Enhancement of Lysozyme Trypsin-Mediated Decay of Intestinal Bifidobacteria and Lactobacilli
SUMMARYLysozyme-mediated lysis of Bifidobacteria and Lactobacilli was studied in in vitro tests using the agar gel plate and turbidometric Micrococcus luteus (lysodeikticus) procedure as a standard. Suspensions of the strains Bifidobacterium infantis, B. infantis liberorum, B. breve, B. longum, B. s...
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| Veröffentlicht in: | Journal of pediatric gastroenterology and nutrition 1995-07, Vol.21 (1), p.54-58 |
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| container_title | Journal of pediatric gastroenterology and nutrition |
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| creator | Heine, W Braun, O H Mohr, C Leitzmann, P |
| description | SUMMARYLysozyme-mediated lysis of Bifidobacteria and Lactobacilli was studied in in vitro tests using the agar gel plate and turbidometric Micrococcus luteus (lysodeikticus) procedure as a standard. Suspensions of the strains Bifidobacterium infantis, B. infantis liberorum, B. breve, B. longum, B. ssp, and Lactobacillus acidophilus proved to be resistant to egg white lysozyme and human milk lysozyme when incubated at 37°C in concentrations of 5, 50, and 500 mg lysozyme/L, respectively, through 30 and 60 min. Heat treatment at 100°C for 1 h and pretreatment with ether, acetone, ascorbic acid, and hydrogen peroxide failed to incline the bacteria to the lytic effects of lysozyme. Consecutive incubation of the lysozyme-pretreated bacteria with trypsin resulted in a significantly enhanced bacteriolysis in all strains of bacteria, with the exception of B. longum. The mode of action of lysozyme and proteolytic enzymes on Bifidobacteria and Lactobacilli offers an explanation for the release of microbial building blocks and their colonic absorption and retention in the breast-fed baby |
| doi_str_mv | 10.1097/00005176-199507000-00009 |
| format | Article |
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Suspensions of the strains Bifidobacterium infantis, B. infantis liberorum, B. breve, B. longum, B. ssp, and Lactobacillus acidophilus proved to be resistant to egg white lysozyme and human milk lysozyme when incubated at 37°C in concentrations of 5, 50, and 500 mg lysozyme/L, respectively, through 30 and 60 min. Heat treatment at 100°C for 1 h and pretreatment with ether, acetone, ascorbic acid, and hydrogen peroxide failed to incline the bacteria to the lytic effects of lysozyme. Consecutive incubation of the lysozyme-pretreated bacteria with trypsin resulted in a significantly enhanced bacteriolysis in all strains of bacteria, with the exception of B. longum. The mode of action of lysozyme and proteolytic enzymes on Bifidobacteria and Lactobacilli offers an explanation for the release of microbial building blocks and their colonic absorption and retention in the breast-fed baby</description><identifier>ISSN: 0277-2116</identifier><identifier>EISSN: 1536-4801</identifier><identifier>DOI: 10.1097/00005176-199507000-00009</identifier><identifier>PMID: 8576815</identifier><identifier>CODEN: JPGND6</identifier><language>eng</language><publisher>Hagerstown, MD: Lippincott-Raven Publishers</publisher><subject>Acetone - pharmacology ; Animals ; Ascorbic Acid - pharmacology ; Bacteriolysis ; Bifidobacterium - metabolism ; Bifidobacterium - physiology ; Biological and medical sciences ; Digestive system ; Dose-Response Relationship, Drug ; Ethers - pharmacology ; Hot Temperature ; Humans ; Hydrogen Peroxide - pharmacology ; Intestines - enzymology ; Intestines - microbiology ; Lactobacillus acidophilus - metabolism ; Lactobacillus acidophilus - physiology ; Medical sciences ; Micrococcus luteus - metabolism ; Micrococcus luteus - physiology ; Milk, Human - enzymology ; Muramidase - metabolism ; Pharmacology. Drug treatments ; Trypsin - metabolism</subject><ispartof>Journal of pediatric gastroenterology and nutrition, 1995-07, Vol.21 (1), p.54-58</ispartof><rights>Lippincott-Raven Publishers.</rights><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4349-589bacc356f3ddf70447732f4d42b385a812dee8450101a1a0a7859e2ebb3d263</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3594851$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8576815$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Heine, W</creatorcontrib><creatorcontrib>Braun, O H</creatorcontrib><creatorcontrib>Mohr, C</creatorcontrib><creatorcontrib>Leitzmann, P</creatorcontrib><title>Enhancement of Lysozyme Trypsin-Mediated Decay of Intestinal Bifidobacteria and Lactobacilli</title><title>Journal of pediatric gastroenterology and nutrition</title><addtitle>J Pediatr Gastroenterol Nutr</addtitle><description>SUMMARYLysozyme-mediated lysis of Bifidobacteria and Lactobacilli was studied in in vitro tests using the agar gel plate and turbidometric Micrococcus luteus (lysodeikticus) procedure as a standard. Suspensions of the strains Bifidobacterium infantis, B. infantis liberorum, B. breve, B. longum, B. ssp, and Lactobacillus acidophilus proved to be resistant to egg white lysozyme and human milk lysozyme when incubated at 37°C in concentrations of 5, 50, and 500 mg lysozyme/L, respectively, through 30 and 60 min. Heat treatment at 100°C for 1 h and pretreatment with ether, acetone, ascorbic acid, and hydrogen peroxide failed to incline the bacteria to the lytic effects of lysozyme. Consecutive incubation of the lysozyme-pretreated bacteria with trypsin resulted in a significantly enhanced bacteriolysis in all strains of bacteria, with the exception of B. longum. The mode of action of lysozyme and proteolytic enzymes on Bifidobacteria and Lactobacilli offers an explanation for the release of microbial building blocks and their colonic absorption and retention in the breast-fed baby</description><subject>Acetone - pharmacology</subject><subject>Animals</subject><subject>Ascorbic Acid - pharmacology</subject><subject>Bacteriolysis</subject><subject>Bifidobacterium - metabolism</subject><subject>Bifidobacterium - physiology</subject><subject>Biological and medical sciences</subject><subject>Digestive system</subject><subject>Dose-Response Relationship, Drug</subject><subject>Ethers - pharmacology</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Intestines - enzymology</subject><subject>Intestines - microbiology</subject><subject>Lactobacillus acidophilus - metabolism</subject><subject>Lactobacillus acidophilus - physiology</subject><subject>Medical sciences</subject><subject>Micrococcus luteus - metabolism</subject><subject>Micrococcus luteus - physiology</subject><subject>Milk, Human - enzymology</subject><subject>Muramidase - metabolism</subject><subject>Pharmacology. Drug treatments</subject><subject>Trypsin - metabolism</subject><issn>0277-2116</issn><issn>1536-4801</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU9v3CAQxVGUKtkm-QiRfIhycwsGDBzT_GukrXpJb5XQ2Iy1JNjegleR8-nLZrd7Kxc0b35vGD0IKRj9wqhRX2k-kqm6ZMZIqnJVbiVzRBZM8roUmrJjsqCVUmXFWH1KPqf0kgklJD0hJ1qqWjO5IL_vhxUMLfY4TMXYFcs5je9zj8VznNfJD-UPdB4mdMUdtjBvkadhwjT5AULxzXfejQ20E0YPBQyuWOZiq_gQ_Dn51EFIeLG_z8ivh_vn2-_l8ufj0-3NsmwFF6aU2mRDy2Xdcec6RYVQiledcKJquJagWeUQdV6dUQYMKCgtDVbYNNxVNT8j17u56zj-2eTlbO9TiyHAgOMmWZVxKRnNoN6BbRxTitjZdfQ9xNkyarfB2n_B2kOwH5LJ1sv9G5umR3cw7pPM_at9H1ILoYs5VZ8OGJdGaMkyJnbY2xhyaOk1bN4w2hVCmFb2f9_K_wJFjY-y</recordid><startdate>199507</startdate><enddate>199507</enddate><creator>Heine, W</creator><creator>Braun, O H</creator><creator>Mohr, C</creator><creator>Leitzmann, P</creator><general>Lippincott-Raven Publishers</general><general>Lippincott</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199507</creationdate><title>Enhancement of Lysozyme Trypsin-Mediated Decay of Intestinal Bifidobacteria and Lactobacilli</title><author>Heine, W ; Braun, O H ; Mohr, C ; Leitzmann, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4349-589bacc356f3ddf70447732f4d42b385a812dee8450101a1a0a7859e2ebb3d263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Acetone - pharmacology</topic><topic>Animals</topic><topic>Ascorbic Acid - pharmacology</topic><topic>Bacteriolysis</topic><topic>Bifidobacterium - metabolism</topic><topic>Bifidobacterium - physiology</topic><topic>Biological and medical sciences</topic><topic>Digestive system</topic><topic>Dose-Response Relationship, Drug</topic><topic>Ethers - pharmacology</topic><topic>Hot Temperature</topic><topic>Humans</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Intestines - enzymology</topic><topic>Intestines - microbiology</topic><topic>Lactobacillus acidophilus - metabolism</topic><topic>Lactobacillus acidophilus - physiology</topic><topic>Medical sciences</topic><topic>Micrococcus luteus - metabolism</topic><topic>Micrococcus luteus - physiology</topic><topic>Milk, Human - enzymology</topic><topic>Muramidase - metabolism</topic><topic>Pharmacology. Drug treatments</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heine, W</creatorcontrib><creatorcontrib>Braun, O H</creatorcontrib><creatorcontrib>Mohr, C</creatorcontrib><creatorcontrib>Leitzmann, P</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of pediatric gastroenterology and nutrition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heine, W</au><au>Braun, O H</au><au>Mohr, C</au><au>Leitzmann, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enhancement of Lysozyme Trypsin-Mediated Decay of Intestinal Bifidobacteria and Lactobacilli</atitle><jtitle>Journal of pediatric gastroenterology and nutrition</jtitle><addtitle>J Pediatr Gastroenterol Nutr</addtitle><date>1995-07</date><risdate>1995</risdate><volume>21</volume><issue>1</issue><spage>54</spage><epage>58</epage><pages>54-58</pages><issn>0277-2116</issn><eissn>1536-4801</eissn><coden>JPGND6</coden><abstract>SUMMARYLysozyme-mediated lysis of Bifidobacteria and Lactobacilli was studied in in vitro tests using the agar gel plate and turbidometric Micrococcus luteus (lysodeikticus) procedure as a standard. Suspensions of the strains Bifidobacterium infantis, B. infantis liberorum, B. breve, B. longum, B. ssp, and Lactobacillus acidophilus proved to be resistant to egg white lysozyme and human milk lysozyme when incubated at 37°C in concentrations of 5, 50, and 500 mg lysozyme/L, respectively, through 30 and 60 min. Heat treatment at 100°C for 1 h and pretreatment with ether, acetone, ascorbic acid, and hydrogen peroxide failed to incline the bacteria to the lytic effects of lysozyme. Consecutive incubation of the lysozyme-pretreated bacteria with trypsin resulted in a significantly enhanced bacteriolysis in all strains of bacteria, with the exception of B. longum. The mode of action of lysozyme and proteolytic enzymes on Bifidobacteria and Lactobacilli offers an explanation for the release of microbial building blocks and their colonic absorption and retention in the breast-fed baby</abstract><cop>Hagerstown, MD</cop><pub>Lippincott-Raven Publishers</pub><pmid>8576815</pmid><doi>10.1097/00005176-199507000-00009</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0277-2116 1536-4801 |
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| source | MEDLINE; Journals@Ovid Complete |
| subjects | Acetone - pharmacology Animals Ascorbic Acid - pharmacology Bacteriolysis Bifidobacterium - metabolism Bifidobacterium - physiology Biological and medical sciences Digestive system Dose-Response Relationship, Drug Ethers - pharmacology Hot Temperature Humans Hydrogen Peroxide - pharmacology Intestines - enzymology Intestines - microbiology Lactobacillus acidophilus - metabolism Lactobacillus acidophilus - physiology Medical sciences Micrococcus luteus - metabolism Micrococcus luteus - physiology Milk, Human - enzymology Muramidase - metabolism Pharmacology. Drug treatments Trypsin - metabolism |
| title | Enhancement of Lysozyme Trypsin-Mediated Decay of Intestinal Bifidobacteria and Lactobacilli |
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