scholarly journals Characterization of amylase and protease activity in the digestive tract of two teleosts (Labeo rohita and Anabas testudineus) with different feeding habits

2021 ◽  
Vol 64 (2) ◽  
pp. 173-179
Author(s):  
Sanjeet Debnath ◽  
Surjya Kumar Saikia
Keyword(s):  
Digestive Tract ◽  
Protease Activity ◽  
Specific Activity ◽  
Labeo Rohita ◽  
Feeding Habits ◽  
Anabas Testudineus ◽  
Pyloric Caeca ◽  
Optimum Ph ◽  
Optimum Ph And Temperature

Two teleosts (Rohu, Labeo rohita and Koi, Anabas testudineus), both with contrasting feeding habits (herbivorous versus carnivorous) were studied for amylase and protease activity concerning different regions of their digestive tracts. Significant differences in enzymatic activity across different regions of the digestive tracts were observed. Rohu, with three equal regions of the stomachless gut, showed the highest amylolytic activity at the posterior digestive tract but the highest proteolytic activity is limited to mid region. Contrary to such observation, Koi with three distinct regions of the digestive tract (stomach, pyloric caeca and intestine), the pyloric caeca exhibited the highest specific activity for both amylase and total protease. The optimum pH and temperature conditions were determined concerning the activity for both amylase and protease.

scholarly journals Morphohistology of the Digestive Tract of the Damsel FishStegastes fuscus(Osteichthyes: Pomacentridae)

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Bhaskara Canan ◽  
Wallace Silva do Nascimento ◽  
Naisandra Bezerra da Silva ◽  
Sathyabama Chellappa
Keyword(s):  
Digestive Tract ◽  
Transition Region ◽  
Digestive System ◽  
Feeding Habits ◽  
Northeastern Brazil ◽  
Muscular Layer ◽  
Pyloric Caeca ◽  
Anterior Intestine ◽  
The Mean ◽  
Tidal Pools

This study investigated the morphohistology of the digestive tract and the mean intestinal coefficient of the damsel fishStegastes fuscuscaptured from the tidal pools of Northeastern Brazil. The wall of the digestive tract ofS. fuscusis composed of the tunica mucosa, tunica muscularis, and tunica serosa. The esophagus is short with sphincter and thick distensible wall with longitudinally folded mucosa. Mucous glands are predominant, and the muscular layer of the esophagus presented striated fibers all along its extension. The transition region close to the stomach shows plain and striated muscular fibers. Between the stomach and intestine, there are three pyloric caeca. The intestine is long and thin with four folds around the stomach. The anterior intestine presents folds similar to those of pyloric caeca. The estimated mean intestinal coefficient and characteristics of the digestive system ofS. fuscuspresent morphological adequacy for both herbivorous and omnivorous feeding habits.

scholarly journals Purification and Characterization of Endoglucanase from local isolate of Aspergillus flavus

2013 ◽  
Vol 10 (3) ◽  
pp. 844-853
Author(s):  
Baghdad Science Journal
Keyword(s):  
Aspergillus Flavus ◽  
Specific Activity ◽  
Gel Filtration ◽  
Temperature Stability ◽  
Exchange Chromatography ◽  
Purification And Characterization ◽  
Original Activity ◽  
A Value ◽  
Optimum Ph

Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.

scholarly journals Partial purification and characterization of human erythrocyte phosphoglycollate phosphatase

1980 ◽  
Vol 191 (1) ◽  
pp. 117-124 ◽  
Author(s):  
R Zecher ◽  
H U Wolf
Keyword(s):  
Specific Activity ◽  
Total Activity ◽  
Partial Purification ◽  
Half Maximum ◽  
Purification And Characterization ◽  
Dimeric Molecule ◽  
Maximum Inhibition ◽  
Optimum Ph ◽  
Triton X

Human erythrocytes contain a phosphatase that is highly specific for phosphoglycollate. It shows optimum pH of 6.7 and has Km 1 mM for phosphoglycollate. The molecular weight appears to be about 72000. The enzyme is a dimeric molecule having subunits of mol. wt. about 35000. It could be purified approx. 4000-fold up to a specific activity of 5.98 units/mg of protein. The activity of the enzyme is Mg2+-dependent. Co2+, and to a smaller extent Mn2+, may substitute for Mg2+. Half-maximum inhibition of the phosphatase by 5,5′-dithiobis-(2-nitrobenzoate), EDTA and NaF is obtained at 0.5 microM, 1 mM and 4 mM respectively. Moreover, it needs a univalent cation for optimum activity. Phosphoglycollate phosphatase is a cytoplasmic enzyme. Approx. 5% of its total activity is membrane-associated. This part of activity can be approx. 70% solubilized by freezing, thawing and treatment with 0.25% Triton X-100.

Characterization of proteases from the digestive tract of sea cucumber (Stichopus japonicus): High alkaline protease activity

Aquaculture ◽  
2005 ◽  
Vol 246 (1-4) ◽  
pp. 321-329 ◽  
Author(s):  
Xue-yan Fu ◽  
Chang-hu Xue ◽  
Ben-chun Miao ◽  
Zhao-jie Li ◽  
Xin Gao ◽  
...  
Keyword(s):  
Digestive Tract ◽  
Alkaline Protease ◽  
Protease Activity ◽  
Sea Cucumber ◽  
Stichopus Japonicus

scholarly journals Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

2011 ◽  
Vol 83 (2) ◽  
pp. 599-609 ◽  
Author(s):  
Amanda R. Sena ◽  
Gildomar L.V. Júnior ◽  
Aristóteles Góes Neto ◽  
Alex G. Taranto ◽  
Carlos P. Pirovani ◽  
...  
Keyword(s):  
Specific Activity ◽  
Gel Filtration ◽  
Industrial Applications ◽  
Enzymatic Extract ◽  
Multivariate Statistical ◽  
Moniliophthora Perniciosa ◽  
Fermentation Time ◽  
Optimum Ph ◽  
Multivariate Statistical Approach

The enzyme glucanase from Moniliophthora perniciosa was produced in liquid medium and purified from the culture supernatant. A multivariate statistical approach (Response Surface Methodology - RSM) was employed to evaluate the effect of variables, including inducer (yeast extract) and fermentation time, on secreted glucanase activities M. perniciosa detected in the culture medium. The crude enzyme present in the supernatant was purified in two steps: precipitation with ammonium sulfate (70%) and gel filtration chromatography on Sephacryl S-200. The best inducer and fermentation time for glucanase activities were 5.9 g L-1 and 13 days, respectively. The results revealed three different isoforms (GLUI, GLUII and GLUIII) with purification factors of 4.33, 1.86 and 3.03, respectively. The partially purified enzymatic extract showed an optimum pH of 5.0 and an optimum temperature of 40°C. The enzymatic activity increased in the presence of KCl at all concentrations studied. The glucanase activity was highest in the presence of 0.2 M NaCl. The enzyme showed high thermal stability, losing only 10.20% of its specific activity after 40 minutes of incubation at 90°C. A purified enzyme with relatively good thermostability that is stable at low pH might be used in future industrial applications.

Post-proline endopeptidase. Partial purification and characterization of the enzyme from pig kidneys

1982 ◽  
Vol 47 (4) ◽  
pp. 1139-1148 ◽  
Author(s):  
Karel Hauzer ◽  
Linda Servítová ◽  
Tomislav Barth ◽  
Karel Jošt
Keyword(s):  
Specific Activity ◽  
Gel Filtration ◽  
Peptide Bond ◽  
Exchange Chromatography ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Optimum Ph ◽  
Hydrolysis Of ◽  
Prolyl Leucyl Glycinamide

Post-proline endopeptidase was isolated from pig kidneys and partially purified. The procedure consisted of fractionation with ammonium sulphate, ion exchange chromatography on DEAE-Sephadex A-50, gel filtration on Sephadex G-200 and rechromatography on DEAE-Sephadex A-50. The preparation had 55 times higher specific activity than the crude extract and did not contain any contaminating enzymic activities. The enzyme cleaved a number of proline-containing peptides and was strictly specific in catalyzing the hydrolysis of the peptide bond on the carboxyl side of the proline residue. The optimum pH for the hydrolysis of the synthetic peptides benzyl-oxycarbonylglycyl-prolyl-leucyl-glycinamide and benzyloxycarbonyl-glycyl-proline β-naphtylamide was 7.8-8.0 and, in the case of benzyloxycarbonylglycyl-proline p-nitroanilide, 7.2 to 7.5. For the hydrolysis of the tetrapeptide benzyloxycarbonylglycyl-prolyl-leucyl-glycinamide, the Km value of 75 μ mol l-1 was obtained.

scholarly journals Expression and characterization of Trichoderma reesei endoglucanase II in Pichia pastoris under the regulation of the GAP promoter

2020 ◽  
Vol 25 (2) ◽  
pp. 127
Author(s):  
Kezia Abib Yerah Tjandra ◽  
Kartika Sari Dewi ◽  
Asrul Muhamad Fuad ◽  
Trisanti Anindyawati
Keyword(s):  
Pichia Pastoris ◽  
Trichoderma Reesei ◽  
Specific Activity ◽  
Catalytic Efficiency ◽  
Endoglucanase Activity ◽  
Gap Promoter ◽  
Sds Page ◽  
Optimum Ph ◽  
High Concentrations

Trichoderma reesei is known to be one of the organisms capable for producing various types of cellulase in high concentrations. Among these cellulases, the highest catalytic efficiency of endoglucanases II (EGII, EC 3.2.1.4) are considered important for industrial application. The characterization of the EGII is necessary since it is widely used in high-temperature reactions in the industries. In this study, the recombinant EGII protein was expressed in Pichia pastoris and it has a molecular mass of approximately 52 kDa. Recombinant EGII was purified using Ni-NTA affinity chromatography and characterized by SDS-PAGE and western blot analyses. The enzyme activity of recombinant EGII was measured using the Nelson Somogyi method to determine its optimum pH and temperature. The result showed that the maximum EGII expression was achieved after 72 h of culture incubation. The crude enzyme has optimum activity at pH 5.0, resulting in 16.3 U/mL and 14.6 U/mL activity at 40 °C and 50 °C, respectively. While the purified enzyme gave the specific activity of 115.7 U/mg under the optimum condition. Finally, our study demonstrated that recombinant EGII could retain the endoglucanase activity for 89% and 80% at 40 °C and 50 °C, respectively.

scholarly journals Characterization of Endogenous Transglutaminase Enzyme of Yellow Pike Conger’s Liver

2017 ◽  
Vol 20 (3) ◽  
pp. 582
Author(s):  
Santhy Wisuda Sidauruk ◽  
Tati Nurhayati ◽  
Untung Trimo Laksono
Keyword(s):  
Food Processing ◽  
Food Industry ◽  
Specific Activity ◽  
Living Organism ◽  
Fish Liver ◽  
Food Processing Industry ◽  
Food Properties ◽  
Optimum Ph ◽  
Pharmacological Application

Transglutaminases have been found in various living organism, such as mammals, plants, <br />microorganisms, and marine organisms including fishes. Transglutaminases have many various functions<br />such as food properties, non-food properties and pharmacologies. This research aimed to characterize<br />transglutaminase that obtained from byproducts of yellow pike conger (Congresox talabon) such as<br />catadromous fish of yellow pike conger’s liver. The characteristic of transglutaminase had the possibility<br />to know the optimum condition in application of transglutaminase from liver of yellow pike conger such<br />as food processing industry, non-food industry and pharmacological application. A yield of yellow pike<br />conger’s liver was 0.88±0.11%. Specific activity of remang fish liver weighing 10 grams was 1,375 U/mg.<br />Characteristic crude transglutaminase from liver of yellow pike conger had optimum pH at 7.5; optimum<br />temperature at 50°C, transglutaminase activity increased on Mg<br />2+<br /> ion dependent and crude transglutaminase <br />had molecular weight of 27.48; 37.00; 69.51; 78.89; 88.18; 108.45; 134.10; dan 172.12 kDa.<br /><br />

scholarly journals Purification and characterization of versatile peroxidase from Lentinus squarrosulus and its application in biodegradation of lignocellulosics

2019 ◽  
Vol 6 (6) ◽  
pp. 280-286
Author(s):  
Aarthi Ravichandran ◽  
Ramya G Rao ◽  
Maheswarappa Gopinath ◽  
Manpal Sridhar
Keyword(s):  
Finger Millet ◽  
Nutritive Value ◽  
Crop Residues ◽  
Specific Activity ◽  
Gel Filtration ◽  
Versatile Peroxidase ◽  
Purification And Characterization ◽  
Optimum Ph ◽  
Km Value

Versatile Peroxidases are high redox potential peroxidases capable of degrading lignin of lignocellulosic crop residues. Hence Versatile Peroxidases are prominent biocatalysts in upgrading lignocellulosic biomass for biotechnological applications. In the interest of exploiting the potential of Versatile Peroxidase in improving the digestibility of crop residues through delignification, a novel Versatile Peroxidase was purified and characterized from the immobilized cultures of native isolate Lentinus squarrosulus. The enzyme was purified with a specific activity of 62 U/mg through ion exchange and gel filtration chromatographic procedures. The enzyme possessed high affinity towards RB5 and manganese with a Km value of 6.84 µM for RB5 and 0.15 mM for manganese. The optimum temperature for oxidation was identified to be 30°C and optimum pH for manganese and RB5 oxidation was 5 and 3 respectively. Reactivity of the enzyme towards diverse substrates was investigated besides studying the effect of metal ions and inhibitors on RB5 oxidation. The enhanced potential of this purified Versatile Peroxidase in biodegradation of crop residues was demonstrated through augmentation of digestibility of finger millet and paddy straws by 20%.The results demonstrated that Versatile Peroxidase from Lentinus squarrosulus is capable of enhancing the nutritive value of crop residues through delignification

scholarly journals Production and Characterization of Crude Protease from RS1 Isolate from silage of Floating Bladderwort (Utricularia gibba)

2020 ◽  
Vol 10 (3) ◽  
pp. 289-293
Author(s):  
Ace Baehaki ◽  
Arif Hidayat ◽  
Nuni Gofar ◽  
Rodiana Nopianti
Keyword(s):  
Molecular Weight ◽  
Production Time ◽  
Molecular Weights ◽  
Sds Page ◽  
Optimum Ph ◽  
Utricularia Gibba ◽  
Optimum Production ◽  
Optimum Ph And Temperature

The purpose of this research was to produce and characterizing crude protease from RS1 isolate of swamp plant silage. The optimum production time of RS1 isolate was 40 h. The optimum pH and temperature of protease from RS1 isolate were 10 and 45℃, respectively.  Ion Mg3+ increased RS1 protease whereas ion of Na+, K+, Fe2+, and Zn2+ inhibited protease from RS1 isolate. Study on the effect of metals ion indicated that protease from RS1 isolate was metaloenzyme. Based analysis on SDS-PAGE, the molecular weight of RS1 protease had 12 bands with molecular weights ranging from 34.75 kDa to 263.53 kDa.

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