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.

Isolation and Identification of Strains with High Chitin Deacetylase Activity

2012 ◽  
Vol 457-458 ◽  
pp. 476-479
Author(s):  
Jing Xuan Gou ◽  
Wen Bin Dong ◽  
Qiao Zeng ◽  
Jing Jing Zhang
Keyword(s):  
Food Industry ◽  
Analysis Data ◽  
Soil Samples ◽  
Optimum Temperature ◽  
Isolation And Identification ◽  
Chitin Deacetylase ◽  
Physiological And Biochemical Characteristics ◽  
Optimum Ph ◽  
Physiological And Biochemical ◽  
Rdna Analysis

Chitosan is an aboundant biopolymer like cellose. To bioprocess them with chitin deacetylase (CDA), the products will be used in medicine and food industry. [In order to get new strains with significant ability of (CDA) Twenty eight strains producing CDA were isolated and screened out from the soil samples by color reaction in plate medium. The strain F2-7-3 was screened out from these strains for the highest CDA activity, which can reach more than 250U/mL. The paranitroacetanilide was used as the substrate, the optimum temperature for enzyme activity was determined to be 50°C and the optimum pH was 7.0. It was studied by method of morphological, physiological and biochemical characteristics and 16S rDNA analysis. Data shows that the strain was Rhodococcus sp.

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>

Purification and Properties of Ribonuclease From Buffalo Milk Whey

1977 ◽  
Vol 40 (6) ◽  
pp. 375-377 ◽  
Author(s):  
AZZA A. ISMAIL ◽  
N. S. AHMED ◽  
M. A. KHORSHID
Keyword(s):  
Deae Cellulose ◽  
Ribonuclease A ◽  
Buffalo Milk ◽  
Optimum Temperature ◽  
Isolation And Identification ◽  
Milk Whey ◽  
Purification And Properties ◽  
Optimum Ph ◽  
Ribonuclease B

A procedure was developed for isolation and identification of ribonuclease from buffalo milk whey. Ribonuclease was precipitated with (NH4)2SO4 between 65 and 90% saturation. The precipitate was dissolved, dialyzed, and fractionated on DEAE-cellulose. Two ribonuclease-rich fractions were collected, i.e. ribonuclease A and B. Ribonuclease A had an optimum pH of 7 .0, and ribonuclease B had an optimum pH of 8.6. Both had an optimum temperature at 38 C. The ribonucleases in the purified state were unstable to heat and their activity decreased as the time of exposure increased. Both enzyme fractions were sensitive to inhibitors. NaCl and NaN3 were stimulatory for ribonuclease A, while ribonuclease B was stimulated only by NaCl.

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.

scholarly journals Production of N-acetylglucosamine from shrimp shells’ chitin using intracellular chitinase from Mucor circinelloides

Food Research ◽  
2020 ◽  
Vol 4 (5) ◽  
pp. 1582-1587
Author(s):  
Yuniwaty Halim ◽  
Fransiska ◽  
Hardoko ◽  
R. Handayani
Keyword(s):  
Incubation Period ◽  
Substrate Concentration ◽  
Chitinase Activity ◽  
Mucor Circinelloides ◽  
Optimum Temperature ◽  
Shrimp Shells ◽  
Incubation Periods ◽  
Optimum Ph ◽  
Substrate Concentrations ◽  
Optimum Ph And Temperature

Chitin is a natural biopolymer found in shrimp shells and can be processed into Nacetylglucosamine which is extensively used as a dietary supplement to treat osteoarthritis, back pain and knee pain. This research was conducted to determine the optimum pH, temperature, substrate concentration and incubation period to produce Nacetylglucosamine using crude and semi pure intracellular chitinase extracted from Mucor circinelloides. Chitinase activity was measured to determine optimum pH and temperature by using various pHs (3, 4, 5, 6, 7, 8 and 9) and temperatures (30oC, 40oC, 50oC, 60oC, 70oC and 80oC). Different substrate concentrations (0.5%, 1.0%, 1.5% and 2.0%) and incubation periods (2, 4, 6 and 24 hrs) were used to determine the optimum condition to produce N-acetylglucosamine. Results showed that crude intracellular chitinase had an optimum pH of 5 with chitinase activity of 4.16±0.07 U/mL and optimum temperature of 60oC with chitinase activity of 4.22±0.07 U/mL. The optimum substrate concentration obtained was 0.5% and the optimum incubation period obtained was 6 hrs with about 961.67±9.13 ppm N-acetylglucosamine produced. Semi pure intracellular chitinase had an optimum pH of 4 with chitinase activity of 4.75±0.09 U/mL and optimum temperature of 50oC with chitinase activity of 5.03±0.08 U/mL. The optimum substrate concentration obtained was 1.5% and the optimum incubation period obtained was 4 hrs with about 1150.56±12.55 ppm N-acetylglucosamine produced.

scholarly journals Staphylococcus Sp. Strain MY 83295F: A Potential P,P’-DDT-Degrading Bacterium Isolated from Pesticide Contaminated Soil

2020 ◽  
Vol 3 (2) ◽  
pp. 22-35
Author(s):  
Ya’u Murtala ◽  
Bennett C Nwanguma ◽  
Lawrence Us Ezeanyika
Keyword(s):  
16S Rrna ◽  
Environmental Degradation ◽  
Contaminated Soil ◽  
Gene Sequence ◽  
Phylogenetic Analyses ◽  
Optimum Temperature ◽  
Inhibitory Effects ◽  
Degrading Bacterium ◽  
Optimum Ph ◽  
Ecological Concern

AbstractAlthough DDT has been on the ban list by the Stockholm Convention for its environmental degradation, still a wave of emerging shreds of evidence has proved its circulation in developing countries. The intensity of environmental degradation and human health problems posed by residual DDT and its metabolites become of serious ecological concern, warranting a search for novel strains with a capacity to biodegrade these environmental contaminants. A new strain of the genus Staphylococcus was isolated from pesticide-contaminated soil. The 16S rRNA and phylogenetic analyses were used to identify the isolate and the 16S rRNA partial gene sequence was deposited in the NCBI GenBank as Staphylococcus sp. strain MY 83295F. The isolate was capable of growing in up to 60 mg L−1 of p,p’-DDT as the sole carbon source at an optimum pH of 6.5 and optimum temperature of 30°C within 120 h. Zn2+ has demonstrated a stimulatory effect on the growth of the strain in p,p’-DDT containing medium. However, Fe, Cu, Pb, Hg, Ag, and Cr ions showed inhibitory effects on the strain’s growth in the medium. The strain could be a handy tool for the bio-cleansing of residual p,p’-DDT in the contaminated environment.

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.

Sign in / Sign up

Export Citation Format

Share Document