{"id":{"repo_id":"vu-aus","oai_identifier":"oai:eprints.vu.edu.au:15367"},"canonical_url":"https://search.dev.ndltd.org/etd/vu-aus/oai:eprints.vu.edu.au:15367","repository":{"repo_id":"vu-aus","name":"Victoria University (Australia)","base_url":"https://vuir.vu.edu.au/cgi/oai2"},"display":{"title":"The proteolytic activity of yoghurt and probiotic bacteria for the improved viability of probiotic bacteria in fermented milk products","abstract":"The proteolytic activity of various strains of yoghurt and probiotic bacteria, particularly their amino-, di-, tri- and endo-peptidase activities was studied. Nine strains of Streptococcus thermophilus, 6 strains of Lactobacillus delbrueckii ssp. bulgaricus, 14 strains of Lactobacillus acidophilus and 13 strains of Bifidobacterium ssp. were screened for proteolytic activity by using the o-phthaldialdehyde based spectrophotometric assay. Those strains showing the highest and lowest proteolytic activity were further studied for their peptidase activities at the extracellular and intracellular levels. Aminopeptidase activities were measured using chromogenic substrates (p-nitroanilide derivatives of Lanomers of leucine, lysine, alanine, proline, arginine, and methionine). Dipeptidase activities were measured using dipeptides including Ala-Met, Leu-Tyr, Leu-Gly, Ala-His, and Pro-lLe as substrates. Endopeptidase and tripeptidase activities were detected using thin-layer chromatography.","abstract_html":"The proteolytic activity of various strains of yoghurt and probiotic bacteria, particularly their amino-, di-, tri- and endo-peptidase activities was studied. Nine strains of Streptococcus thermophilus, 6 strains of Lactobacillus delbrueckii ssp. bulgaricus, 14 strains of Lactobacillus acidophilus and 13 strains of Bifidobacterium ssp. were screened for proteolytic activity by using the o-phthaldialdehyde based spectrophotometric assay. Those strains showing the highest and lowest proteolytic activity were further studied for their peptidase activities at the extracellular and intracellular levels. Aminopeptidase activities were measured using chromogenic substrates (p-nitroanilide derivatives of Lanomers of leucine, lysine, alanine, proline, arginine, and methionine). Dipeptidase activities were measured using dipeptides including Ala-Met, Leu-Tyr, Leu-Gly, Ala-His, and Pro-lLe as substrates. Endopeptidase and tripeptidase activities were detected using thin-layer chromatography.","abstract_has_math":false,"creators":["Shihata, Amal"],"institution":"Victoria University of Technology","degree_name":"phd","degree_level":"doctoral","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2004,"date_issued":"2004","date_published":"2004","updated_at":"2026-07-24T06:33:09Z","subjects":["0908 Food Sciences","0605 Microbiology","School of Engineering and Science"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Shihata, Amal"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2004"]},{"key":"dc:date.issued","label":"Date","values":["2004"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["School of Molecular Sciences"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["Victoria University of Technology"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["https://vuir.vu.edu.au/15367/"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["doctoral"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["phd"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["0908 Food Sciences","0605 Microbiology","School of Engineering and Science"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://vuir.vu.edu.au/15367/3/SHIHATA%20Amal-thesis_nosignature.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The proteolytic activity of various strains of yoghurt and probiotic bacteria, particularly their amino-, di-, tri- and endo-peptidase activities was studied. Nine strains of Streptococcus thermophilus, 6 strains of Lactobacillus delbrueckii ssp. bulgaricus, 14 strains of Lactobacillus acidophilus and 13 strains of Bifidobacterium ssp. were screened for proteolytic activity by using the o-phthaldialdehyde based spectrophotometric assay. Those strains showing the highest and lowest proteolytic activity were further studied for their peptidase activities at the extracellular and intracellular levels. Aminopeptidase activities were measured using chromogenic substrates (p-nitroanilide derivatives of Lanomers of leucine, lysine, alanine, proline, arginine, and methionine). Dipeptidase activities were measured using dipeptides including Ala-Met, Leu-Tyr, Leu-Gly, Ala-His, and Pro-lLe as substrates. Endopeptidase and tripeptidase activities were detected using thin-layer chromatography."]},{"key":"dc:format","label":"Dc Format","values":["text"]},{"key":"dc:title","label":"Title","values":["The proteolytic activity of yoghurt and probiotic bacteria for the improved viability of probiotic bacteria in fermented milk products"]}]}],"canonical_facts":{"dc:creator":["Shihata, Amal"],"dc:date":["2004"],"dc:date.issued":["2004"],"dc:description.abstract":["The proteolytic activity of various strains of yoghurt and probiotic bacteria, particularly their amino-, di-, tri- and endo-peptidase activities was studied. Nine strains of Streptococcus thermophilus, 6 strains of Lactobacillus delbrueckii ssp. bulgaricus, 14 strains of Lactobacillus acidophilus and 13 strains of Bifidobacterium ssp. were screened for proteolytic activity by using the o-phthaldialdehyde based spectrophotometric assay. Those strains showing the highest and lowest proteolytic activity were further studied for their peptidase activities at the extracellular and intracellular levels. Aminopeptidase activities were measured using chromogenic substrates (p-nitroanilide derivatives of Lanomers of leucine, lysine, alanine, proline, arginine, and methionine). Dipeptidase activities were measured using dipeptides including Ala-Met, Leu-Tyr, Leu-Gly, Ala-His, and Pro-lLe as substrates. Endopeptidase and tripeptidase activities were detected using thin-layer chromatography."],"dc:format":["text"],"dc:identifier.uri":["https://vuir.vu.edu.au/15367/3/SHIHATA%20Amal-thesis_nosignature.pdf"],"dc:language":["en"],"dc:publisher.department":["School of Molecular Sciences"],"dc:publisher.institution":["Victoria University of Technology"],"dc:relation.isreferencedby":["https://vuir.vu.edu.au/15367/"],"dc:subject":["0908 Food Sciences","0605 Microbiology","School of Engineering and Science"],"dc:title":["The proteolytic activity of yoghurt and probiotic bacteria for the improved viability of probiotic bacteria in fermented milk products"],"dc:type":["Thesis"],"dc:type.qualificationlevel":["doctoral"],"dc:type.qualificationname":["phd"]},"updated_at":"2026-07-24T06:33:09Z"}