Academic Journal
Characterization of a Metallic-Ions-Independent L-Arabinose Isomerase from Endophytic Bacillus amyloliquefaciens for Production of D-Tagatose as a Functional Sweetener
| العنوان: | Characterization of a Metallic-Ions-Independent L-Arabinose Isomerase from Endophytic Bacillus amyloliquefaciens for Production of D-Tagatose as a Functional Sweetener |
|---|---|
| المؤلفون: | Hoda M. Shehata, Mohamed N. Abd El-Ghany, Salwa A. Hamdi, Mosleh M. Abomughaid, Khaled I. Ghaleb, Zeinat Kamel, Mohamed G. Farahat |
| المصدر: | Fermentation, Vol 9, Iss 8, p 749 (2023) |
| بيانات النشر: | MDPI AG, 2023. |
| سنة النشر: | 2023 |
| المجموعة: | LCC:Fermentation industries. Beverages. Alcohol |
| مصطلحات موضوعية: | L-arabinose isomerase, tagatose production, recombinant enzyme, enzyme characterization, endophytic bacteria, Bacillus amyloliquefaciens, Fermentation industries. Beverages. Alcohol, TP500-660 |
| الوصف: | D-Tagatose is a low-calorie sugar substitute that has gained increased attention as a functional sweetener owing to its nutraceutical and prebiotic properties. Traditionally, D-tagatose is produced via the enzymatic conversion of L-galactose to D-tagatose by L-arabinose isomerase (L-AI). Nonetheless, the most reported L-AI enzymes are ion-dependent enzymes requiring Mn2+ and/or Co2+ as cofactors for their reactions, which limits their application due to safety and health concerns. Herein, we addressed the facile bioconversion of L-galactose to D-tagatose using a novel recombinant metallic-ions-independent L-AI derived from endophytic Bacillus amyloliquefaciens CAAI isolated from cantaloupe fruits. The ORF (1500 bp) of the L-arabinose isomerase gene (araA) was cloned and over-expressed in Escherichia coli. The recombinant enzyme (BAAI) was purified to homogeneity using Ni-NTA affinity chromatography, yielding a single distinct band with an apparent molecular mass of approximately 59 kDa as deduced from SDS-PAGE analysis. The purified enzyme showed optimum activity at pH and temperature of 7.5 and 45 °C, respectively, with obvious enzymatic activity in the presence of ethylenediaminetetraacetic acid (EDTA), indicating the metallic-ions independence from BAAI. The Km values of BAAI for D-galactose and L-arabinose were 251.6 mM and 92.8 mM, respectively. The catalytic efficiency (kcat/Km) values for D-galactose and L-arabinose were found to be 2.34 and 46.85 mM–1 min–1, respectively. The results revealed the production of 47.2 g/L D-tagatose from D-galactose (100 g/L) with 47.2% bioconversion efficiency in a metallic-ions-free reaction system that could be implemented in safe-production of food-grade low-calorie sweetener, D-tagatose. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 2311-5637 |
| Relation: | https://www.mdpi.com/2311-5637/9/8/749; https://doaj.org/toc/2311-5637 |
| DOI: | 10.3390/fermentation9080749 |
| URL الوصول: | https://doaj.org/article/8603ba90feb243c9930cda9e66ccd41f |
| رقم الانضمام: | edsdoj.8603ba90feb243c9930cda9e66ccd41f |
| قاعدة البيانات: | Directory of Open Access Journals |
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