Inhibitory effects of plant polyphenoloxidase on colonization factors of Streptococcus sobrinus 6715.
Exogenously added polyphenoloxidase (EC 1.14.18.1), an enzyme which oxidizes tyrosine residues and is commonly found in many dietary components, abolished the aggregation of Streptococcus sobrinus 6715 by high-molecular-weight dextran. The enzyme decreased glucan-binding lectin and/or glucosyltransferase I activities.
Cowan
M M
MM
Department of Microbiology, Miami University, Oxford, Ohio 45056, USA. cowanmm@muohio.edu
Horst
E A
EA
Luengpailin
S
S
Doyle
R J
RJ
D001422:Bacterial Adhesion / Q000187:drug effects; D001426:Bacterial Proteins; D004156:Catechol Oxidase / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D015169:Colony Count, Microbial; D003911:Dextrans / Q000494:pharmacology; D005936:Glucans / Q000378:metabolism; D005964:Glucosyltransferases; D006801:Humans; D037102:Lectins / Q000378:metabolism; D037121:Plant Lectins; D010944:Plants / Q000737:chemistry* / Q000201:enzymology; D011506:Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D016986:Streptococcus sobrinus / Q000187:drug effects* / Q000502:physiology
D001426:Bacterial Proteins; D003911:Dextrans; D005936:Glucans; D037102:Lectins; D037121:Plant Lectins; D011506:Proteins; C067118:GTF-I protein, Streptococcus; D004156:Catechol Oxidase; D005964:Glucosyltransferases; C489364:glucosyltransferase I