دورية أكاديمية
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Protease production and molecular characterization of a protease dipeptidyl-aminopeptidase gene from different strains of Sordaria fimicola.

التفاصيل البيبلوغرافية
العنوان: Protease production and molecular characterization of a protease dipeptidyl-aminopeptidase gene from different strains of Sordaria fimicola.
المؤلفون: Naureen U; University of the Punjab, Department of Botany, Molecular Genetics Research Laboratory, Lahore, Pakistan., Kayani A; Government Model Degree College for Women, Model Town, Lahore, Pakistan., Akram F; University of the Punjab, Department of Botany, Molecular Genetics Research Laboratory, Lahore, Pakistan., Rasheed A; University of the Punjab, Department of Botany, Molecular Genetics Research Laboratory, Lahore, Pakistan., Saleem M; University of the Punjab, Department of Botany, Molecular Genetics Research Laboratory, Lahore, Pakistan.
المصدر: Brazilian journal of biology = Revista brasleira de biologia [Braz J Biol] 2022 May 20; Vol. 84, pp. e255692. Date of Electronic Publication: 2022 May 20 (Print Publication: 2022).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: International Institute of Ecology Country of Publication: Brazil NLM ID: 101129542 Publication Model: eCollection Cited Medium: Internet ISSN: 1678-4375 (Electronic) Linking ISSN: 15196984 NLM ISO Abbreviation: Braz J Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: São Carlos, SP [Brazil] : International Institute of Ecology, [2000]-
مواضيع طبية MeSH: Aminopeptidases*/genetics , Peptide Hydrolases*/genetics , Sordariales*/enzymology , Sordariales*/genetics, Fermentation ; Hydrogen-Ion Concentration ; Serine
مستخلص: The current research was designed to reach extracellular protease production potential in different strains of Sordaria fimicola which were previously obtained from Dr. Lamb (Imperial College, London) from North Facing Slope and South Facing Slope of Evolution Canyon. After initial and secondary screening, two hyper-producers strains S2 and N6 were selected for submerged fermentation and cultural conditions including temperature, pH, incubation period, inoculum size, substrate concentration, and different carbon and nitrogen sources were optimized for enzyme production. S2 strain showed maximum protease production of 3.291 U/mL after 14 days of incubation at 30 °C with 7 pH, 1% substrate concentration and 1 mL inoculum, While N6 strain showed maximum protease production of 1.929 U/mL under fermentation optimized conditions. Another aim of the present research was to underpin the biodiversity of genetics and post-translational modifications (PTMs) of protease DPAP (peptidyl-aminopeptidase) in Sordaria fimicola. Five polymorphic sites were observed in amino acid sequence of S. fimicola strains with reference to Neurospora crassa. PTMs prediction from bioinformatics tools predicted 38 phosphorylation sites on serine residues for protease peptidyl-aminopeptidase in S1 strain of S. fimicola while 45 phosphorylation sites on serine in N7 strain and 47 serine phosphorylation modifications were predicted in N. crassa. Current research gave an insight that change in genetic makeup effected PTMs which ultimately affected the production of protease enzyme in different strains of same organism (S. fimicola). The production and molecular data of the research revealed that environmental stress has strong effects on the specific genes through mutations which may cause genetic diversity. S. fimicola is non- pathogenic fungus and has a short life cycle. This fungus can be chosen to produce protease enzyme on a commercial scale.
المشرفين على المادة: 452VLY9402 (Serine)
EC 3.4.- (Peptide Hydrolases)
EC 3.4.11.- (Aminopeptidases)
SCR Organism: Sordaria fimicola
تواريخ الأحداث: Date Created: 20220518 Date Completed: 20220520 Latest Revision: 20220629
رمز التحديث: 20240829
DOI: 10.1590/1519-6984.255692
PMID: 35584457
قاعدة البيانات: MEDLINE
الوصف
تدمد:1678-4375
DOI:10.1590/1519-6984.255692