):  
Endometrial Carcinoma ◽  
Ammonium Sulphate ◽  
Isoelectric Focusing ◽  
Hydroxysteroid Dehydrogenase ◽  
Maximal Velocity ◽  
Optimum Temperature ◽  
Ammonium Sulphate Precipitation ◽  
Optimum Ph ◽  
Triton X ◽  
Secretory Endometrium

ABSTRACT Microsomal 17β-hydroxysteroid dehydrogenase obtained from the human secretory endometrium (17β-HSD) was solubilized with triton X-100. A 4-fold purification was achieved by ammonium sulphate precipitation and isoelectric focusing. In the presence of glycerol the partially purified enzyme was stable at 4°C for at least 48 h. Using crude microsomes, the conversion of oestradiol to oestrone was linear with time and with the concentration of protein. The optimum temperature was approximately 40°C and the optimum pH 9.4. For the reduction of oestrone the optimum pH was 6.5. With NAD, oestradiol was oxidized approximately three times more rapidly than with NADP. Km-values for oestradiol were nearly the same in endometrial carcinoma and in proliferative and secretory endometrium (i. e. approximately 3 × 10−6 m). The maximal velocity was highest in secretory endometrium. Testosterone and androstenedione could also serve as substrates but they were interconverted more slowly than oestradiol and oestrone. Sulphhydryl groups were shown to be essential for catalysis.

scholarly journals Isolasi, Pemurnian dan Karakterisasi Lipase Bakteri Hasil Skrining dari Tanah Tempat Pembuangan Akhir (TPA) Gunung Tugel Banyumas

2012 ◽  
Vol 12 (2) ◽  
pp. 124
Author(s):  
Zusfahair Zusfahair ◽  
Tien Setyaningtyas ◽  
Amin Fatoni
Keyword(s):  
Ammonium Sulfate ◽  
Lipase Activity ◽  
Crude Extract ◽  
Optimum Temperature ◽  
Production Time ◽  
Garbage Dump ◽  
Optimum Ph ◽  
Influence Of Ph ◽  
Optimum Production ◽  
Enzyme Characteristic

A bacterial lipase producer was isolated from garbage dump soil and was identified its genus. Lipase was extractedaccording to production time optimized, purified using ammonium sulfate fractionation and gel chromatograph.Determination of enzyme characteristic studied were influence of pH, temperature, various metals to lipaseactivity. The result of this research shows that the genus of isolated bacteria which produced lipase wasAcinetobacter sp., the lipase optimum production time is about 18 hours with the activity is about 115 unit/mL. Thehighest activity of lipase fractionation using ammonium sulfate is about 45% and the highest activity of purifyingwith filtration gel chromatograph column using Sephadex G-150 at 24 th fraction. Lipase from crude extract andpurifying product at this fraction has optimum pH 6 and optimum temperature is about 40 oC. Lipase to be classifiedas metalloenzyme that shows with decreasing the activity after added the EDTA. Metals ion, such as Cu 2+ and Zn2+were inhibited the lipase activity. Ca 2+ ion could increase lipase crude extract activity but inhibited the activity oflipase purifying product. Hg2+ ion could increase the activity of lipase purifying product.

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 EKSTRAK KASAR ENZIM BROMELIN DARI BATANG NANAS (Ananas comusus L.merr)

2006 ◽  
Vol 12 (1) ◽  
pp. 75-77
Author(s):  
Nuniek Herdyastuti
Keyword(s):  
Enzyme Activity ◽  
Crude Extract ◽  
Soluble Protein ◽  
Food Industry ◽  
Optimum Temperature ◽  
Ph Variation ◽  
Isolation And Characterization ◽  
Optimum Ph

Brommelain is an enzyme hydrolyze most soluble protein easily and efficiently. This enzyme is used in many industry like food industry. This research aimed to isolation and characterization crude extract brommelain. This enzyme has been extracted from the stems of pineapples to produce crude extract, precipitated with amonium sulfat, and enzyme activity to decided with Bergmeyer methode. The higher activity was 1,996 U/ml in precipitate 40-60 percent amonium sulfat. Optimum temperature and pH to decided temperature and pH variation was detected based on enzyme activity. Characterization to indicate that bromelain has an optimum temperature at 55°C, optimum pH of 7, KM = 5.074 mg/ml and Vmax = 0.666 mg/ml.second.

Bovine milk esterases

1971 ◽  
Vol 38 (2) ◽  
pp. 171-177 ◽  
Author(s):  
B. J. Kitchen
Keyword(s):  
Ammonium Sulphate ◽  
Bovine Milk ◽  
Skim Milk ◽  
Histochemical Staining ◽  
Major Type ◽  
Polyacrylamide Gels ◽  
Selective Inhibitors ◽  
Choline Ester ◽  
Ultra Filtration ◽  
Ammonium Sulphate Fractionation

SummaryThe type and distribution of esterases in milk has been investigated using selective inhibitors during normal assay procedures and during histochemical staining of polyacrylamide gels. Enzyme solutions were obtained from skim-milk by acid and alkali precipitation, followed by ammonium sulphate fractionation, ultra-filtration and Sephadex G-100 chromatography. The major type of esterase present was an aryl-esterase (E.C. 5.1.1.2) while a smaller amount of a choline-ester hydrolase (E.C. 3.1.1.7; 3.1.1.8) was detected. The significance of these findings is discussed.

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 Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors.

1980 ◽  
Vol 85 (2) ◽  
pp. 414-428 ◽  
Author(s):  
S D MacLean-Fletcher ◽  
T D Pollard
Keyword(s):  
Crude Extract ◽  
Cross Linking ◽  
Cross Link ◽  
Gelation Process ◽  
Optimum Ph ◽  
Kinetics Of ◽  
Low Shear

We have studied the kinetics of the gelation process that occurs upon warming cold extracts of Acanthamoeba using a low-shear falling ball assay. We find that the reaction has at least two steps, requires 0.5 mM ATP and 1.5 mM MgCl2, and is inhibited by micromolar Ca++. The optimum pH is 7.0 and temperature, 25 degrees-30 degrees C. The rate of the reaction is increased by cold preincubation with both MgCl2 and ATP. Nonhydrolyzable analogues of ATP will not substitute for ATP either in this "potentiation reaction" or in the gelation process. Either of two purified or any one of four partially purified Acanthamoeba proteins will cross-link purified actin to form a gel, but none can account for the dependence of the reaction in the crude extract on Mg-ATP or its regulation by Ca++. This suggests that the extract contains, in addition to actin-cross-linking proteins, factors dependent on Mg-ATP and Ca++ that regulate the gelation process.

scholarly journals Properties of a new fungal b-galactosidase with potential application in the dairy industry

1999 ◽  
Vol 30 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Rubens Cruz ◽  
Vinícius D'Arcádia Cruz ◽  
Juliana Gisele Belote ◽  
Marcelo de Oliveira Khenayfes ◽  
Claudia Dorta ◽  
...  
Keyword(s):  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Transferase Activity ◽  
Optimum Temperature ◽  
Milk Whey ◽  
Beneficial Effects ◽  
Optimum Ph ◽  
Semi Solid ◽  
Good Productivity ◽  
Hydrolysis Of

<FONT FACE="Symbol">b</font>-Galactosidase or <FONT FACE="Symbol">b</font>-D-galactoside-galactohydrolase (EC. 3.2.1.23) is an important enzyme industrially used for the hydrolysis of lactose from milk and milk whey for several applications. Lately, the importance of this enzyme was enhanced by its galactosyltransferase activity, which is responsible for the synthesis of transgalactosylated oligosaccharides (TOS) that act as functional foods, with several beneficial effects on consumers. Penicillium simplicissimum, a strain isolated from soil, when grown in semi-solid medium showed good productivity of <FONT FACE="Symbol">b</font>-galactosidase with galactosyltransferase activity. The optimum pH for hydrolysis was in the 4.04.6 range and the optimum pH for galactosyltransferase activity was in the 6.07.0 range. The optimum temperature for hydrolysis and transferase activity was 55-60°C and 50°C, respectively, and the enzyme showed high thermostability for the hydrolytic activity. The enzyme showed a potential for several industrial applications such as removal of 67% of the lactose from milk and 84% of the lactose from milk whey when incubated at their original pH (4.5 and 6.34, respectively) under optimum temperature conditions. When incubated with a 40% lactose solution in 150 mM McIlvaine buffer, pH 4.5, at 55°C the enzyme converted 86.5% of the lactose to its component monosaccharides. When incubated with a 60% lactose solution in the same buffer but at pH 6.5 and 50°C, the enzyme can synthetize up to 30.5% TOS, with 39.5% lactose and 30% monosaccharides remaining in the preparation.

scholarly journals Characterization of Biosynthetic Enzymes for Ectoine as a Compatible Solute in a Moderately Halophilic Eubacterium, Halomonas elongata

1999 ◽  
Vol 181 (1) ◽  
pp. 91-99 ◽  
Author(s):  
Hisayo Ono ◽  
Kazuhisa Sawada ◽  
Nonpanga Khunajakr ◽  
Tao Tao ◽  
Mihoko Yamamoto ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Apparent Molecular Mass ◽  
Optimum Temperature ◽  
Sds Page ◽  
Halomonas Elongata ◽  
Optimum Ph

ABSTRACT 1,4,5,6-Tetrahydro-2-methyl-4-pyrimidinecarboxylic acid (ectoine) is an excellent osmoprotectant. The biosynthetic pathway of ectoine from aspartic β-semialdehyde (ASA), in Halomonas elongata, was elucidated by purification and characterization of each enzyme involved. 2,4-Diaminobutyrate (DABA) aminotransferase catalyzed reversively the first step of the pathway, conversion of ASA to DABA by transamination with l-glutamate. This enzyme required pyridoxal 5′-phosphate and potassium ions for its activity and stability. The gel filtration estimated an apparent molecular mass of 260 kDa, whereas molecular mass measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was 44 kDa. This enzyme exhibited an optimum pH of 8.6 and an optimum temperature of 25°C and had Km s of 9.1 mM forl-glutamate and 4.5 mM for dl-ASA. DABA acetyltransferase catalyzed acetylation of DABA to γ-N-acetyl-α,γ-diaminobutyric acid (ADABA) with acetyl coenzyme A and exhibited an optimum pH of 8.2 and an optimum temperature of 20°C in the presence of 0.4 M NaCl. The molecular mass was 45 kDa by gel filtration. Ectoine synthase catalyzed circularization of ADABA to ectoine and exhibited an optimum pH of 8.5 to 9.0 and an optimum temperature of 15°C in the presence of 0.5 M NaCl. This enzyme had an apparent molecular mass of 19 kDa by SDS-PAGE and a Km of 8.4 mM in the presence of 0.77 M NaCl. DABA acetyltransferase and ectoine synthase were stabilized in the presence of NaCl (>2 M) and DABA (100 mM) at temperatures below 30°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.

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