Isolation of Chrysosporium indicum from poultry soil for keratinase  enzyme, its purification and  partial characterization

Keratinases are produced by microorganisms as fungi, actinomycetes and bacteria and have the capacity to degrade tough insoluble keratin proteins, including feathers. Feathers are waste produced from the poultry industry worldwide and accumulated as solid waste. Therefore, keratinolytic fungal strains Chrysosporium indicum were isolated by hair baiting method from poultry farm soil of Punjab, India. Isolated C. indicum were screened for proteolytic activity on skimmed milk agar. Field Emission Scanning Electron Microscopy (FeSEM) analysis confirmed morphological characters as C. indicum. Fourier transform infrared spectroscopy analysis was studied for the structural and mechanism analysis of feather degraded during keratinase production. Keratinase enzyme was purified 48.03% recovery by ammonium sulphate precipitation, dialysis for desalting and chromatography. Diethylaminoethyl sepharose (DEAE sepharose) and Sephadex-G75 column were used to perform chromatography and partial characterization of the keratinase for temperature, pH, and substrate. The maximum keratinase activity was observed at 500C, at pH 10. The maximum enzyme activity of 289.1 U/ml was observed with keratin powder as substrate and minimum enzyme activity 67.1 U/ml with keratin azure. This is the first report on the purification and characterization of keratinase by C. indicum using DEAE sepharose as affinity chromatography for the purification of the keratinase enzyme.

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In vitro conversion of proapoprotein A-I to apoprotein A-I. Partial characterization of an extracellular enzyme activity.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)44242-6 ◽

1983 ◽

Vol 258 (19) ◽

pp. 11430-11433 ◽

Cited By ~ 18

Author(s):

C Edelstein ◽

J I Gordon ◽

K Toscas ◽

H F Sims ◽

A W Strauss ◽

...

Keyword(s):

Enzyme Activity ◽

Extracellular Enzyme ◽

Extracellular Enzyme Activity ◽

Partial Characterization

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Purification and Partial Characterization of Cellulase Produced by Aspergillus niger Cultured on Vitellaria paradoxa shells

Fountain Journal of Natural and Applied Sciences ◽

10.53704/fujnas.v6i2.167 ◽

2017 ◽

Vol 6 (2) ◽

Author(s):

Abdulhakeem Olarewaju Sulyman ◽

Yusuf A Iyanda ◽

Afolabi Olaniyi Opasola ◽

OtunOla Adedayo ◽

Raliat Abimbola Aladodo

Keyword(s):

Aspergillus Niger ◽

Specific Activity ◽

Gel Filtration ◽

Inoculum Size ◽

Partial Characterization ◽

Effect Of Temperature ◽

Vitellaria Paradoxa ◽

Endoglucanase Activity ◽

Ammonium Sulphate Precipitation

This research investigated the purification and partial characterization of cellulase produced by Aspergillus niger cultured on Vitellaria paradoxa shells. Cellulase (endoglucanase) from A. niger was produced under optimum fermentation conditions at 35 Â°C, pH 4.7, V. paradoxa, 4 g/L, inoculum size of 10 mm and the fermentation media incubated for 120 hours. The crude endoglucanase obtained were partially purified by subjecting to ammonium sulphate precipitation, dialysis and gel filtration chromatography for further purification. The effect of temperature and pH on the activity of purified endoglucanase was determined. Cellulase was purified to 734.33 folds by Sephadex G-100 column chromatography with a specific activity and yield of 4.406 U/mg and 63.03% respectively. Fractions 4 and 7 contained the highest endoglucanase activity out of 18 fractions collected and the two fractions were pooled for further analysis. The activity of purified endoglucanase was optimum at a temperature of 40 Â°C and pH 5. Therefore, the purified endoglucanase produced may be explored in detergent industry.

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Partial characterization of endothelin-converting enzyme activity in human serum lipoproteins

Atherosclerosis ◽

10.1016/0021-9150(94)90112-0 ◽

1994 ◽

Vol 108 (2) ◽

pp. 175-181

Author(s):

Tatsuya Ohwaki ◽

Hiroshi Sakai ◽

Yukio Hirata

Keyword(s):

Enzyme Activity ◽

Human Serum ◽

Partial Characterization ◽

Converting Enzyme ◽

Serum Lipoproteins ◽

Endothelin Converting Enzyme

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Isolation, purification and characterization of mannan degrading enzyme from a new isolate Acinetobacter baummanni

IOP Conference Series Earth and Environmental Science ◽

10.1088/1755-1315/924/1/012078 ◽

2021 ◽

Vol 924 (1) ◽

pp. 012078

Author(s):

D Muzaki ◽

E Zubaidah ◽

S Santoso ◽

A Sutrisno

Keyword(s):

Enzyme Activity ◽

Guar Gum ◽

Relative Activity ◽

Purification And Characterization ◽

Rrna Sequence ◽

16S Rrna Sequence ◽

Ammonium Sulphate Precipitation ◽

Optimum Ph ◽

16S Rrna Sequence Analysis

Abstract A mannan-degrading microbe was isolated from rotting porang tubers (Amorphophallus muelleri Blume). Molecular identification using 16S-rRNA sequence analysis revealed that the isolate showed 99.67% similarity with Acinetobacter baummanni. A crude enzyme from ammonium sulphate precipitation was used for preliminary characterization. The characterization results showed that the enzyme activity is optimum at 45 °C, and stable at 35-50 °C, while the optimum pH is 7, and stable at pH 5-7. The substrate with the highest relative activity was found in guar gum which was 137.512%. The enzyme activity was inhibited by Ca, Na, K ions, and increased by Mn2+ ions.

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Production and partial characterization of elastase of Bacillus subtilis isolated from the cervices of human females

Canadian Journal of Microbiology ◽

10.1139/m88-147 ◽

1988 ◽

Vol 34 (7) ◽

pp. 855-859 ◽

Cited By ~ 1

Author(s):

Mohinder Kaur ◽

K. K. Tripathi ◽

Meenakshi Gupta ◽

P. K. Jain ◽

M. R. Bansal ◽

...

Keyword(s):

Molecular Weight ◽

Enzyme Activity ◽

Bacillus Subtilis ◽

Ammonium Sulphate ◽

Phosphate Buffer ◽

Gel Filtration ◽

Ammonium Sulphate Precipitation ◽

Tris Maleate ◽

Culture Supernatants

Conditions are described for the production of extracellular elastase by Bacillus subtilis. The yield of enzyme was maximum in shake–cultures grown in Syncase medium at 37 °C and was stable in culture supernatants. The enzyme, purified by ammonium sulphate precipitation and Sephadex G-75 gel filtration, showed a molecular weight of 25 000 and activity between pH 6.0 and 9.5, with an optimum of 9.0 in Tris–maleate buffer. Elastinolytic activity was maximum in glycine–NaOH buffer and minimum in phosphate buffer. Enzyme activity was adversely affected by temperature ≥ 40 °C.

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MOLECULAR CHARACTERIZATION OF β-AGARASE PRODUCED BY SPHINGOMONAS PAUCIMOBILIS, A MARINE BACTERIUM

Bacterial Empire ◽

10.36547/be.159 ◽

2021 ◽

Vol 4 (2) ◽

pp. e159

Author(s):

Arunmozhi Bharathi Achudhan ◽

Mahalakshmi Velrajan

Keyword(s):

Extracellular Enzyme ◽

Spectroscopy Analysis ◽

Biochemical Tests ◽

Ammonium Sulphate Precipitation ◽

Sds Page ◽

Marine Source ◽

Solid Waste Generation ◽

Automated Instrument ◽

Hydrolysis Of

Agarases are enzymes that catalyze the hydrolysis of agar. The present study was carried out to isolate the agar degrading microorganisms from marine source. The characterization of agar degrading organism was done by VITEK 2.0 automated instrument, which confirmed the sample as Spinghomonas paucimobilis by a set of 64 biochemical tests. Production of agarase, an extracellular enzyme was done in mineral salt broth with agar and the enzyme was purified by ammonium sulphate precipitation and dialysis. The molecular weight of the enzyme was determined by SDS-PAGE method. Fourier transform infrared spectroscopy analysis was done to authenticate the degree of degradation of agar. The presence of agarase gene was targeted using the required primers and amplified by Polymerase chain reaction. Also the study addresses the problem of solid waste generation of agar waste by any microbiological laboratories and industries.

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