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.

Characterisation of a Neutral Protease Produced by Micrococcus luteus

1996 ◽  
Vol 51 (5-6) ◽  
pp. 429-431 ◽  
Author(s):  
M.O. Ilori ◽  
O.O. Amund ◽  
O. Omidiji
Keyword(s):  
Molecular Weight ◽  
Citric Acid ◽  
Proteolytic Enzyme ◽  
Micrococcus Luteus ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Optimum Temperature ◽  
Optimum Ph

Abstract A proteolytic enzyme produced by a cassava-ferment­ing strain of Micrococcus luteus was extracted and puri­fied 50-fold by gel filtration and ion exchange chromatography. The optimum pH for the enzyme was 7.0, the optimum temperature 25 °C, the apparent molecular weight 42 kDa and the Km value, 0.45 mg ml-1 with casein as substrate. The enzyme was stimulated by Ca2+ and Mg2+ but inhibited by Zn2+ and Co2+ ions. Other inhibitors were EDTA, KCN, citric acid and L-cysteine indicating the enzyme to be a metalloprotease.

STUDIES ON THE EXTRACELLULAR PROTEOLYTIC ENZYMES OF RHIZOPUS OLIGOSPORUS

1965 ◽  
Vol 11 (4) ◽  
pp. 727-732 ◽  
Author(s):  
Hwa L. Wang ◽  
C. W. Hesseltine
Keyword(s):  
Proteolytic Activity ◽  
Wheat Flour ◽  
Proteolytic Enzyme ◽  
Proteolytic Enzymes ◽  
The Other ◽  
Soybean Flour ◽  
Rhizopus Oligosporus ◽  
Enzyme Systems ◽  
Culture Filtrates ◽  
Optimum Ph

Two proteolytic enzyme systems were observed in the culture filtrates of Rhizopus oligosporus. One has an optimum pH at 3.0; the other, at 5.5. Both enzyme systems have maximum activities at 50–55 °C and are fairly stable at pH 3.0–6.0. Maximum production of the enzymes occurred after 72 to 96 hours of incubation and then it decreased rapidly. Higher proteolytic activity was noted in the culture filtrates of the organism grown in wheat flour medium than in soybean flour. Data suggest that formation of the enzyme systems appears to be inhibited by soybean extracts.

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.

PURIFICATION AND PROPERTIES OF A PROTEASE FROM PENICILLIUM CYANEO-FULVUM

1960 ◽  
Vol 38 (1) ◽  
pp. 969-980 ◽  
Author(s):  
Kartar Singh ◽  
S. M. Martin
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Proteolytic Enzyme ◽  
Ethylenediaminetetraacetic Acid ◽  
Alkaline Proteases ◽  
Plasma Albumin ◽  
Metal Chelating ◽  
Bovine Plasma ◽  
Purification And Properties ◽  
Optimum Ph

A proteolytic enzyme present in culture filtrates of Penicillium cyaneo-fulvum was purified approximately 100-fold. In the ultracentrifuge the enzyme behaved as a homogeneous protein, but on electrophoresis some contamination was apparent. The molecular weight of the enzyme was estimated to be about 45,000.The protease hydrolyzed casein and denatured haemoglobin, gelatin, and native bovine plasma albumin but not native or denatured ovalbumin. It also coagulated milk. The optimum pH for caseolysis was 9.5 to 11.0. Metal chelating- and sulphydryl-reagents did not affect enzyme activity but zinc and mercurous ions inhibited the enzyme, the inhibition being reversed with ethylenediaminetetraacetic acid (EDTA). Soybean trypsin inhibitor was without effect on the enzyme whereas ovomucoid inhibited the enzyme. Although it is similar in some respects to other alkaline proteases, the P. cyaneo-fulvum enzyme does not appear to be identical with any one of them.

The development of the digestive system of the young animal IV. Proteolytic enzyme development in the young lamb

1959 ◽  
Vol 53 (3) ◽  
pp. 381-386 ◽  
Author(s):  
D. M. Walker
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Digestive System ◽  
Young Animal ◽  
Milk Clotting ◽  
Digestive Organs ◽  
Proteolytic Enzyme Activity ◽  
Enzyme Development

1. The digestive organs and contents of twelve lambs, varying in age from 1 to 5 weeks, have been examined for their proteolytic enzyme activity at pH 1·8, 3·5 and 8·5.2. Enzyme activity at 1·8 was present only in the abomasum and its contents.3. All tissues and contents examined were active on haemoglobin at pH 3·5.4. Small intestine contents and pancreas alone were active on azocasein at pH 8·5.5. The majority of tissues and contents increased their proteolytic activity with increase in age. The abomasum wall, however, increased in activity up to 21 days and thereafter decreased, both at pH 1·8 and 3·5.6. Milk-clotting action was measured on abomasum wall and contents. There was an absence of milk clots in the abomasum after 21 days, by which time rumen function had commenced.

scholarly journals PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES

1940 ◽  
Vol 23 (3) ◽  
pp. 275-288 ◽  
Author(s):  
Theodore Winnick ◽  
Alva R. Davis ◽  
David M. Greenberg
Keyword(s):  
Physicochemical Properties ◽  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Chemical Diffusion ◽  
Urea Solution ◽  
Optimum Temperature ◽  
Asclepias Speciosa ◽  
Clot Blood

1. A study has been made of the properties of a hitherto unreported proteolytic enzyme from the latex of the milkweed, Asclepias speciosa. The new protease has been named asclepain by the authors. 2. The results of chemical, diffusion, and denaturation tests indicate that asclepain is a protein. 3. Like papain, asclepain dots milk and digests most proteins, particularly if they are dissolved in concentrated urea solution. Unlike papain, asclepain did not clot blood. 4. The activation and inhibition phenomena of asclepain resemble those of papain, and seem best explained on the assumption that free sulfhydryl in the enzyme is necessary for proteolytic activity. The sulfhydryl of asclepain appears more labile than that of papain. 5. The measurement of pH-activity curves of asclepain on casein, ovalbumin, hemoglobin, edestin, and ovovitellin showed no definite digestion maxima for most of the undenatured proteins, while in urea solution there were well defined maxima near pH 7.0. Native hemoglobin and ovovitellin were especially undigestible, while native casein was rapidly attacked. 6. Temperature-activity curves were determined for asclepain on hemoglobin, casein, and milk solutions. The optimum temperature was shown to increase with decreasing time of digestion.

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.

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