Medium Chain Fatty Acid
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2021 ◽  
Vol 87 ◽  
pp. 104724
Author(s):  
P.G. Roopashree ◽  
Shilpa S. Shetty ◽  
N. Suchetha Kumari

2021 ◽  
Author(s):  
Qingzhuoma Yang ◽  
Shengtao Guo ◽  
Qi Lu ◽  
Yong Tao ◽  
Decong Zheng ◽  
...  

Coenzyme A transferases (CoATs) are important enzymes involved in carbon chain elongation, contributing to medium-chain fatty acid (MCFA) biosynthesis. For example, butyryl-CoA:acetate CoA transferase (BCoAT) is responsible for the final step of butyrate synthesis from butyryl-CoA. However, little is known about caproyl-CoA:acetate CoA-transferase (CCoAT), which is responsible for the final step of caproate synthesis from caproyl-CoA. In this study, two CoAT genes from Ruminococcaceae bacterium CPB6 and Clostridium tyrobutyricum BEY8 were identified by gene cloning and expression analysis. Enzyme assays and kinetic studies were carried out using butyryl-CoA or caproyl-CoA as the substrate. CPB6-CoAT can catalyze the conversion of both butyryl-CoA to butyrate and caproyl-CoA to caproate, but its catalytic efficiency with caproyl-CoA as the substrate was 3.8 times higher than that with butyryl-CoA. In contrast, BEY8-CoAT had only BCoAT activity, not CCoAT activity. This demonstrated the existence of a specific CCoAT involved in chain elongation via the reverse β-oxidation pathway. Comparative bioinformatics analysis showed the presence of a highly conserved motif (GGQXDFXXGAXX) in CoATs, which is predicted to be the active center. Single point mutations in the conserved motif of CPB6-CoAT (Asp346 and Ala351) led to marked decreases in the activity for butyryl-CoA and caproyl-CoA, indicating that the conserved motif is the active center of CPB6-CoAT and that Asp346 and Ala351 have a significant impact on the enzymatic activity. This work provides insight into the function of CCoAT in caproic acid biosynthesis and improves understanding of the chain elongation pathway for MCFA production.


Food Research ◽  
2021 ◽  
Vol 5 (2) ◽  
pp. 214-220
Author(s):  
H. Jadhav ◽  
J. Waghmare ◽  
U. Annapure

Flavour emulsion is used in a wide range of food products including carbonated beverages, dairy products, confectionaries, and bakery products. Among its food applications are extensive uses in bakery products due to its high heat resistant properties. In flavour emulsion flavour oil is suspended in water phase and this water phase retains flavour even if such flavour emulsion is used for high temperature food application like baking. But flavour extracts are made by suspending flavour oil in alcohol. So, such flavour extracts are not suitable for high temperature food processing, since alcohol evaporates at high temperature. Thus, flavour emulsion is much better than flavour extracts. The stability of flavour emulsion depends on the emulsifier used in making flavour emulsion. Monocaprylin and dicaprylin are mono and diglyceride of mediumchain fatty acids having very good emulsifying properties. The stability of flavour emulsion can be improved by making use of mono and diglyceride as an emulsifier. The present study focused on the development of stable flavour emulsion from fruit waste using mono and diglyceride of medium-chain fatty acid as an emulsifier. The stable flavour emulsion is made from orange oil, water and emulsifier using ultra high-pressure homogenizer with 25 MPa pressure. Emulsifier mono and dicaprylin were synthesized by the esterification reaction between glycerol and caprylic acid. The effect of various combination of mono and dicaprylin is studied on the formation of stable flavour emulsion. The higher monocaprylin content in the emulsifier combination showed excellent results and a good synergistic effect on the stability of the emulsion. The combination of mono: diglyceride which resulted in the formation of stable flavour emulsion is 80:20 at 10% concentration, 2 passes and 25 mPa pressure in a high-pressure homogenizer. The stability of flavour emulsion was investigated using a storage study. The emulsion was found to be stable for 30 days at ambient temperature (25ºC) and refrigeration temperature (4ºC) but showed low stability at 50ºC.


2021 ◽  
Author(s):  
Qingzhuoma Yang ◽  
Shengtao Guo ◽  
Qi Lu ◽  
Yong Tao ◽  
Decong Zheng ◽  
...  

AbstractCoenzyme A transferases (CoATs) are important enzymes involved in carbon chain elongation contributing to medium-chain fatty acid (MCFA) biosynthesis. For example, butyryl-CoA:acetate CoA transferase (BCoAT) is responsible for the final step of butyrate synthesis from butyryl-CoA. However, little is known about caproyl-CoA:acetate CoA-transferase (CCoAT), which is responsible for the final step of caproate synthesis from caproyl-CoA. In this study, two CoAT genes from Ruminococcaceae bacterium CPB6 and Clostridium tyrobutyricum BEY8 were identified by gene cloning and expression analysis. The enzyme assays and kinetic studies were carried out using butyryl-CoA or caproyl-CoA as the substrate. CPB6-CoAT can catalyze the conversion of both butyryl-CoA to butyrate and caproyl-CoA to caproate, but its catalytic efficiency with caproyl-CoA as the substrate was 3.8 times higher than that with butyryl-CoA. In contrast, BEY8-CoAT had only BCoAT activity, not CCoAT activity. This demonstrated the existence of a specific CCoAT involved in chain elongation via the reverse β-oxidation pathway. Comparative bioinformatics analysis showed the presence of a highly conserved motif (GGQXDFXXGAXX) in CoATs, which is predicted to be the active center of CoATs. Single point mutations in the conserved motif of CPB6-CoAT (Asp346 and Ala351) led to marked decreases in the activity for butyryl-CoA and caproyl-CoA, indicating that the conserved motif is the active center of CPB6-CoAT, and sites Asp346 and Ala351 were critical residues that affect enzymatic activity. This work provides insight into the function of CCoAT in caproic acid biosynthesis and improves the understanding of the chain elongation pathway for MCFA production.


2021 ◽  
Author(s):  
Leonie Baumann ◽  
Tyler Doughty ◽  
Verena Siewers ◽  
Jens Nielsen ◽  
Eckhard Boles ◽  
...  

Abstract The medium-chain fatty acid octanoic acid is an important platform compound widely used in industry. The microbial production from sugars in Saccharomyces cerevisiae is a promising alternative to current non-sustainable production methods, however, titers need to be further increased. To achieve this, it is essential to have in-depth knowledge about the cell's physiology during octanoic acid production. To this end, we collected the first RNA-Seq data of an octanoic acid producer strain at three time points during fermentation. The strain produced higher levels of octanoic acid and increased levels of fatty acids of other chain lengths (C6-C18) but showed decreased growth compared to the reference. Furthermore, we show that the here analyzed transcriptomic response to internally produced octanoic acid is notably distinct from a wild type's response to externally supplied octanoic acid as reported in previous publications. By comparing the transcriptomic response of different sampling times, we identified several genes that we subsequently overexpressed and knocked out, respectively. Hereby we identified RPL40B, to date unknown to play a role in fatty acid biosynthesis or medium-chain fatty acid tolerance. Overexpression of RPL40B led to an increase in octanoic acid titers by 40%.


2021 ◽  
Vol 25 (02) ◽  
pp. 455-459
Author(s):  
Chunyin Geng

The aim of this study was to evaluate the effect of two typical yeast preparation (ADY and YC) supplementation on the concentration of ruminal medium chain fatty acid, lactic acid, ethanol and the abundance of relative rumen bacteria in finishing beef cattle. The results showed that ADY supplementation significantly increased the concentration of caproate (C6:0) (P < 0.05) and tended to increase the content of total medium chain fatty acids (P = 0.094), while had no significant effect on concentration of caprylate (C8:0) and caprate (C10:0) (P > 0.1). YC supplementation did not show a significant effect on the content of total medium chain fatty acids and the concentration of individual volatile acids (P > 0.1); ADY supplementation significantly decreased the concentration of lactic acid (P < 0.05) and has a tendency to decrease the ethanol concentration (P = 0.057). YC did not affect significantly the concentration of lactic acid and ethanol (P > 0.1); Both ADY and YC supplementation significantly decreased relative abundance of B. fibrisolvens (P < 0.05) and increased relative abundance S. ruminantium (P < 0.05), and YC rather than ADY tended to increase relative abundance of S. bovis (P= 0.053). Furthermore, both ADY and YC did not show the significant effect on relative abundance of M. elsdenii and C. kluyveri (P > 0.1). These data suggested that there are significant differences between ADY and YC in the effects on rumen metabolites including MCFAs, ethanol and lactic acid, and increased concentration of caproate (C6:0) in rumen may be responsible for the increment of circulating ghrelin caused by ADY supplementation finishing bull. © 2021 Friends Science Publishers


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