Comment to Sherr and Sherr (1999): "Is there any appropriate way to distinguish different beta-N-acetylhexosaminidase activities in aquatic environments?"
J. Vrba, Comment to Sherr and Sherr (1999): "Is there any appropriate way to distinguish different beta-N-acetylhexosaminidase activities in aquatic environments?", FEMS MIC EC, 33(1), 2000, pp. 81-84
The recent paper of Sherr and Sherr on detecting low-affinity beta-glucosam
inidase activity in several marine microbes extends current knowledge about
hydrolytic enzyme activities in natural aquatic systems. However, their co
nclusions regarding the whole-cell assay with MUF-N-acetyl-beta-D-glucosami
nide (MUF-[GlcNAc]) cannot be accepted. First, we explicitly demonstrate a
strong correlation between extracellular activities of the high-affinity en
zymes and grazing rates of bacterivorous protists. Therefore, the assay can
still be recommended for the estimation of total protistan grazing on prok
aryotic picoplankton. Second, the ability of many aquatic organisms to prod
uce enzymes which cleave fluorogenic substrates, such as MUF-[GlcNAc] and/o
r MUF-beta-D-N,N',N"-triacetylchitotriose (MUF-[GlcNAc](3)), has been well-
documented during the last decade. Thus, neither of the two substrates may
be considered as exclusively specific for targeting either lysozymes or bet
a-N-acetylhexosaminidases. (C) 2000 Federation of European Microbiological
Societies. Published by Elsevier Science B.V. All rights reserved.