Effect of fermented soybean meal on intestinal morphology and digestive enzyme activities in weaned piglets

Dig Dis Sci. 2007 Aug;52(8):1845-50. doi: 10.1007/s10620-006-9705-0. Epub 2007 Apr 5.

Abstract

The objective of the current experiment was to investigate the effect of Bacillus subtilis fermented soybean meal (FSBM) on intestinal morphology and digestive enzyme activities in piglets. Sixty crossbred (Duroc x Landrance x Yorkshire) piglets at an average weight of 8.62 kg were randomly allotted to two treatments and fed diets containing soybean meal (SBM) and FSBM, respectively. At the end of the experimental period, six piglets of each treatment were slaughtered humanly to collect the contents and tissue samples at three different locations in small intestine. Light microscopy and scanning electron indicated that piglets fed FSBM had a higher (P<0.05) villus height at three different locations of small intestine and had la ower (P<0.05) crypt depth in the duodenum compared to piglets fed SBM. The results showed that activities of total protease and trypsin at the duodenum and jejunum of piglets fed with FSBM increased (P<0.05) compared with the control. The trypsin activity in the pancreas of piglets decreased (P<0.05) when they were fed with FSBM. The results showed that FSBM improved intestinal morphology and digestive enzyme activities in weaned piglets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amylases / metabolism
  • Animals
  • Bacillus subtilis / metabolism
  • Chymotrypsin / metabolism
  • Diet
  • Duodenum / cytology
  • Duodenum / enzymology
  • Fermentation
  • Glycine max*
  • Ileum / cytology
  • Ileum / enzymology
  • Intestine, Small / cytology*
  • Intestine, Small / enzymology*
  • Jejunum / cytology
  • Jejunum / enzymology
  • Lipase / metabolism
  • Microscopy, Electron, Scanning
  • Peptide Hydrolases / metabolism
  • Random Allocation
  • Swine
  • Trypsin / metabolism

Substances

  • Lipase
  • Amylases
  • Peptide Hydrolases
  • Chymotrypsin
  • Trypsin