Enhanced d-tagatose production by spore surface-displayed l-arabinose isomerase from isolated Lactobacillus brevis PC16 and biotransformation. (January 2018)

• Record Type: Journal Article
• Authors: Guo, Qi; An, Yingfeng; Yun, Junhua; Yang, Miaomiao; Magocha, Tinashe A.; Zhu, Jingfei; Xue, Yanbo; Qi, Yilin; Hossain, Zabed; Sun, Wenjing; Qi, Xianghui
• Is Part Of: Bioresource technology. Volume 247(2018)
• Page Start: 940
• Page End: 946
• Publication Date: 2018-01
• Subjects: Lactobacillus brevis -- l-arabinose isomerase -- d-tagatose -- Spore surface-display -- Immobilization; Biomass -- Periodicals; Biomass energy -- Periodicals; Bioremediation -- Periodicals; Agricultural wastes -- Periodicals; Factory and trade waste -- Periodicals; Organic wastes -- Periodicals; Bioénergie -- Périodiques; Déchets agricoles -- Périodiques; Déchets industriels -- Périodiques; Déchets organiques -- Périodiques; Déchets (Combustible) -- Périodiques; 662.88
• DOI: 10.1016/j.biortech.2017.09.187
• Languages: English
• ISSNs: 0960-8524

Abstract

Graphical abstract: Highlights: A new strain, L. brevis PC16, producing d -tagatose was isolated and identified. A novel biocatalyst was developed and characterized via surface-displayed L-AI. The immobilized L. brevis L-AI was firstly used in the d -tagatose biosynthesis. A high efficient immobilized method for producing d -tagatose was established. Abstract: In the present study, a new strain of Lactobacillus brevis producing d -tagatose was isolated and identified. Then, the l -arabinose isomerase (L-AI) of this strain was displayed on the spore surface of Bacillus subtilis DB403 by using an anchoring protein CotG and a peptide linker (Gly–Gly–Gly–Gly–Ser). This displayed L-AI with high specific activity and stability was used as a novel immobilized biocatalyst for producing d -tagatose through batch and semi-continuous biotransformation. The conversion rate of d -tagatose from 125 g/L d -galactose was achieved 79.7% at 28 h, and the volumetric productivity reached 4.3 g/L/h at 20 h. Furthermore, the displayed L-AI showed a good performance on the reusability and remained 87% of the specific activity and 40.7% of the conversion rate after five recycles. A high efficient immobilized method for producing food-grade d -tagatose was established using spore surface-displayed L-AI.