Esterase plays a major role in the degradation of natural materials and industrial pollutants, viz, cereal wastes, plastics, and other toxic chemicals It is useful in the synthesis of optically pure compounds, perfumes, and antioxidants The potential applications of esterase with reference to agriculture, food, and pharmaceutical industries, are discussed in this review Promising applications in this avenue can be supported by appropriate production strategies

Production and applications of esterases

Physico-chemical pre-treatment and biotransformation of wastewater and wastewater Sludge – Fate of bisphenol A

Screening and characterization of a novel esterase from a metagenomic library.

Enzyme technology is an ever-growing field of knowledge and, in recent years, this technology has raised renewed interest, due to the search for new paradigms in several productive processes. Lipases, esterases and cutinases are enzymes used in a wide range of processes involving synthesis and hydrolysis reactions. The objective of this work was to investigate and compare the specific lipase and esterase activities of five enzymes - four already classified as lipases and one classified as cutinase - in the presence of natural and synthetic substrates. All tested enzymes presented both esterase and lipase specific activities. The highest specific esterase activity was observed for Aspergillus 1068 lipase in natural substrate and for F. oxysporum cutinase in synthetic substrate, while the highest specific lipase activity was observed for Geotrichum sp. lipase in natural substrate and for F. oxysporum cutinase in synthetic substrate. These results display some interface-independent lipolytic activity for all lipases tested. This is in accordance with the rationale that a new and broader definition of lipases may be necessary.

https://www.scielo.br/pdf/cta/v31n3/a09v31n3.pdf

Lipase and esterase: to what extent can this classification be applied accurately?

Enzyme technology is an ever-growing field of knowledge and, in recent years, this technology has raised renewed interest, due to the search for new paradigms in several productive processes. Lipases, esterases and cutinases are enzymes used in a wide range of processes involving synthesis and hydrolysis reactions. The objective of this work was to investigate and compare the specific lipase and esterase activities of five enzymes – four already classified as lipases and one classified as cutinase - in the presence of natural and synthetic substrates. All tested enzymes presented both esterase and lipase specific activities. The highest specific esterase activity was observed for Aspergillus 1068 lipase in natural substrate and for F. oxysporum cutinase in synthetic substrate, while the highest specific lipase activity was observed for Geotrichum sp. lipase in natural substrate and for F. oxysporum cutinase in synthetic substrate. These results display some interface-independent lipolytic activity for all lipases tested. This is in accordance with the rationale that a new and broader definition of lipases may be necessary.

http://repositorio.unicamp.br/jspui/bitstream/REPOSIP/108427/1/2-s2.0-80054989587.pdf

Lipase And Esterase - To What Extent Can This Classification Be Applied Accurately? [lipases E Esterases: Como Definir E Classificar?]

To isolate novel strains expressing an esterase that hydrolyzed the rac-ketoprofen ethyl ester to (S)-ketoprofen in the stereospecific manner, we screened broad ecological niches and soil samples in which the activity was expected to be found. Thousands of microbial strains were tested to determine their ester-hydrolyzing activity by using an agar plate containing insoluble tributyrin as an indicative substrate, and then further screened by activity on the (R, S)-ketoprofen ethyl ester. Twenty-eight strains were screened primarily and compared with respect to the potential to ketoprofen ethyl ester-hydrolyzing activity in terms of conversion yield and chiral specificity. Consequently, a strain S34 was isolated as a best producer and finally identified as a Pseudomonas sp. S34. We first formulated the optimal medium for the high level production of the enzyme, and as a preliminary experiment for enzymatic resolution, we characterized the fractionated enzyme. The enzyme with ketoprofen ethyl ester-hydrolyzing activity to (S)-ketoprofen showed a high degree of enantioselectivity (>94%) and was mainly found in cell extracts, whereas no distinct activity was detected in culture broth. The optimum pH and temperature of the enzyme were 9.5 and 35 °C, respectively. The activity of the enzyme was markedly increased (four-fold) by addition of a non-ionic detergent Triton X-100 and, resultantly, a high activity toward ketoprofen ethyl ester (52 U/mg) was found. The small-scale conversion of (R, S)-ketoprofen ethyl ester to (S)-ketoprofen using the partially purified enzymes was completed in 28 h, with optical purity of 99% and yield of 47%.

Jeong-Bog Lee

Papers

Screening, production and properties of a stereospecific esterase from Pseudomonas sp. S34 with high selectivity to (S)-ketoprofen ethyl ester