Abstract
Construction of recombinant Escherichia coli strains carrying feruloyl esterase genes for secretory expression offers an attractive way to facilitate enzyme purification and one-step production of ferulic acid from agricultural waste. A total of 10 feruloyl esterases derived from nine Lactobacillus species were expressed in E. coli BL21 (DE3) to investigate their secretion and ferulic acid production. Extracellular activity determination showed all these Lactobacillus feruloyl esterases could be secreted out of E. coli cells. However, protein analysis indicated that they could be classified as three types. The first type presented a low secretion level, including feruloyl esterases derived from Lactobacillus acidophilus and Lactobacillus johnsonii. The second type showed a high secretion level, including feruloyl esterases derived from Lactobacillus amylovorus, Lactobacillus crispatus, Lactobacillus gasseri, and Lactobacillus helveticus. The third type also behaved a high secretion level but easy degradation, including feruloyl esterases derived from Lactobacillus farciminis, Lactobacillus fermentum, and Lactobacillus reuteri. Moreover, these recombinant E. coli strains could directly release ferulic acid from agricultural waste. The highest yield was 140 μg on the basis of 0.1 g de-starched wheat bran by using E. coli expressed L. amylovorus feruloyl esterase. These results provided a solid basis for the production of feruloyl esterase and ferulic acid.
Highlights
Feruloyl esterase (E.C. 3.1.1.73), belonging to the hemicellulase family, is a type of hydrolase capable of degrading the ester bond between the ferulic acid and lignin in the cell wall of plants
Nine Lactobacillus strains belonging to L. acidophilus, L. amylovorus, L. crispatus, L. farciminis, L. fermentum, L. gasseri, L. helveticus, L. johnsonii, and L. reuteri were used to compare their feruloyl esterases
Considering the generally recognized safe status of lactic acid bacteria and the extensive application of feruloyl esterase in the food, cosmetics, and pharmaceutical industries, the feruloyl esterases produced by Lactobacillus strains have received increasing attention
Summary
Feruloyl esterase (E.C. 3.1.1.73), belonging to the hemicellulase family, is a type of hydrolase capable of degrading the ester bond between the ferulic acid and lignin in the cell wall of plants. It acts in conjunction with other cellulases and hemicellulases to synergistically open the crosslinked network structures of cell walls (Fazary et al, 2009; Várnai et al, 2014). This feature endows its applications in many areas, such as feed additives and pulp and paper industries. The produced esters have the promising potential for application as antibacterial, antiviral, and antiinflammatory drugs (Chong et al, 2019)
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