Abstract

The question of how to distinguish between lipases and esterases is about as old as the definition of the subclassification is. Many different criteria have been proposed to this end, all indicative but not decisive. Here, the activity of lipases in dry organic solvents as a criterion is probed on a minimal α/β hydrolase fold enzyme, the Bacillus subtilis lipase A (BSLA), and compared to Candida antarctica lipase B (CALB), a proven lipase. Both hydrolases show activity in dry solvents and this proves BSLA to be a lipase. Overall, this demonstrates the value of this additional parameter to distinguish between lipases and esterases. Lipases tend to be active in dry organic solvents, while esterases are not active under these circumstances.

Highlights

  • Lipases and esterases both catalyze the hydrolysis of esters. This has led to the longstanding question: how can we distinguish between a lipase and an esterase? As the simple hydrolysis of an ester does not suffice, a range of different criteria has been suggested [1,2,3,4,5]

  • To probe whether aw is a suitable parameter to distinguish between lipases and esterases and between lipases and other hydrolases in general, we studied the behavior of Bacillus subtilis

  • The pdb between enzyme and all theare other enzymesby area determined by a statistical principal component codes of the The processed enzyme indicated in different colors according to colors their class: lipases analysis

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Summary

Introduction

Lipases and esterases both catalyze the hydrolysis of esters. This has led to the longstanding question: how can we distinguish between a lipase and an esterase? As the simple hydrolysis of an ester does not suffice, a range of different criteria has been suggested [1,2,3,4,5]. (1) The oldest distinction is the kinetic and structural criterion of interfacial activation, which was already described in 1936 [6]. (5) The activity of the enzyme in the presence of (water-miscible) organic solvents has been proposed as a property of lipases, but other enzymes fulfill this criterion, too [2,10,11,12,13,14]. BSLA is a small (181 amino acids, 19 kDa) serine hydrolase (Figure 1) It is Catalysts 2019, 9, x FOR PEER REVIEW neither interfacially activated nor does it have a lid (criteria one and two) [9,22,23,24] and sequence datainterfacially are not conclusive, butdoes it is ait minimal hydrolase enzyme [9,23,25]. (BSLA) is the smallest with an an α/βα/β hydrolase fold.fold

Bacillus subtilis smallestserine serinehydrolase hydrolase with hydrolase
Results
Amidase
BSLA Activity in Dry Organic Solvents
Discussion
Materials
Methods
BioGPS Computational Analysis
Findings
Conclusions
Full Text
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