Biomaterial Database

Comparison of proteolytic activities in various lactobacilli. 1995

M Sasaki, and B W Bosman, and P S Tan

Snow Brand European Research Laboratories BV, AN Groningen, The Netherlands.

A total of 169 Lactobacillus strains from 12 species (Lb. acidophilus, Lb. brevis, Lb. buchneri, Lb. casei, Lb. delbrueckii subsp. bulgaricus, Lb. delbrueckii subsp. delbrueckii, Lb. delbrueckii subsp. lactis, Lb. fermentum, Lb. helveticus, Lb. paracasei subsp. paracasei, Lb. plantarum and Lb. rhamnosus), isolated from raw milk and various milk products, and 9 Lactococcus lactis strains were evaluated for peptidase activities with five chromogenic substrates and a tryptic digest of casein. Within each species, the peptidase activity of the cell-free extracts of the strains varied. Furthermore, differences were observed between the Lactobacillus species and Lc. lactis. Lb. helveticus had by far the highest hydrolysing activities towards all substrates, indicating the presence of powerful aminopeptidases, X-prolyl-dipeptidyl aminopeptidases and proline iminopeptidases. Lb. delbrueckii subsp. bulgaricus possessed high hydrolysing activities towards substrates containing proline, alanyl-prolyl-p-nitroanilide and prolyl-p-nitroanilide. On the other hand, Lb. fermentum and Lb. brevis could be considered as weakly proteolytic species. A more detailed study with highly proteolytic Lactobacillus strains indicated that at least three different proteinases or endopeptidases were present. Compared with Lc. lactis, the Lactobacillus strains had a much lower hydrolytic action on glutamyl-glutamic acid, suggesting that glutamyl aminopeptidase was absent in lactobacilli.

UI	MeSH Term	Description	Entries
D007778	Lactobacillus	A genus of gram-positive, microaerophilic, rod-shaped bacteria occurring widely in nature. Its species are also part of the many normal flora of the mouth, intestinal tract, and vagina of many mammals, including humans. Lactobacillus species are homofermentative and ferment a broad spectrum of carbohydrates often host-adapted but do not ferment PENTOSES. Most members were previously assigned to the Lactobacillus delbrueckii group. Pathogenicity from this genus is rare.
D008892	Milk	The off-white liquid secreted by the mammary glands of humans and other mammals. It contains proteins, sugar, lipids, vitamins, and minerals.	Cow Milk,Cow's Milk,Milk, Cow,Milk, Cow's
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010450	Endopeptidases	A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.	Endopeptidase,Peptide Peptidohydrolases
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D002364	Caseins	A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.	alpha-Casein,gamma-Casein,AD beta-Casein,Acetylated, Dephosphorylated beta-Casein,Casein,Casein A,K-Casein,Sodium Caseinate,alpha(S1)-Casein,alpha(S1)-Casein A,alpha(S1)-Casein B,alpha(S1)-Casein C,alpha(S2)-Casein,alpha-Caseins,beta-Casein,beta-Caseins,epsilon-Casein,gamma-Caseins,kappa-Casein,kappa-Caseins,AD beta Casein,Caseinate, Sodium,K Casein,alpha Casein,alpha Caseins,beta Casein,beta Caseins,beta-Casein Acetylated, Dephosphorylated,beta-Casein, AD,epsilon Casein,gamma Casein,gamma Caseins,kappa Casein,kappa Caseins
D002863	Chromogenic Compounds	Colorless, endogenous or exogenous pigment precursors that may be transformed by biological mechanisms into colored compounds; used in biochemical assays and in diagnosis as indicators, especially in the form of enzyme substrates. Synonym: chromogens (not to be confused with pigment-synthesizing bacteria also called chromogens).	Chromogenic Compound,Chromogenic Substrate,Chromogenic Substrates,Compound, Chromogenic,Compounds, Chromogenic,Substrate, Chromogenic,Substrates, Chromogenic
D006868	Hydrolysis	The process of cleaving a chemical compound by the addition of a molecule of water.
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia

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