TY - JOUR
T1 - Giant bacterium (Epulopiscium fishelsoni ) influences digestive enzyme activity of an herbivorous surgeonfish (Acanthurus nigrofuscus)
AU - Pollak, Peggy E.
AU - Montgomery, W. Linn
N1 - Funding Information:
Acknowledgements--Funding was provided by the Tobias Landau Foundation (MS Helen Hayes, Director), a Fulbright Research Award (Council for International Exchange of Scholars and U.S. Information Agency), The Hebrew University, and the National Geographic Society (grant # 37 1687). The Interuniversity Institute, H. Steinitz Marine Biology Laboratory (A. Baranes, Resident Director) graciously provided space and facilities in Eilat. Professor Y. Cohen, Hebrew University and the Interuniversity Institute, served as Fulbright sponsor for Montgomery. Y. Cohen, L. Fishelson, A. Genin, A. Mazeroll, D. Shapiro and M. Leighton provided scientific advice and collaborative assistancew hile we were in Eilat. Critical comments on the manuscript were provided by P. Spruell, W. Young and P. Wheeler.
PY - 1994/8
Y1 - 1994/8
N2 - Giant bacteria (Epulopiscium fishelsoni) dominate the intestinal microbiota of brown surgeonfish, Acanthurus nigrofuscus, and reduce activity of the host's intestinal amylase, protease and lipase at physiologically relevant pH. Bacteria reduced activity of host amylase and protease directly at pH 6-8, and reduced pH-sensitive lipase activity indirectly by locally reducing pH in gut fluids. Inhibition of enzyme activity is inconsistent with a mutualistic role for the microbes relative to these host enzymes. However, high lipase activity at pH ~ 6, the pH where bacteria are dense, indicates that the bacteria counteract suppression of host lipase and contribute to lipid digestion.
AB - Giant bacteria (Epulopiscium fishelsoni) dominate the intestinal microbiota of brown surgeonfish, Acanthurus nigrofuscus, and reduce activity of the host's intestinal amylase, protease and lipase at physiologically relevant pH. Bacteria reduced activity of host amylase and protease directly at pH 6-8, and reduced pH-sensitive lipase activity indirectly by locally reducing pH in gut fluids. Inhibition of enzyme activity is inconsistent with a mutualistic role for the microbes relative to these host enzymes. However, high lipase activity at pH ~ 6, the pH where bacteria are dense, indicates that the bacteria counteract suppression of host lipase and contribute to lipid digestion.
KW - Acanthurus nigrofuscus
KW - Digestive enzyme
KW - Epulopiscium fishelsoni
UR - http://www.scopus.com/inward/record.url?scp=0028240635&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028240635&partnerID=8YFLogxK
U2 - 10.1016/0300-9629(94)90352-2
DO - 10.1016/0300-9629(94)90352-2
M3 - Article
AN - SCOPUS:0028240635
SN - 0300-9629
VL - 108
SP - 657
EP - 662
JO - Comparative Biochemistry and Physiology -- Part A: Physiology
JF - Comparative Biochemistry and Physiology -- Part A: Physiology
IS - 4
ER -