دورية أكاديمية

Antioxidant capacity of xylooligosaccharides generated from beechwood xylan by recombinant family GH10 Aspergillus niger xylanase A and insights into the enzyme's competitive inhibition by riceXIP.

التفاصيل البيبلوغرافية
العنوان: Antioxidant capacity of xylooligosaccharides generated from beechwood xylan by recombinant family GH10 Aspergillus niger xylanase A and insights into the enzyme's competitive inhibition by riceXIP.
المؤلفون: Zhang K; Key Laboratory of Specialty Agri-product Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou 310018, China., Qi X; Key Laboratory of Specialty Agri-product Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou 310018, China., Feng N; Key Laboratory of Specialty Agri-product Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou 310018, China., Wang Y; Key Laboratory of Specialty Agri-product Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou 310018, China., Wei H; Key Laboratory of Specialty Agri-product Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou 310018, China., Liu M; Key Laboratory of Specialty Agri-product Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou 310018, China. Electronic address: mqliu524@163.com.
المصدر: Enzyme and microbial technology [Enzyme Microb Technol] 2024 Sep; Vol. 179, pp. 110456. Date of Electronic Publication: 2024 May 12.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: United States NLM ID: 8003761 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0909 (Electronic) Linking ISSN: 01410229 NLM ISO Abbreviation: Enzyme Microb Technol Subsets: MEDLINE
أسماء مطبوعة: Publication: New York, NY : Elsevier
Original Publication: [Guildford, Eng.] IPC Science and Technology Press.
مواضيع طبية MeSH: Glucuronates*/metabolism , Glucuronates*/chemistry , Xylans*/metabolism , Endo-1,4-beta Xylanases*/metabolism , Endo-1,4-beta Xylanases*/genetics , Endo-1,4-beta Xylanases*/chemistry , Aspergillus niger*/enzymology , Aspergillus niger*/genetics , Recombinant Proteins*/metabolism , Recombinant Proteins*/genetics , Recombinant Proteins*/chemistry , Oligosaccharides*/metabolism , Antioxidants*/metabolism , Antioxidants*/chemistry , Fungal Proteins*/metabolism , Fungal Proteins*/genetics , Fungal Proteins*/chemistry, Molecular Dynamics Simulation ; Oryza ; Fagus ; Enzyme Inhibitors/metabolism ; Enzyme Inhibitors/pharmacology ; Enzyme Inhibitors/chemistry ; Wood ; Pichia/genetics ; Pichia/metabolism ; Hydrolysis ; Catalytic Domain
مستخلص: In this study, the family GH10 xylanase AnXylA10 derived from Aspergillus niger JL15 strain was expressed in Pichia pastoris X33. The recombinant xylanase, reAnXylA10 exhibited optimal activity at 40 ℃ and pH 5.0. The hydrolysates generated from beechwood xylan using reAnXylA10 primarily consisted of xylobiose (X2) to xylohexaose (X6) and demonstrated remarkable antioxidant capacity. Furthermore, the rice xylanase inhibitory protein (riceXIP) was observed to competitively inhibit reAnXylA10, exhibiting an inhibition constant (K i ) of 140.6 nM. Molecular dynamics (MD) simulations of AnXylA10-riceXIP complex revealed that the α-7 helix (Q225-S238) of riceXIP intruded into the catalytic pocket of AnXylA10, thereby obstructing substrate access to the active site. Specifically, residue K226 of riceXIP formed robust interactions with E136 and E242, the two catalytic sites of AnXylA10, predominantly through high-occupied hydrogen bonds. Based on QTAIM, electron densities for the atom pairs K226 riceXIP @HZ1-E136 AnXylA10 @OE2 and K226 riceXIP @HZ3-E242 AnXylA10 @OE1 were determined to be 0.04628 and 0.02914 a.u., respectively. Binding free energy of AnXylA10-riceXIP complex was -59.0±7.6 kcal/mol, significantly driven by electrostatic and van der Waals forces. Gaining insights into the interaction between xylanase and its inhibitors, and mining the inhibition mechanism in depth, will facilitate the design of innovative GH10 family xylanases that are both highly efficient and resistant to inhibitors.
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 © 2024 Elsevier Inc. All rights reserved.)
فهرسة مساهمة: Keywords: Antioxidant; Key interface residue; Molecular simulation; Xylanase; Xylooligosaccharides (XOS)
المشرفين على المادة: 0 (Glucuronates)
0 (xylooligosaccharide)
0 (Xylans)
EC 3.2.1.8 (Endo-1,4-beta Xylanases)
0 (Recombinant Proteins)
0 (Oligosaccharides)
0 (Antioxidants)
0 (Fungal Proteins)
0 (Enzyme Inhibitors)
تواريخ الأحداث: Date Created: 20240516 Date Completed: 20240805 Latest Revision: 20240805
رمز التحديث: 20240806
DOI: 10.1016/j.enzmictec.2024.110456
PMID: 38754147
قاعدة البيانات: MEDLINE