Characterization of two acyl-acyl carrier protein thioesterases from developing Cuphea seeds specific for medium-chain- and oleoyl-acyl carrier protein

Planta ◽  
1993 ◽  
Vol 189 (3) ◽  
pp. 425-432 ◽  
Author(s):  
Peter Dörmann ◽  
Friedrich Spener ◽  
John B. Ohlrogge
2017 ◽  
Vol 214 ◽  
pp. 152-160 ◽  
Author(s):  
Wangdan Xiong ◽  
Qian Wei ◽  
Pingzhi Wu ◽  
Sheng Zhang ◽  
Jun Li ◽  
...  

2021 ◽  
Author(s):  
fangxiang hu ◽  
Weijie Cai ◽  
Junzhang Lin ◽  
Weidong Wang ◽  
Shuang Li

Abstract BackgroundSurfactin, a representative biosurfactant of popeptide mainly produced by Bacillus subtilis, consists of a cyclic heptapeptide linked to a β-hydroxy fatty acid chain. The functional activity of surfactin is closely related to the length and isomerism of the fatty acid chain. ResultsIn this study, the plant medium-chain acyl-carrier protein (ACP) thioesterase (BTE) from Umbellularia californica was overexpressed in a recombinant surfactin production strain based on B. subtilis 168. As a result, the surfactin yield after 24 h of cultivation improved by 23%, and the production rate increased from 0.112 to 0.177 g/L/h. The isoforms identified by RP-HPLC and GC-MS showed that the proportion of nC14-surfactin increased 6.4 times compared to the control strain. A comparison of further properties revealed that the product with more nC14-surfactin had higher surface activity and better performance in oil-washing. Finally, the product with more nC14-surfactin isoform had a higher hydrocarbon-emulsification index, and it increased the water-wettability of the oil-saturated silicate surface. ConclusionThe obtained results provide an original approach to modify the fatty acid chain of surfactin and further demonstrate the importance of the length and isomerism of the β-hydroxy fatty acid chain for the MEOR application of surfactin.


ChemInform ◽  
2010 ◽  
Vol 33 (22) ◽  
pp. no-no
Author(s):  
Christopher Arthur ◽  
Russell J. Cox ◽  
John Crosby ◽  
Mujiber M. Rahman ◽  
Thomas J. Simpson ◽  
...  

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