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Statistical optimization of enzyme cocktail production using Jew's mallow stalks residues by a new isolate Aspergillus flavus B2 via statistical strategy and enzymes characterization.

التفاصيل البيبلوغرافية
العنوان: Statistical optimization of enzyme cocktail production using Jew's mallow stalks residues by a new isolate Aspergillus flavus B2 via statistical strategy and enzymes characterization.
المؤلفون: Abdel Wahab WA; Chemistry of Natural and Microbial Products Department National Research Centre, Dokki, Cairo 12622, Egypt., Mostafa FA; Chemistry of Natural and Microbial Products Department National Research Centre, Dokki, Cairo 12622, Egypt., Ahmed SA; Chemistry of Natural and Microbial Products Department National Research Centre, Dokki, Cairo 12622, Egypt. Electronic address: dr_sa_ahmed@yahoo.Com., Saleh SAA; Chemistry of Natural and Microbial Products Department National Research Centre, Dokki, Cairo 12622, Egypt.
المصدر: Journal of biotechnology [J Biotechnol] 2023 Apr 10; Vol. 367, pp. 89-97. Date of Electronic Publication: 2023 Apr 05.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Science Publishers Country of Publication: Netherlands NLM ID: 8411927 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-4863 (Electronic) Linking ISSN: 01681656 NLM ISO Abbreviation: J Biotechnol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Amsterdam : Elsevier Science Publishers, c1984-
مواضيع طبية MeSH: Aspergillus flavus* , Polygalacturonase*, Humans ; Jews ; Hydrogen-Ion Concentration ; Temperature
مستخلص: This study investigates the production of the enzyme cocktail by the isolated fungi Aspergillus flavus B2 (GenBank accession number OL655454) using agricultural and industrial (AI) residues as the sole substrate. Of all the AI residues tested, Jew's mallow stalk was the best inducer substrate for enzyme cocktail production without adding any nutrients. Statistical optimization using Response Surface Methodology enhanced the production by 5.45, 5.20, and 3.34-fold, respectively for pectinase, xylanase, and CMCase. Optimum temperature, activation energy (E a ), and activation energy for denaturation (E d ) were determined. Michaelis constant (K m ) for CMCase, xylanase, and pectinase enzyme was 1.82, 1.23, and 1.05 mg/mL, respectively. Maximum reaction rate (V max ) was 4.67, 5.29, and 17.13 U/mL, respectively for CMCase, xylanase, and pectinase. Thermal stability revealed that pectinase, CMCase, and xylanase enzymes retained 64.7%, 61.8%, and 53.2% residual activities after incubation for 1 h at 50 °C. Half-life time (t 0.5 ) of pectinase, CMCase, and xylanase at 50 °C were 189.38, 129.8, and 127.89 min, respectively. Thermodynamics of the produced enzymes enthalpy (ΔH* d ), free energy (ΔG* d ), and entropy (ΔS* d ) were determined at 40, 50, and 60 °C. In the presence of EDTA (5 mM), CMCase, xylanase, and pectinase retained 69.5%, 66.2%, and 41.2%, respectively of their activity. This work is significant for the valorization of AI residues and the production of value-added products.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2023 Elsevier B.V. All rights reserved.)
فهرسة مساهمة: Keywords: Enzymes properties; Jew’s mallow; Optimization; Residues
المشرفين على المادة: EC 3.2.1.15 (Polygalacturonase)
تواريخ الأحداث: Date Created: 20230407 Date Completed: 20230501 Latest Revision: 20230501
رمز التحديث: 20231215
DOI: 10.1016/j.jbiotec.2023.04.003
PMID: 37028558
قاعدة البيانات: MEDLINE
الوصف
تدمد:1873-4863
DOI:10.1016/j.jbiotec.2023.04.003