• Je něco špatně v tomto záznamu ?

Production, purification, and characterization of p-diphenol oxidase (PDO) enzyme from lignolytic fungal isolate Schizophyllum commune MF-O5

M. Faheem, SAI. Bokhari, MA. Malik, B. Ahmad, M. Riaz, N. Zahid, A. Hussain, A. Ghani, H. Ullah, W. Shah, R. Mehmood, K. Ahmad, H. Rasheed, A. Zain, S. Hussain, A. Khan, MT. Yasin, H. Tariq, . Rizwanullah, MM. Basheir, N. Jogezai

. 2023 ; 68 (6) : 867-888. [pub] 20230509

Jazyk angličtina Země Česko

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc23020592

Fungi are producers of lignolytic extracellular enzymes which are used in industries like textile, detergents, biorefineries, and paper pulping. This study assessed for the production, purification, and characterization of novel p-diphenol oxidase (PDO; laccase) enzyme from lignolytic white-rot fungal isolate. Fungi samples collected from different areas of Pakistan were initially screened using guaiacol plate method. The maximum PDO producing fungal isolate was identified on the basis of ITS (internal transcribed spacer sequence of DNA of ribosomal RNA) sequencing. To get optimum enzyme yield, various growth and fermentation conditions were optimized. Later PDO was purified using ammonium sulfate precipitation, size exclusion, and anion exchange chromatography and characterized. It was observed that the maximum PDO producing fungal isolate was Schizophyllum commune (MF-O5). Characterization results showed that the purified PDO was a monomeric protein with a molecular mass of 68 kDa and showed stability at lower temperature (30 °C) for 1 h. The Km and Vmax values of the purified PDO recorded were 2.48 mM and 6.20 U/min. Thermal stability results showed that at 30 °C PDO had 119.17 kJ/K/mol Ea value and 33.64 min half-life. The PDO activity was stimulated by Cu2+ ion at 1.0 mM showing enhanced activity up to 111.04%. Strong inhibition effect was noted for Fe2+ ions at 1 mM showing 12.04% activity. The enzyme showed stability against 10 mM concentration oxidizing reducing agents like DMSO, EDTA, H2O2, NaOCl, and urea and retained more than 75% of relative activity. The characterization of purified PDO enzyme confirmed its tolerance against salt, metal ions, organic solvents, and surfactants indicating its ability to be used in the versatile commercial applications.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc23020592
003      
CZ-PrNML
005      
20231215110123.0
007      
ta
008      
231215s2023 xr f 000 0|eng||
009      
AR
024    7_
$a 10.1007/s12223-023-01056-w $2 doi
035    __
$a (PubMed)37160524
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xr
100    1_
$a Faheem, Muhammad $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan. faheem.biotechnologist@gmail.com $1 https://orcid.org/000000033347765X
245    10
$a Production, purification, and characterization of p-diphenol oxidase (PDO) enzyme from lignolytic fungal isolate Schizophyllum commune MF-O5 / $c M. Faheem, SAI. Bokhari, MA. Malik, B. Ahmad, M. Riaz, N. Zahid, A. Hussain, A. Ghani, H. Ullah, W. Shah, R. Mehmood, K. Ahmad, H. Rasheed, A. Zain, S. Hussain, A. Khan, MT. Yasin, H. Tariq, . Rizwanullah, MM. Basheir, N. Jogezai
520    9_
$a Fungi are producers of lignolytic extracellular enzymes which are used in industries like textile, detergents, biorefineries, and paper pulping. This study assessed for the production, purification, and characterization of novel p-diphenol oxidase (PDO; laccase) enzyme from lignolytic white-rot fungal isolate. Fungi samples collected from different areas of Pakistan were initially screened using guaiacol plate method. The maximum PDO producing fungal isolate was identified on the basis of ITS (internal transcribed spacer sequence of DNA of ribosomal RNA) sequencing. To get optimum enzyme yield, various growth and fermentation conditions were optimized. Later PDO was purified using ammonium sulfate precipitation, size exclusion, and anion exchange chromatography and characterized. It was observed that the maximum PDO producing fungal isolate was Schizophyllum commune (MF-O5). Characterization results showed that the purified PDO was a monomeric protein with a molecular mass of 68 kDa and showed stability at lower temperature (30 °C) for 1 h. The Km and Vmax values of the purified PDO recorded were 2.48 mM and 6.20 U/min. Thermal stability results showed that at 30 °C PDO had 119.17 kJ/K/mol Ea value and 33.64 min half-life. The PDO activity was stimulated by Cu2+ ion at 1.0 mM showing enhanced activity up to 111.04%. Strong inhibition effect was noted for Fe2+ ions at 1 mM showing 12.04% activity. The enzyme showed stability against 10 mM concentration oxidizing reducing agents like DMSO, EDTA, H2O2, NaOCl, and urea and retained more than 75% of relative activity. The characterization of purified PDO enzyme confirmed its tolerance against salt, metal ions, organic solvents, and surfactants indicating its ability to be used in the versatile commercial applications.
650    12
$a lakasa $x metabolismus $7 D042845
650    12
$a Schizophyllum $x genetika $x metabolismus $7 D012567
650    _2
$a peroxid vodíku $7 D006861
650    _2
$a koncentrace vodíkových iontů $7 D006863
650    _2
$a teplota $7 D013696
650    _2
$a stabilita enzymů $7 D004795
655    _2
$a časopisecké články $7 D016428
700    1_
$a Bokhari, Syed Ali Imran $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Malik, Muhammad Arshad $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Ahmad, Bashir $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Riaz, Muhammad $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Zahid, Nafeesa $u Department of Botany, Mirpur University of Science and Technology (MUST), Mirpur, Azad Kashmir, 10250, Pakistan
700    1_
$a Hussain, Adil $u Food and Biotechnology Research Centre, Pakistan, Council of Scientific and Industrial Research (PCSIR), Laboratories Complex , Ferozepur Road, Lahore, 54600, Pakistan
700    1_
$a Ghani, Abdul $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Ullah, Hanif $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Shah, Waseem $u Department of Biosciences, Comsats University, Islamabad, 45550, Pakistan
700    1_
$a Mehmood, Rashid $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Ahmad, Khurshid $u College of Food Sciences and Engineering, Ocean University of China, Shandong Province, 266003, Qingdao, China
700    1_
$a Rasheed, Hassam $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Zain, Ali $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Hussain, Saddam $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Khan, Abrar $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Yasin, Muhammad Talha $u Insititute of Biological Sciences, Khwaja Fareed University of Engineering and Information Technology, Rahim Yar Khan, 64200, Pakistan
700    1_
$a Tariq, Hasnat $u Department of Biotechnology, Quaid-i-Azam University, Islamabad, Pakistan
700    1_
$a Rizwanullah, $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Basheir, Muhammad Mudassir $u Department of Biological Sciences, Faculty of Basic and Applied Sciences, International Islamic University, H-10, Islamabad, 44000, Pakistan
700    1_
$a Jogezai, NaqeebUllah $u Directorate of QEC, University of Loralai, Loralai, 84800, Pakistan
773    0_
$w MED00011005 $t Folia microbiologica $x 1874-9356 $g Roč. 68, č. 6 (2023), s. 867-888
856    41
$u https://pubmed.ncbi.nlm.nih.gov/37160524 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y - $z 0
990    __
$a 20231215 $b ABA008
991    __
$a 20231215110116 $b ABA008
999    __
$a ok $b bmc $g 2021894 $s 1207031
BAS    __
$a 3
BAS    __
$a PreBMC-MEDLINE
BMC    __
$a 2023 $b 68 $c 6 $d 867-888 $e 20230509 $i 1874-9356 $m Folia microbiologica $n Folia microbiol. (Prague) $x MED00011005
LZP    __
$a Pubmed-20231215
Zpět

Najít záznam

Citační ukazatele

Možnosti archivace