Proteolytic processing of dextransucrase of Leuconostoc mesenteroides

Citation
M. Sanchez-gonzalez et al., Proteolytic processing of dextransucrase of Leuconostoc mesenteroides, FEMS MICROB, 181(1), 1999, pp. 25-30
Citations number
21
Categorie Soggetti
Microbiology
Journal title
FEMS MICROBIOLOGY LETTERS
ISSN journal
03781097 → ACNP
Volume
181
Issue
1
Year of publication
1999
Pages
25 - 30
Database
ISI
SICI code
0378-1097(199912)181:1<25:PPODOL>2.0.ZU;2-5
Abstract
Various dextransucrase molecular mass forms found in enzyme preparations ma y sometimes be products of proteolytic activity. Extracellular protease in Leuconostoc mesenteroides strains NRRL B-512F and B-512FMC dextransucrase p reparations was identified. Protease had a molecular mass of 30 kDa and was the predominant form derived from a high molecular mass precursor. The pro duction and activity of protease in culture medium was strongly dependent o n pH. When L. mesenteroides dextransucrase (173 kDa) was hydrolyzed by prot ease, at pH 7 and 37 degrees C, various dextransucrase forms with molecular masses as low as 120 kDa conserving dextransucrase activity were obtained. (C) 1999 Published by Elsevier Science B.V. All rights reserved.