Engineering Artificial Fusion Naringinase for Enhancing Naringenin Biosynthesis DOI

Chen-Mu Luo,

Wenting Zhang,

Song-Yi Xie

и другие.

Опубликована: Янв. 1, 2023

Naringinase (NGase) is a multisubunit complex enzyme with α-L-rhamnosidase (Rha) and β-D-glucosidase (BGL). The biotransformation of naringin into the more valuable naringenin was impeded by uncoordinated activity instability natural naringinases. In this study, efficient artificial fusion naringinases Rha from Spirochaeta thermophila (StRha) BGL Pyrococcus furiosus (PfBGL) were constructed utilized in biosynthesis naringenin. Fusion StRha-PfBGL (DL-NGase), StRha-(GGGGS)-PfBGL (FL-NGase) StRha-(EAAAK)-PfBGL (RL-NGase) obtained fusing StRha PfBGL through direct or mediated peptide linkers. DL-NGase showed coordinated better thermostability than FL-NGase RL-NGase. optimal temperature above 65 ℃, both retained 75% initial activities at 55 ℃ for 2 h. addition, exhibited catalytic performance mixed free systems, efficiency increased 49.8%. Furthermore, whole-cell catalyst applied high-efficient naringenin, final yield 13.5 mg/mL time-space 2.25 mg/mL/h. These results demonstrate great potential bioconversion to

Язык: Английский

Bacillus spp. as microbial factories for levan and fructooligosaccharide production – Recent trends DOI

Bhuvaneshwari Veerapandian,

Srividhya Krishnan,

Subramaniyasharma Sivaraman

и другие.

International Journal of Biological Macromolecules, Год журнала: 2025, Номер unknown, С. 140252 - 140252

Опубликована: Янв. 1, 2025

Язык: Английский

Процитировано

1
Endo- and exo-levanases from Bacillus subtilis HM7: Catalytic components, synergistic cooperation, and application in fructooligosaccharide synthesis DOI
Thanapon Charoenwongpaiboon,

Chonnipha Charoenwongphaibun,

Karan Wangpaiboon

и другие.

International Journal of Biological Macromolecules, Год журнала: 2024, Номер 271, С. 132508 - 132508

Опубликована: Май 21, 2024

Язык: Английский

Процитировано

5
Improving the thermostability and modulating the inulin profile of inulosucrase through rational glycine-to-proline substitution DOI Creative Commons
Thanapon Charoenwongpaiboon,

Nawapat Sommanat,

Karan Wangpaiboon

и другие.

RSC Advances, Год журнала: 2024, Номер 14(4), С. 2346 - 2353

Опубликована: Янв. 1, 2024

The flexibility of protein structure plays a crucial role in enzyme stability and catalysis. Among the amino acids, glycine is particularly important conferring to proteins. In this study, effects flexible residues Lactobacillus reuteri 121 inulosucrase (LrInu) on inulin profile were investigated through glycine-to-proline substitutions. Molecular dynamics (MD) simulations employed discover residues, eight including Gly217, Gly298, Gly330, Gly416, Gly450, Gly624, Gly627, Gly629, selected for site-directed mutagenesis. results demonstrated significant changes both thermostability profiles variants. Particularly, G624P G627P variants showed reduced production long-chain oligosaccharides compared WT. This can be ascribed increased rigidity active site, which induction-fit mechanism. Overall, study provides valuable insights into activity, stability, synthesis LrInu.

Язык: Английский

Процитировано

3
Microbial polysaccharides biosynthesis and their regulatory strategies DOI

Dafang Yin,

Yadong Zhong,

Jielun Hu

и другие.

International Journal of Biological Macromolecules, Год журнала: 2025, Номер unknown, С. 143013 - 143013

Опубликована: Апрель 1, 2025

Язык: Английский

Процитировано

0
Microbial synthesis of terephthalic acid via Saccharomyces cerevisiae cell factories DOI

Danfeng Liu,

Xin Xin,

Ru-Jie Shang

и другие.

Biochemical Engineering Journal, Год журнала: 2025, Номер 220, С. 109766 - 109766

Опубликована: Апрель 28, 2025

Язык: Английский

Процитировано

0
Levansucrases: a review of their catalytic properties, product characterization and applications in food systems DOI

Muriel Wong Min,

Salwa Karboune

Critical Reviews in Food Science and Nutrition, Год журнала: 2025, Номер unknown, С. 1 - 21

Опубликована: Июнь 2, 2025

Owing to the promising physiological effects of levan and levan-type fructooligosaccharides, levansucrase (LS, EC 2.4.1.10) has garnered much interest in recent years for pharmaceutical, cosmetic, food applications. LS is a fructosyl-transferase that catalyzes synthesis complex oligosaccharides by acquiring fructosyl residue from donor molecule performing non-Leloir transfer an acceptor molecule. The mechanism action toward various carbohydrates been well documented, increasing drawn ability alkyl phenolic compounds act as substrates LS-catalyzed transfructosylation reactions. Many studies have also focused on improving production LSs their product spectrum, whether overall activity or shifting selectivity particular reaction. With these advances, possibility applying processing gradually gained momentum. This review provides comprehensive discussion catalytic properties full characterization its reaction products. We then discuss some applications microbial biogeneration functional ingredients systems.

Язык: Английский

Процитировано

0
Engineering artificial fusion naringinase for enhancing naringenin biosynthesis DOI

Chen-Mu Luo,

Wenting Zhang,

Song-Yi Xie

и другие.

Biochemical Engineering Journal, Год журнала: 2024, Номер 205, С. 109253 - 109253

Опубликована: Фев. 9, 2024

Язык: Английский

Процитировано

2
Cross-linked enzyme aggregates (combi-CLEAs) derived from levansucrase and variant inulosucrase are highly efficient catalysts for the synthesis of levan-type fructooligosaccharides DOI
Thanapon Charoenwongpaiboon, Karan Wangpaiboon, Robert A. Field

и другие.

Molecular Catalysis, Год журнала: 2022, Номер 535, С. 112827 - 112827

Опубликована: Ноя. 28, 2022

Язык: Английский

Процитировано

8
An Exploration of various Fructooligosaccharides production methods using novel engineered enzymes with innovative core-shell chitosan beads DOI Creative Commons
Treerat Vacharanukrauh,

Sasina Plubwungklam,

Manatsanan Puangpathanachai

и другие.

LWT, Год журнала: 2024, Номер 200, С. 116200 - 116200

Опубликована: Май 1, 2024

This study investigates Fructooligosaccharides (FOSs) production as prebiotics to promote gut health and overall well-being. Various methods for FOSs were explored, leveraging novel engineered inulosucrase (IN) levansucrase (LV) enzymes. The methodologies included batch stirred reactors with free enzymes fixed-bed utilizing immobilized on hydrogel chitosan beads (HGBs) core-shell (CSBs). found that exhibited the highest sucrose consumption rates, IN achieving 142.8 g/L∙h LV 82.9 g/L∙h. However, CSB-immobilized demonstrated substantial enzyme savings (55% 41% reduction in consumption, respectively) through reuse across multiple cycles, while delivering superior yields. outperformed HGB-immobilized terms of immobilization efficiency, activity recovery, conversion, yields, repeatability. A reactor setup involving interconnected different series produced promising results, generating species alongside expected I-FOSs L-FOSs. Consumable cost analysis indicated usage is initially cost-effective (5.09 - 7.06 USD/kg FOSs), significant increases prices could make CSB a cost-competitive alternative. highlights potential innovative strategies designs efficient production, considering both performance economic feasibility.

Язык: Английский

Процитировано

1
Engineering Artificial Fusion Naringinase for Enhancing Naringenin Biosynthesis DOI

Chen-Mu Luo,

Wenting Zhang,

Song-Yi Xie

и другие.

Опубликована: Янв. 1, 2023

Naringinase (NGase) is a multisubunit complex enzyme with α-L-rhamnosidase (Rha) and β-D-glucosidase (BGL). The biotransformation of naringin into the more valuable naringenin was impeded by uncoordinated activity instability natural naringinases. In this study, efficient artificial fusion naringinases Rha from Spirochaeta thermophila (StRha) BGL Pyrococcus furiosus (PfBGL) were constructed utilized in biosynthesis naringenin. Fusion StRha-PfBGL (DL-NGase), StRha-(GGGGS)-PfBGL (FL-NGase) StRha-(EAAAK)-PfBGL (RL-NGase) obtained fusing StRha PfBGL through direct or mediated peptide linkers. DL-NGase showed coordinated better thermostability than FL-NGase RL-NGase. optimal temperature above 65 ℃, both retained 75% initial activities at 55 ℃ for 2 h. addition, exhibited catalytic performance mixed free systems, efficiency increased 49.8%. Furthermore, whole-cell catalyst applied high-efficient naringenin, final yield 13.5 mg/mL time-space 2.25 mg/mL/h. These results demonstrate great potential bioconversion to

Язык: Английский

Процитировано

0