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Keywords = Bacillus amyloliquefaciens DSM 7

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15 pages, 944 KB  
Article
Harnessing Carrot Discard as a Novel Feedstock for 2,3-Butanediol Bioproduction: A Comparison of Fermentation Strategies and Bacillus Performance
by Juan Carlos López-Linares, Alba Mei González-Galán, Mónica Coca, Susana Lucas and María Teresa García-Cubero
Appl. Sci. 2025, 15(14), 7808; https://doi.org/10.3390/app15147808 - 11 Jul 2025
Viewed by 307
Abstract
This study investigates the valorization of carrot discard, a carbohydrate-rich agricultural residue, for the production of 2,3-butanediol (2,3-BDO). The fermentation process was evaluated using two strains, Bacillus licheniformis DSM 8785 and Bacillus amyloliquefaciens DSM 7. Two process configurations were compared: separate hydrolysis and [...] Read more.
This study investigates the valorization of carrot discard, a carbohydrate-rich agricultural residue, for the production of 2,3-butanediol (2,3-BDO). The fermentation process was evaluated using two strains, Bacillus licheniformis DSM 8785 and Bacillus amyloliquefaciens DSM 7. Two process configurations were compared: separate hydrolysis and fermentation (SHF) and simultaneous saccharification and fermentation (SSF). Additionally, to determine substrate and product inhibition thresholds, fermentation assays were conducted in semi-defined media with glucose concentrations ranging from 20 to 120 g/L. The SHF strategy proved more effective than the SSF configuration. Under the SHF configuration, B. amyloliquefaciens demonstrated superior performance, yielding 16.7 g/L of 2,3-BDO. In contrast, B. licheniformis was notable for its high capacity for acetoin synthesis, producing 24.2 g/L of acetoin in addition to 10.9 g/L of 2,3-BDO. Therefore, these findings demonstrate that carrot discard is a viable feedstock for the co-production of 2,3-BDO and acetoin. Full article
(This article belongs to the Section Applied Biosciences and Bioengineering)
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15 pages, 1793 KB  
Article
Optimization and Engineering of a Self-Sufficient CYP102 Enzyme from Bacillus amyloliquefaciens towards Synthesis of In-Chain Hydroxy Fatty Acids
by Li Zong, Yan Zhang, Zhengkang Shao, Yingwu Wang, Zheng Guo, Renjun Gao and Bekir Engin Eser
Catalysts 2021, 11(6), 665; https://doi.org/10.3390/catal11060665 - 23 May 2021
Cited by 8 | Viewed by 3871
Abstract
Cytochrome P450 (CYP) mediated enzymatic hydroxylation of fatty acids present a green alternative to chemical synthesis of hydroxy fatty acids (HFAs), which are high-value oleochemicals with various uses in materials industry and medical field. Although many CYPs require the presence of additional reductase [...] Read more.
Cytochrome P450 (CYP) mediated enzymatic hydroxylation of fatty acids present a green alternative to chemical synthesis of hydroxy fatty acids (HFAs), which are high-value oleochemicals with various uses in materials industry and medical field. Although many CYPs require the presence of additional reductase proteins for catalytic activity, self-sufficient CYPs have their reductase partner naturally fused into their catalytic domain, leading to a greatly simplified biotransformation process. A recently discovered self-sufficient CYP, BAMF2522 from Bacillus amyloliquefaciens DSM 7, exhibits novel regioselectivity by hydroxylating in-chain positions of palmitic acid generating ω-1 to ω-7 HFAs, a rare regiodiversity profile among CYPs. Besides, F89I mutant of BAMF2522 expanded hydroxylation up to ω-9 position of palmitic acid. Here, we further characterize this enzyme by determining optimum temperature and pH as well as thermal stability. Moreover, using extensive site-directed and site-saturation mutagenesis, we obtained BAMF2522 variants that demonstrate greatly increased regioselectivity for in-chain positions (ω-4 to ω-9) of various medium to long chain fatty acids. Remarkably, when a six-residue mutant was reacted with palmitic acid, 84% of total product content was the sum of ω-7, ω-8 and ω-9 HFA products, the highest in-chain selectivity observed to date with a self-sufficient CYP. In short, our study demonstrates the potential of a recently identified CYP and its mutants for green and sustainable production of a variety of in-chain hydroxy enriched HFAs. Full article
(This article belongs to the Special Issue Biocatalysis for Green Chemistry)
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