Chopped alfalfa and chopped whole-plant corn were ensiled and the proteolytic changes which occurred during ensiling were investigated. Proteolysis was measured in terms of end-products of protein degradation and by protein isolation followed by electrophoresis. The effects of formic acid and ammonia, applied at the time of ensiling, on proteolytic changes were investigated. / Alfalfa treated with formic acid contained significantly reduced levels of NH$ sb3$-N and NPN compared to control silage; ammonia (NH$ sb3$)-treated alfalfa silage had significantly less NPN (P $<$ 0.05). After 90d of storage, formic acid-treated and NH$ sb3$-treated alfalfa silage contained lower levels of both branched and non-branched amino acids, sulfur containing, and basic amino acids compared to control silage; formic acid-treated and NH$ sb3$-treated corn silage contained lower levels of branched chain amino acids and sulfur containing amino acids after the same time period. Formic acid and ammonia were most effective in the reduction of proteolysis in alfalfa silage and corn silage, respectively. The protein ribulose 1,5-diphosphate carboxylase (RuDPCase) was depleted completely after 2d of fermentation in control silage. Conditions in NH$ sb3$-treated alfalfa silage stabilized RuDPCase during the first 24h of storage.
Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.75861 |
Date | January 1988 |
Creators | Fairbairn, Robert L. |
Publisher | McGill University |
Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
Language | English |
Detected Language | English |
Type | Electronic Thesis or Dissertation |
Format | application/pdf |
Coverage | Doctor of Philosophy (Department of Food Science and Agricultural Chemistry.) |
Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
Relation | alephsysno: 000730727, proquestno: AAINL48608, Theses scanned by UMI/ProQuest. |
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