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Purification, characterization and application of hemagglutinin (lectin) from different mushroom species / Sara Seleem Mahmoud Seleem ; Supervised Ismail Mohamed Kamel Ismail , Neveen Mahmoud Mohamed Mohamed , Sherien Mohamed Mabrouk Atalla

By: Contributor(s): Material type: TextTextLanguage: English Publication details: Cairo : Sara Seleem Mahmoud Seleem , 2021Description: 225 P . : charts , photographs ; 25cmOther title:
  • تنقية : توصيف و تطبيق الهيماجلوتينين (ليكتين) من بعض انواع المشروم [Added title page title]
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Dissertation note: Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Botany and Microbiology Summary: The ability to synthesize lectin was screened in the intracellular mycelium, the extracellular supernatant and the fruiting bodies of three mushroom species belonging to genus Pleurotus (P. ostreatus, P. columbinus and P. sajor-caju). It was revealed that all tested Pleurotus species were able to produce intracellular mycelial and fruiting bodies lectins with different degrees of activity, while all were unable to synthesize extracellular lectin. Mycelial lectins of the studied species had significantly lower hemagglutinating activity compared with fruiting bodies lectins from the same species. All mushrooms crude lectin extracts lacked specificity toward certain human erythrocyte type, except for that of dried fruiting bodies of P. ostreatus which showed specificity only toward human blood type AB. This extract exerted the highest activity among the other studied species, so it was selected for further studies. The selected Pleurotus species was molecularly identified by amplification and sequencing of fungal 18rRNA gene which resulted in 556 bp long nucleotide sequence that was submitted in the NCBI database under accession number; MN795635.1 and was given a strain identifier; Pleurotus ostreatus SS89. The lectin gene was amplified using specific designed forward and reverse primers, and the nucleotide sequence was determined. Reverse and forward DNA sequences were read and assembled to obtain the consensus 1094 bp that contained 801 bp coding sequence resulting in 267 amino acids. Nucleotide sequence of P. ostreatus SS89 lectin gene was submitted to the NCBI database under accession number MT074428.2, also the amino acid sequence was deduced (protein_id "QJQ82566.1")
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Thesis Thesis قاعة الرسائل الجامعية - الدور الاول المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.05.Ph.D.2021.Sa.P (Browse shelf(Opens below)) Not for loan 01010110083298000
CD - Rom CD - Rom مخـــزن الرســائل الجـــامعية - البدروم المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.05.Ph.D.2021.Sa.P (Browse shelf(Opens below)) 83298.CD Not for loan 01020110083298000

Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Botany and Microbiology

The ability to synthesize lectin was screened in the intracellular mycelium, the extracellular supernatant and the fruiting bodies of three mushroom species belonging to genus Pleurotus (P. ostreatus, P. columbinus and P. sajor-caju). It was revealed that all tested Pleurotus species were able to produce intracellular mycelial and fruiting bodies lectins with different degrees of activity, while all were unable to synthesize extracellular lectin. Mycelial lectins of the studied species had significantly lower hemagglutinating activity compared with fruiting bodies lectins from the same species. All mushrooms crude lectin extracts lacked specificity toward certain human erythrocyte type, except for that of dried fruiting bodies of P. ostreatus which showed specificity only toward human blood type AB. This extract exerted the highest activity among the other studied species, so it was selected for further studies. The selected Pleurotus species was molecularly identified by amplification and sequencing of fungal 18rRNA gene which resulted in 556 bp long nucleotide sequence that was submitted in the NCBI database under accession number; MN795635.1 and was given a strain identifier; Pleurotus ostreatus SS89. The lectin gene was amplified using specific designed forward and reverse primers, and the nucleotide sequence was determined. Reverse and forward DNA sequences were read and assembled to obtain the consensus 1094 bp that contained 801 bp coding sequence resulting in 267 amino acids. Nucleotide sequence of P. ostreatus SS89 lectin gene was submitted to the NCBI database under accession number MT074428.2, also the amino acid sequence was deduced (protein_id "QJQ82566.1")

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