دورية أكاديمية
Enzyme immobilization on α-1,3-glucan: development of flow reactor with fusion protein of α-1,3-glucan binding domains and histamine dehydrogenase.
| العنوان: | Enzyme immobilization on α-1,3-glucan: development of flow reactor with fusion protein of α-1,3-glucan binding domains and histamine dehydrogenase. |
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| المؤلفون: | Nagahashi Y; Graduate School of Sciences and Engineering, Yamagata University., Hasegawa K; Graduate School of Sciences and Engineering, Yamagata University., Takagi K; Department of Applied Chemistry, Faculty of Life Sciences, Ritsumeikan University., Yano S; Graduate School of Sciences and Engineering, Yamagata University. |
| المصدر: | The Journal of general and applied microbiology [J Gen Appl Microbiol] 2024 Feb 02; Vol. 69 (4), pp. 206-214. Date of Electronic Publication: 2023 May 16. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Microbiology Research Foundation Country of Publication: Japan NLM ID: 0165543 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1349-8037 (Electronic) Linking ISSN: 00221260 NLM ISO Abbreviation: J Gen Appl Microbiol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Tokyo : Microbiology Research Foundation Original Publication: Tokyo, Institute of Applied Microbiology, Univ. of Tokyo. |
| مواضيع طبية MeSH: | Histamine* , Glucans*/metabolism , Oxidoreductases Acting on CH-NH Group Donors*, Catalytic Domain |
| مستخلص: | α-1,3-Glucanase Agl-KA from Bacillus circulans KA-304 consists of a discoidin domain (DS1), a carbohydrate binding module family 6 (CBM6), a threonine-proline-rich-linker (TP linker), a discoidin domain (DS2), an uncharacterized domain, and a catalytic domain. The binding of DS1, CBM6, and DS2 to α-1,3-glucan can be improved in the presence of two of these three domains. In this study, DS1, CBM6, and TP linker were genetically fused to histamine dehydrogenase (HmDH) from Nocardioides simplex NBRC 12069. The fusion enzyme, AGBDs-HmDH, was expressed in Escherichia coli Rosetta 2 (DE3) and purified from the cell-free extract. AGBDs-HmDH bound to 1% micro-particle of α-1,3-glucan (diameter: less than 1 μm) and 7.5% coarse-particle of α-1,3-glucan (less than 200 μm) at about 97 % and 70% of the initial amounts of the enzyme, respectively. A reactor for flow injection analysis filled with AGBDs-HmDH immobilized on the coarse-particle of α-1,3-glucan was successfully applied to determine histamine. A linear calibration curve was observed in the range for about 0.1 to 3.0 mM histamine. These findings suggest that the combination of α-1,3-glucan and α-1,3-glucan binding domains is a candidate for novel enzyme immobilization. |
| فهرسة مساهمة: | Keywords: enzyme immobilization; flow reactor; histamine dehydrogenase; α-1,3-glucan binding domain |
| المشرفين على المادة: | 9051-95-0 (alpha-1,3-glucan) EC 1.5.99.- (histamine dehydrogenase) 820484N8I3 (Histamine) 0 (Glucans) EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors) |
| تواريخ الأحداث: | Date Created: 20230517 Date Completed: 20240206 Latest Revision: 20240206 |
| رمز التحديث: | 20240206 |
| DOI: | 10.2323/jgam.2023.04.002 |
| PMID: | 37197975 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1349-8037 |
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| DOI: | 10.2323/jgam.2023.04.002 |