scholarly journals Isolation and caracterization of ficin enzyme from Ficus septica Burm F stem latex

2017 ◽  
Vol 20 (2) ◽  
pp. 161
Author(s):  
Sri Wahyuni ◽  
R. Susanti ◽  
Retno Sri Iswari
Keyword(s):  
Enzyme Activity ◽  
Column Chromatography ◽  
Temperature Treatment ◽  
Optimum Temperature ◽  
Optimum Ph ◽  
Incubation Temperatures ◽  
Joint Treatment ◽  
Plant Latex

This research aims to isolate and characterize the fcin enzyme from Ficus septica stem latex. Ficin from Ficus septica stem latex was isolated using column chromatography. Then enzyme activity was tested at different temperature (40oC, 50oC, 60oC, 70oC) and pH (6.0, 7.0, 8.0) levels. Ficin enzyme activity of joint treatment with variations in temperature and pH was analyzed using two-way ANOVA with a factorial pattern followed by Least Signifcant Difference (LSD) test. The results showed that temperature treatment signifcantly affects enzyme activity. However, the treatment of pH and the interaction between temperature and pH did not signifcantly affect the fcin enzyme activity. There was no signifcant difference in fcin activity at the incubation temperatures of 40oC and 50oC, as well as 60oC and 70oC. However, comparing the incubation temperatures of 40oC and 50oC with treatment 60°C and 70°C showed a signifcant difference in fcin enzyme activity. In the treatment of incubation at pH 6, 7 and 8 for fcin enzyme activity showed no signifcant difference. We concluded that the Ficus septica plant latex contained fcin enzyme with an optimum temperature of 60°C and optimum pH of 6, 7, and 8.

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.

scholarly journals Characterization and Effects of β–Galactosidase in the Crude Extracts of Cuminum cyminum and Curcuma longa in Preparation of Delactosed Milk and Whey

2016 ◽  
Vol 5 (1) ◽  
pp. 1
Author(s):  
Omar M. Atrooz
Keyword(s):  
Enzyme Activity ◽  
Curcuma Longa ◽  
Maximum Activity ◽  
Cow’S Milk ◽  
Enzyme Kinetic ◽  
Optimum Temperature ◽  
Cuminum Cyminum ◽  
Crude Extracts ◽  
Optimum Ph ◽  
Hydrolysis Of

<p>β-galactosidase (EC 3.2.1.23) was extracted from <em>Cuminum cyminum </em>and<em> Curcuma longa</em>. The crude extracts of these plants were then characterized in term of pH, temperature, and enzyme kinetic. The crude extracts were also used in hydrolysis of lactose in milk and whey. The enzyme activity was measured by its ability to hydrolyze the substrate o-nitrophenyl β -D-galactopyranoside (ONPG).</p><p>It was found that β-galactosidase in the crude extracts of <em>Cuminum cyminum </em>exhibited maximum activity at pH 8.0 and optimum temperature at 60 °C. While, β-galactosidase in the crude extracts of <em>Curcuma longa</em> have optimum pH at 5.0 and 7.0 and optimum temperature at 50 °C.The K<sub>m</sub> and V<sub>max</sub> values of the β-galactosidase in the crude extracts of <em>Cuminum cyminum</em> and <em>Curcuma longa </em>were 4.16 mM and 0.087 μmol/min, and 2.63 mM and 0.333μmol/min, respectively.</p><p>The results showed that 96.84-97.08% of lactose was hydrolyzed in cow’s milk and whey when treated with crude extracts of <em>Cuminum cyminum</em> and 90-98.6% when treated with crude extracts of <em>Curcuma longa</em>.</p>

scholarly journals Purification, Characterization and De-Staining Potentials of a Thermotolerant Protease Produced by Fusarium oxysporum

2019 ◽  
Vol 64 (4) ◽  
pp. 539-547
Author(s):  
Mohammed Inuwa Ja’afaru ◽  
Konjerimam Ishaku Chimbekujwo ◽  
Obinna Markraphael Ajunwa
Keyword(s):  
Enzyme Activity ◽  
Fusarium Oxysporum ◽  
Treatment Time ◽  
Specific Activity ◽  
Total Yield ◽  
Tween 20 ◽  
Optimum Temperature ◽  
Industrial Enzymes ◽  
Sds Page ◽  
Optimum Ph

Proteases are important industrial enzymes and fungi prove to be good sources of such enzymes. Purification techniques are however necessary for increased specificity in activity and better industrial value. Based on this, a protease produced by a Fusarium oxysporum was purified to homogeneity by Sephadex G-200 column and α–casein agarose chromatography. The enzyme had a molecular weight of 70 kDa in SDS-PAGE. Purified Fusarium oxysporum protease had a specific activity of 93.88 U/mg protein. The purification magnitude was 7.7 and the total yield was 20 %. Purified protease had an optimum pH of 5.0 while the optimum temperature was 40 °C. The enzyme was also thermotolerant (approximately 100 % at 40 °C for 2 h). The enzyme activity was stimulated by surfactants and metal ions like, Tween-20 and Mg2+. Enzyme activity was inhibited in presence of PMSF and EDTA. Casein was found to be the best substrate for protease activity of Fusarium oxysporum FWT1. Protease were tested upon blood stain for de-clotting of blood and was found to exhibit good de-clotting and de-staining activity after 15 minutes treatment time.

Isolation and Identification of a Chitin Degrading Bacterium Aeromonas SP D5-23 and Properties of Chitinase

2012 ◽  
Vol 457-458 ◽  
pp. 472-475
Author(s):  
Jing Xuan Gou ◽  
Wen Bin Dong ◽  
Qiao Zeng ◽  
Lei Jin
Keyword(s):  
Enzyme Activity ◽  
Soil Sample ◽  
16S Rdna ◽  
Morphological Analysis ◽  
Chitinase Activity ◽  
Vibrio Alginolyticus ◽  
Optimum Temperature ◽  
Isolation And Identification ◽  
Degrading Bacterium ◽  
Optimum Ph

Chitin is an abundant biopolymer like cellulose that is rather resistant to degradation. In order to develop a bio-digesting method, soil sample in Qinling Mountain were collected for screening the bacteria with high chitinase activity by method of the transparent circle. The strain D5-23 was isolated and screened out from soil, which was found with amazing chitinase acitivity. The ratio of transient circle and colony circle is no less than 10. The strain was then identified as Aeromonas sp according to the sequences of 16S rDNA and morphological analysis. The enzyme activity was studied further, ,data shows that the optimum temperature was 45°C, which is similar to other Aeromonas sp, wheras the optimum pH is 5 and 9, which is more similar to Vibrio alginolyticus TK-22.

A Study of the Proteolytic Enzyme Activity of the Pyloric Caeca of Redfish

1953 ◽  
Vol 10 (8) ◽  
pp. 590-598 ◽  
Author(s):  
Joseph A. Stern ◽  
Ernest E. Lockhart
Keyword(s):  
Enzyme Activity ◽  
Proteolytic Activity ◽  
Intestinal Mucosa ◽  
Proteolytic Enzyme ◽  
Enzyme Preparation ◽  
Statistical Study ◽  
Optimum Temperature ◽  
Suitable Material ◽  
Pyloric Caeca ◽  
Optimum Ph

The proteolytic activity of an enzyme preparation from the pyloric caeca of redfish (Sebastes marinus) was studied and measured colorimetrically by the biuret reaction. The optimum temperature of this preparation was found to be 51–52 °C. A statistical study of the data showed the optimum pH to be 8.75, or slightly higher than the optimum pH of trypsin. A comparison of the actions of a commercial leather bate, hog intestinal mucosa, papain, pancreatin, trypsin and the caecal enzyme of redfish on casein led to the conclusion that the pyloric caeca of redfish would furnish a suitable material from which to prepare a leather bate.

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 Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242

1992 ◽  
Vol 288 (2) ◽  
pp. 475-482 ◽  
Author(s):  
I Ishii-Karakasa ◽  
H Iwase ◽  
K Hotta ◽  
Y Tanaka ◽  
S Omura
Keyword(s):  
Enzyme Activity ◽  
Culture Medium ◽  
Gel Filtration ◽  
Partial Purification ◽  
Gastric Mucus ◽  
Purification And Characterization ◽  
Streptomyces Sp ◽  
Optimum Ph ◽  
New Type

For the purification of a new type of endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242 (endo-GalNAc-ase-S) [Iwase, Ishii, Ishihara, Tanaka, Omura & Hotta (1988) Biochem. Biophys. Res. Commun. 151, 422-428], a method for assaying enzyme activity was established. Using purified pig gastric mucus glycoprotein (PGM) as the substrate, oligosaccharides liberated from PGM were pyridylaminated, and the reducing terminal sugars of oligosaccharides larger than Gal beta 1-3GalNAc were analysed by h.p.1.c. The crude enzyme of endo-GalNAc-ase-S was prepared as an 80% (w/v) ammonium sulphate precipitate from the concentrated culture medium. The enzyme was partially purified by gel chromatofocusing and subsequent DEAE-Toyopearl chromatography. Endo-enzyme activity eluted around pI 4.8 on a gel chromatofocusing column and eluted with 0.19-0.25 M-NaCl on a DEAE-Toyopearl column. In the enzyme fraction obtained, no exo-glycosidases or proteases could be detected. The molecular mass of the enzyme was estimated as 105 kDa by gel filtration, and the optimum pH was 5.5. Endo-GalNAc-ase-S hydrolysed the O-glycosidic linkage between GalNAc and Ser (Thr) in 3H-labelled and unlabelled asialofetuin, liberating both the disaccharide (Gal beta 1-3GalNAc) and the tetrasaccharide [Gal beta 1-3 (Gal beta 1-4GlcNAc beta 1-6)GalNAc]. When endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. (endo-GalNac-ase-A) was incubated with 3H-labelled and unlabelled asialofetuin, only the disaccharide (Gal beta 1-3GalNAc) was liberated.

Effect of temperature and pH on the production, activity, and stability of α-amylase from Bacillus subtilis V37

2021 ◽  
Vol 66 (1) ◽  
pp. 72-79
Author(s):  
Thuoc Doan Van ◽  
Hung Nguyen Phuc
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Animal Feed ◽  
Culture Conditions ◽  
Effect Of Temperature ◽  
Physical Parameters ◽  
Original Activity ◽  
Optimum Ph ◽  
Production Activity ◽  
Ph Range

The effect of physical parameters such as temperature and pH on the production, activity, and stability of α-amylase from Bacillus subtilis V37 was investigated. The results indicated that the optimum culture conditions for enzyme activity were pH 7.0 and 35 oC. The optimum pH and temperature for enzyme activity were 6.0 and 70 oC. The crude enzyme was found to be stable in the pH range of 5.0 to 7.0. The enzyme was stable for 1 h at a temperature from 30 to 80 oC; nearly 100% of enzyme activity remained at temperatures of 30 - 40 oC, and about 34% of original activity remained at a temperature of 80 oC. These features demonstrated that α-amylase from B. subtilis V37 can be applied in many areas such as the food, fermentation, and animal feed industries.

scholarly journals Properties of cytosolic components activating rat hepatic 5-deiodination in the presence of NADPH

1986 ◽  
Vol 234 (2) ◽  
pp. 391-398 ◽  
Author(s):  
K Sawada ◽  
B C W Hummel ◽  
P G Walfish
Keyword(s):  
Enzyme Activity ◽  
Glutathione Reductase ◽  
Rat Liver ◽  
Column Chromatography ◽  
Reduced Glutathione ◽  
Hydrogen Acceptor ◽  
Simultaneous Addition ◽  
Heat Stable ◽  
Hepatic Microsomes ◽  
Normal Rat

The effects of cytosol, NADPH and reduced glutathione (GSH) on the activity of 5′-deiodinase were studied by using washed hepatic microsomes from normal fed rats. Cytosol alone had little stimulatory effect on the activation of microsomal 5′-deiodinase. NADPH had no stimulatory effect on the microsomal 5′-deiodinase unless cytosol was added. 5′-deiodinase activity was greatly enhanced by the simultaneous addition of NADPH and cytosol (P less than 0.001); this was significantly higher than that with either NADPH or cytosol alone (P less than 0.001). GSH was active in stimulating the enzyme activity in the absence of cytosol, but the activity of 5′-deiodinase with 62 microM-NADPH in the presence of cytosol was significantly higher than that with 250 microM-GSH in the presence of the same concentration of cytosol (P less than 0.001). The properties of the cytosolic components essential for the NADPH-dependent activation of microsomal 5′-deiodinase independent of a glutathione/glutathione reductase system were further assessed using Sephadex G-50 column chromatography to yield three cytosolic fractions (A, B and C), wherein A represents pooled fractions near the void volume, B pooled fractions of intermediate Mr (approx. 13 000), and C of low Mr (approx. 300) containing glutathione. In the presence of NADPH (1 mM), the 5′-deiodination rate by hepatic washed microsomes is greatly increased if both A and B are added and is a function of the concentrations of A, B, washed microsomes and NADPH. A is heat-labile, whereas B is heat-stable and non-dialysable. These observations provide the first evidence of an NADPH-dependent cytosolic reductase system not involving glutathione which stimulates microsomal 5′-deiodinase of normal rat liver. The present data are consistent with a deiodination mechanism involving mediation by a reductase (other than glutathione reductase) in fraction A of an NADPH-dependent reduction of a hydrogen acceptor in fraction B, followed by reduction of oxidized microsomal deiodinase by the reduced acceptor (component in fraction B).

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.

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