Title page for ETD etd-12142011-170539


Type of Document Master's Thesis
Author Ramirez, Elizabeth Maria
URN etd-12142011-170539
Title Variations in Amino Acid Standardized Ileal Digestibility in Soybean Meal
Degree Master of Science
Department Animal and Poultry Sciences
Advisory Committee
Advisor Name Title
Escobar, Jeffery Committee Chair
Hanigan, Mark D. Committee Member
Scheffler, Jason M. Committee Member
Keywords
  • soybean meal
  • digestibility
  • amino acid
  • broiler
Date of Defense 2011-12-05
Availability unrestricted
Abstract
Soybean meal (SBM) is a staple proteinaceous feedstuff in diets for monogastric animals like poultry and swine. It is known that soybeans contain several anti-nutritional factors that, if untreated, results in decreased quality and bioavailability of amino acids (AA). Thermal processing via heat treatment of soybeans and SBM is essential for inactivation of these anti-nutritional factors; however, over-processing may result in extensive AA damage, particularly lysine. Feeding heat damaged SBM has been proven to be an inefficient source of AA for monogastrics as they cannot be used for any metabolic function. In typical corn-soybean meal diets for pigs and poultry, lysine is the first- and second- limiting AA, respectively. Currently, laboratory procedures are unable to accurately determine digestible lysine in SBM. The objective of this thesis was to compare SBM AA digestibility obtained from 28-day old broilers to values obtained from an in vitro digestion procedure. The correlation between AA concentration in the SBM and its in vivo standardized ileal digestibility (SID) was also analyzed. Twenty-four SBM samples (21 from U.S.A., 2 from Canada, and 1 from Mexico) were analyzed. In vivo lysine SID ranged from 69-93%. Results indicated no correlation (r = -0.16 to 0.21; P = 0.33 to 0.98) between analyzed AA content in SBM and in vivo SID. An increase in lysine SID was associated with an increase in the SID of phenylalanine, leucine, isoleucine, valine, tyrosine, alanine, threonine, glutamate, aspartate, methionine, histidine, and glycine (r² = 0.63 to 0.93; P < 0.001). Poor association was determined between lysine proline, arginine, and serine (r² = 0.14 to 0.43; P = 0.001 to 0.003). Lastly, results indicated no association (r² = 0.00 to 0.08; P = 0.17 to 0.99) between in vivo and in vitro SID for any of the AA tested. In summary, it appears that lysine may be a good indicator for SID estimations for most essential AA; however, SBM content of a particular AA is not a good indicator of its digestibility. Additionally, current in vitro digestibility techniques seemed inadequate in identifying in vivo SID differences and further analytical improvements are needed.
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