TY - JOUR
T1 - Efficient production of d -tagatose using a food-grade surface display system
AU - Liu, Yi
AU - Li, Sha
AU - Xu, Hong
AU - Wu, Lingtian
AU - Xu, Zheng
AU - Liu, Jing
AU - Feng, Xiaohai
PY - 2014/7/16
Y1 - 2014/7/16
N2 - d-Tagatose, a functional sweetener, is commonly transformed from d-galactose by l-arabinose isomerase (l-AI). In this study, a novel type of biocatalyst, l-AI from Lactobacillus fermentum CGMCC2921 displayed on the spore surface of Bacillus subtilis 168, was developed for producing d-tagatose. The anchored l-AI, exhibiting the relatively high bioactivity, suggested that the surface display system using CotX as the anchoring protein was successfully constructed. The stability of the anchored l-AI was significantly improved. Specifically, the consolidation of thermal stability representing 87% of relative activity was retained even at 80 °C for 30 min, which remarkably favored the production of d-tagatose. Under the optimal conditions, the robust spores can convert 75% d-galactose (100 g/L) into d-tagatose after 24 h, and the conversion rate remained at 56% at the third cycle. Therefore, this biocatalysis system, which could express the target enzyme on the food-grade vector, was an alternative method for the value-added production of d-tagatose.
AB - d-Tagatose, a functional sweetener, is commonly transformed from d-galactose by l-arabinose isomerase (l-AI). In this study, a novel type of biocatalyst, l-AI from Lactobacillus fermentum CGMCC2921 displayed on the spore surface of Bacillus subtilis 168, was developed for producing d-tagatose. The anchored l-AI, exhibiting the relatively high bioactivity, suggested that the surface display system using CotX as the anchoring protein was successfully constructed. The stability of the anchored l-AI was significantly improved. Specifically, the consolidation of thermal stability representing 87% of relative activity was retained even at 80 °C for 30 min, which remarkably favored the production of d-tagatose. Under the optimal conditions, the robust spores can convert 75% d-galactose (100 g/L) into d-tagatose after 24 h, and the conversion rate remained at 56% at the third cycle. Therefore, this biocatalysis system, which could express the target enzyme on the food-grade vector, was an alternative method for the value-added production of d-tagatose.
KW - biocatalysis
KW - d -tagatose
KW - l -arabinose isomerase
KW - spore surface display
UR - http://www.scopus.com/inward/record.url?scp=84904430838&partnerID=8YFLogxK
U2 - 10.1021/jf501937j
DO - 10.1021/jf501937j
M3 - 文章
C2 - 24979201
AN - SCOPUS:84904430838
SN - 0021-8561
VL - 62
SP - 6756
EP - 6762
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 28
ER -