Engineering Artificial Fusion Naringinase for Enhancing Naringenin Biosynthesis DOI

Chen-Mu Luo,

Wenting Zhang,

Song-Yi Xie

et al.

Published: Jan. 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

Language: Английский

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

Bhuvaneshwari Veerapandian,

Srividhya Krishnan,

Subramaniyasharma Sivaraman

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 140252 - 140252

Published: Jan. 1, 2025

Language: Английский

Citations

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

et al.

International Journal of Biological Macromolecules, Journal Year: 2024, Volume and Issue: 271, P. 132508 - 132508

Published: May 21, 2024

Language: Английский

Citations

5
Microbial polysaccharides biosynthesis and their regulatory strategies DOI

Dafang Yin,

Yadong Zhong,

Jielun Hu

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 143013 - 143013

Published: April 1, 2025

Language: Английский

Citations

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

Danfeng Liu,

Xin Xin,

Ru-Jie Shang

et al.

Biochemical Engineering Journal, Journal Year: 2025, Volume and Issue: 220, P. 109766 - 109766

Published: April 28, 2025

Language: Английский

Citations

0
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

et al.

RSC Advances, Journal Year: 2024, Volume and Issue: 14(4), P. 2346 - 2353

Published: Jan. 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.

Language: Английский

Citations

3
Engineering artificial fusion naringinase for enhancing naringenin biosynthesis DOI

Chen-Mu Luo,

Wenting Zhang,

Song-Yi Xie

et al.

Biochemical Engineering Journal, Journal Year: 2024, Volume and Issue: 205, P. 109253 - 109253

Published: Feb. 9, 2024

Language: Английский

Citations

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

et al.

Molecular Catalysis, Journal Year: 2022, Volume and Issue: 535, P. 112827 - 112827

Published: Nov. 28, 2022

Language: Английский

Citations

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

et al.

LWT, Journal Year: 2024, Volume and Issue: 200, P. 116200 - 116200

Published: May 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.

Language: Английский

Citations

1
Engineering Artificial Fusion Naringinase for Enhancing Naringenin Biosynthesis DOI

Chen-Mu Luo,

Wenting Zhang,

Song-Yi Xie

et al.

Published: Jan. 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

Language: Английский

Citations

0