The Soluble Acyl-Acyl Carrier Protein Synthetase ofVibrio harveyiB392 Is a Member of the Medium Chain Acyl-CoA Synthetase Family†

Biochemistry ◽  
2006 ◽  
Vol 45 (33) ◽  
pp. 10008-10019 ◽  
Author(s):  
Yanfang Jiang ◽  
Chi Ho Chan ◽  
John E. Cronan
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.


1997 ◽  
Vol 114 (2) ◽  
pp. 669-677 ◽  
Author(s):  
T. A. Voelker ◽  
A. Jones ◽  
A. M. Cranmer ◽  
H. M. Davies ◽  
D. S. Knutzon

2000 ◽  
Vol 28 (6) ◽  
pp. 619-622 ◽  
Author(s):  
A. Othman ◽  
C. Lazarus ◽  
T. Fraser ◽  
K. Stobart

A palmitoyl-acyl carrier protein (ACP) thioesterase cDNA clone was isolated from an oil palm cDNA library. The cDNA was expressed in Escherichia coli as a glutathione S-transferase fusion protein and a crude bacterial extract was assayed for acyl-CoA-hydrolysing activity. The recombinant enzyme was able to hydrolyse medium- and long-chain acyl-CoAs. Northernblot analysis showed a high level of gene expression in leaf, flower and 15-, 17- and 18-week mesocarp tissues. Low-level gene expression was detected in germinated seedlings and 8- and 12-week mesocarp tissues, but no transcript was detected in any kernel tissues. Southern-blot analysis indicated the presence of a single gene and we have also isolated a genomic clone using the cDNA as a probe. Two genomic fragments were subcloned and a 7 kb contiguous stretch of the oil palm genome was sequenced. Comparison of this sequence with the cDNA sequence identified a putative 93 amino acid transit peptide, most of which is missing from the cDNA. The coding region of the gene consisted of seven exons and six introns.


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