Proximate analysis of lignocellulosic biomass and its utilization for production, purification and characterization of ligninolytic enzymes by Aspergillus flavus

Khan, Jehangir; Asad, Muahammad Javaid; Mahmood, Raja Tahir; Wattoo, Feeroza Hamid; Zainab, Tayyaba; Nazir, Sidrah; Shah, Muhammad Basir; Ahmed, Dawood

doi:10.24425/aep.2020.132520

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Tytuł artykułu

Proximate analysis of lignocellulosic biomass and its utilization for production, purification and characterization of ligninolytic enzymes by Aspergillus flavus

Autorzy

Khan Jehangir , Asad Muahammad Javaid , Mahmood Raja Tahir , Wattoo Feeroza Hamid , Zainab Tayyaba , Nazir Sidrah , Shah Muhammad Basir , Ahmed Dawood

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DOI

10.24425/aep.2020.132520

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Abstrakty

Ligninolytic enzymes are employed for the production of second-generation biofuel to minimize fuel crisis. Additionally, they play a crucial role in global carbon cycle and a variety of applications in food, agriculture, paper and textile industries. On a large scale production of ligninolytic enzymes, microorganisms can be cultured on lignocellulosic wastes. In the present study, proximate analysis including acid detergent lignin (ADL), acid detergent cellulose (ADC), acid detergent fiber (ADF) and acid insoluble ash (AIA) were performed for Platanus orientalis (chinar), Bauhinia variegata (orchid tree), Pinus roxburghii (chirpine), wheat straw and wheat husk. Platanus orientalis was selected as substrate because of higher lignin contents for the production of ligninolytic enzymes by Aspergillus flavus. Solid State Fermentation was used and Response Surface Methodology was employed for optimizing various parameters and enzymes production. Maximum production was achieved at temperature 32°C, fermentation period 120 hours, pH 4.5, inoculums size 3.5 mL, substrate mesh size 80 mm, substrate size 7 g. Maximum purification of laccase, manganese peroxidase (MnP) and lignin peroxidase (LiP) was achieved with 50%, 60% and 40% ammonium sulfate respectively and it was enhanced by gel filtration chromatography. Characterization of enzymes shows that Laccase has 35°C optimum temperature, 4.5 pH, 0.289 mM Km and 227.27 μM/ml Vmax. Manganese peroxidase has 30°C optimum temperature, 5.5 pH, 0.538 mM Km and 203.08 μM/ml Vmax. Lignin peroxidase has 30°C optimum temperature, 3 pH, 2 mM Km and 2000 uM/ml Vmax. Protein concentrations found in crude extracts and partially purified enzymes are respectively: laccase 1.78 and 0.71 mg/ml, MnP 1.59 and 0.68 mg/ml. LiP, 1.70 and 0.69 mg/ml.

Słowa kluczowe

Aspergillus flavus acid detergent lignin ammonium sulfate ligninolytic enzymes Platanus orientalis

Wydawca

Institute of Environmental Engineering, Polish Academy of Sciences

Czasopismo

Archives of Environmental Protection

Rocznik

2020

Tom

Vol. 46, no. 1

Strony

3--13

Opis fizyczny

Bibliogr. 52 poz., tab., wykr.

Twórcy

autor

Khan Jehangir

University Institute of Biochemistry and Biotechnology, PMAS-Arid Agriculture University Rawalpindi, Pakistan
Department of Biosciences, University of WAH, WAH Pakistan

autor

Asad Muahammad Javaid

University Institute of Biochemistry and Biotechnology, PMAS-Arid Agriculture University Rawalpindi, Pakistan

autor

Mahmood Raja Tahir

raja.tahir@must.edu.pk

Department of Biotechnology, Mirpur University of Science and Technology (MUST), Mirpur-10250 (AJK), Pakistan

autor

Wattoo Feeroza Hamid

University Institute of Biochemistry and Biotechnology, PMAS-Arid Agriculture University Rawalpindi, Pakistan

autor

Zainab Tayyaba

University Institute of Biochemistry and Biotechnology, PMAS-Arid Agriculture University Rawalpindi, Pakistan

autor

Nazir Sidrah

University Institute of Biochemistry and Biotechnology, PMAS-Arid Agriculture University Rawalpindi, Pakistan

autor

Shah Muhammad Basir

Department of Plant Breeding & Genetics, Balochistan Agriculture College Quetta, Pakistan

autor

Ahmed Dawood

Department of Medical Laboratory Technology, Haripur University, Haripur, KPK, Pakistan

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Uwagi

Opracowanie rekordu ze środków MNiSW, umowa Nr 461252 w ramach programu "Społeczna odpowiedzialność nauki" - moduł: Popularyzacja nauki i promocja sportu (2020).

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