Details

Autor(en) / Beteiligte

• Rollan, G
• De Angelis, M
• Gobbetti, M
• Valdez, G.F. de

Titel

Proteolytic activity and reduction of gliadin-like fractions by sourdough lactobacilli

Ist Teil von

• Journal of applied microbiology, 2005-01, Vol.99 (6), p.1495-1502

Ort / Verlag

Oxford, UK: Blackwell Science Ltd

Erscheinungsjahr

2005

Quelle

Wiley Online Library - AutoHoldings Journals

Beschreibungen/Notizen

• Aims: To characterize the peptide hydrolase system of Lactobacillus plantarum CRL 759 and CRL 778 and evaluate their proteolytic activity in reducing gliadin-like fractions. Methods and Results: The intracellular peptide hydrolase system of Lact. plantarum CRL 759 and CRL 778 involves amino-, di- (DP), tri- (TP) and endopeptidase activities. These peptidases are metalloenzymes inhibited by EDTA and 1,10-phenanthroline and stimulated by Co(2+). DP and TP activities of Lact. plantarum CRL 759 and CRL 778, respectively, were completely inhibited by Cu(2+). Lactobacillus plantarum CRL 778 showed the highest proteolytic activity and amino acids release in fermented dough. The synthetic 31-43 alpha-gliadin fragment was hydrolysed to 36% and 73% by Lact. plantarum CRL 778 and CRL 759 respectively. Conclusions: Lactobacillus plantarum CRL 759 and CRL 778 have an active proteolytic system, which is responsible for the high amino acid release during sourdough fermentation and the hydrolysis of the 31-43 alpha-gliadin-like fragment. Significance and Impact of the Study: This work provides new information of use when obtaining sourdough starters for bread making. Moreover, knowledge regarding lactobacilli capable of reducing the level of gliadin-like fractions, a toxic peptide for coeliac patients, has a beneficial health impact.