Abstract:
:The invertase of Lactobacillus reuteri CRL 1100 is a glycoprotein composed by a single subunit with a molecular weight of 58 kDa. The enzyme was stable below 45 degrees C over a wide pH range (4.5-7.0) with maximum activity at pH 6.0 and 37 degrees C. The invertase activity was significantly inhibited by bivalent metal ions (Ca(++), Cu(++), Cd(++), and Hg(++)), beta-mercaptoethanol, and dithiothreitol and partially improved by ethylenediaminetetraacetic acid. The enzyme was purified 32 times over the crude extract by gel filtration and ion-exchange chromatography with a recovery of 17%. The K(m) and V(max) values for sucrose were 6.66 mM and 0.028 micromol/min, respectively. An invertase is purified and characterized for the first time in Lactobacillus, and it proved to be a beta-fructofuranosidase.
journal_name
Curr Microbioljournal_title
Current microbiologyauthors
Cuezzo de Ginés S,Maldonado MC,Font de Valdez Gdoi
10.1007/s002849910036keywords:
subject
Has Abstractpub_date
2000-03-01 00:00:00pages
181-4issue
3eissn
0343-8651issn
1432-0991pii
10.1007/s002849910036journal_volume
40pub_type
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