Distinctive proteolytic activity of cell envelope proteinase of Lactobacillus helveticus isolated from airag, a traditional Mongolian fermented mare's milk
| Autor: | Mari Miyamoto, Taku Miyamoto, Yumi Tatsuma, Masayuki Watanabe, Hadjime Nakajima, Yasuyuki Seto, Hiroshi Ueno |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
food.ingredient
ved/biology.organism_classification_rank.species Microbiology chemistry.chemical_compound food Casein Endopeptidases Skimmed milk Animals Amino Acid Sequence Horses Gel electrophoresis Lactobacillus helveticus Sequence Homology Amino Acid biology ved/biology Cell Membrane Caseins food and beverages Mongolia General Medicine biology.organism_classification Lactic acid Milk chemistry Fermentation Proteolysis Dairy Products Bacteria Food Science Lactobacillus kefiranofaciens |
| Zdroj: | International Journal of Food Microbiology. 197:65-71 |
| ISSN: | 0168-1605 |
| Popis: | Airag is a traditional fermented milk of Mongolia that is usually made from raw mare's milk. Lactobacillus helveticus is one of the lactic acid bacteria most frequently isolated from airag. In this study, we investigated the genetic and physiological characteristics of L. helveticus strains isolated from airag and clarified their significance in airag by comparing them with strains from different sources. Six strains of L. helveticus were isolated from five home-made airag samples collected from different regions of Mongolia. The optimal temperature for acidification in skim milk was 30 to 35°C for all the Mongolian strains, which is lower than those for the reference strains (JCM 1554 and JCM 1120(T)) isolated from European cheeses. All of the strains had a prtH1-like gene encoding a variant type of cell envelope proteinase (CEP). The CEP amino acid sequence in Snow Brand Typeculture (SBT) 11087 isolated from airag shared 71% identity with PrtH of L. helveticus CNRZ32 (AAD50643.1) but 98% identity with PrtH of Lactobacillus kefiranofaciens ZW3 (AEG40278.1) isolated from a traditional fermented milk in Tibet. The proteolytic activities of the CEP from SBT11087 on artificial substrate (N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide) and pure casein were measured using an intact-cell degradation assay. The activity of the CEP from SBT11087 was observed to be weak and exhibited a lower optimal temperature (40°C) than those from the reference strains (45-50°C). The specificity of the SBT11087 CEP for αS1-casein was typical of the CEPs previously reported in L. helveticus, as determined through the degradation profiles obtained through gel electrophoresis and mass spectrometry analyses. In contrast, the degradation profile of β-casein revealed that the CEP of SBT11087 primarily hydrolyzes its C-terminal domain and hydrolyzed nine of the 16 cleavage sites shared among the CEPs of other L. helveticus strains. Thus, the CEP of SBT11087 is distinct from those from previously reported L. helveticus strains in terms of its optimal temperature and its degradation of β-casein. Therefore, the Mongolian L. helveticus strains differ from other strains of the species in different collections and are specifically suited for the natural lactic acid bacterial population in airag. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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