Alternative pig liver esterase (APLE) – Cloning, identification and functional expression in Pichia pastoris of a versatile new biocatalyst

Insights into the physiological role of pig liver esterase: Isoenzymes show differences in the demethylation of prenylated proteins

“…Hermann et al obtained similar results expressing and analysing another PLE isoenzyme (APLE). 18 However, they only detected esterase activity in the periplasm, irrespective of the existence of an ER-retention signal.…”

Enzyme Catalysis in the Synthesis of Active Pharmaceutical Ingredients

“…Although the enzyme is very efficient, its application in API production is often limited, due to its animal origin. The enzyme is a mixture of several isozymes that have recently been cloned and expressed in microorganisms [5]. The cloned enzyme is made by microbial fermentation, hence completely eliminating the risk associated with the animal origin and TSE/BSE issues of the original pig liver-derived enzyme.…”

Biocatalyst Identification and Scale‐Up: Molecular Biology for Chemists

“…Recently, recombinant PLE enzymes (including commercially produced enzyme) have become available, making its broader use in industrial applications possible once more. 20 Enzymes from other plant or animal sources may also be difficult to obtain in quantity, either due to limited access to the source material and/or difficulty in obtaining enough purified active enzyme to perform the reaction. In other cases, a less-than-suitable enzyme is available and one would like to change its properties such as its substrate selectivity or process stability, or it might be thought necessary to find a new enzyme -either by searching for one from nature and/or by engineering of existing enzymes.…”