“…Apart from the different functions of serine hydrolase enzymes, their catalytic triad, consisting of Ser, His and Asp (or Glu) residues, provides them with the potential to catalyse reactions by the formation and cleavage of both ester and amide bonds through similar reaction mechanisms. However, only restricted number of lipases (lipases from Candida rugosa , Aspergillus niger, Rhizomucor miehei and Pseudomonas stutzeri , Pseudomonas aerigunosa , and lipases A (CAL‐A), and B (CAL‐B)– from Candida antarctica ) have been reported to cleave amide bonds, although usually very slowly. The mechanistic difference between the two enzyme types was previously proposed to reside in the transition‐state‐stabilising hydrogen bond at the amide hydrogen of endopeptidases, which is lacking in lipases…”