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Paper Information

Journal:   PAJOUHESH-VA-SAZANDEGI   SPRING 2006 , Volume 19 , Number 1 (70 IN ANIMAL AND FISHERIES SCIENCES); Page(s) 65 To 72.
 
Paper: 

PROTEIN DEGRADATION KINETICS OF UNTREATED AND ROASTED RAPESEED MEAL BY USING NYLON BAGS AND SDS-PAGE TECHNIQUES

 
 
Author(s):  SADEGHI A.A.*, NIKKHAH A., SHOURANG P., MORADI SHAHR BABAK M.
 
* DEPARTMENT OF ANIMAL SCIENCE AND RESEARCH BRANCH, ISLAMIC AZAD UNIVERSITY, TEHRAN, IRAN
 
Abstract: 

This study was carried out to determine rapeseed meal dry matter (DM) and crude protein (CP) degradation characteristics by using nylon bags and SDS-PAGE techniques. There were significant differences (p<0.05) between the effective rumen degradability values of untreated and roasted rapeseed meal CP at different rumen outflow rates. The rumen degradability of untreoted and treated rapeseed meal DM and CP at ruminal outflow rate of 0.05/h were 83.3 and 71.4 % for DM, 82.7 and 68.3% for CP, respectively. From the slab gel analysis, rapeseed meal proteins were composed of two major components napin and cruciferin, accounting for approximately 18.8 and 52.9 percent of the total meal protein, respectively. Both proteins were multisubunits. The molecular weights of 32.0, 26.8, 21.1, 20.5 KDa for cruciferin subunits and 8.5, 10.8 KDa for napin subunits were observed in this trial. Electrophoretic and densitometric analysis of untreated rapeseed meal protein residues revealed that napin subunits were degraded completely within 2 h, whereas the four subunits of cruciferin were not degraded after 48 h incubation. In roasted rapeseed meal, napin subunits were resistant untilll2 h incubation. The four subunits of cruciferin were more resistant to degradation. There were significant differences (p<0.05) between crude protein digestibility of untreated and roasted rapeseed meal. Crude protein digestibility of untreated rapeseed meal at 0,8, 12and 24 h incubation were 65.32, 73.28, 73.50,75.30 percent and for roasted rapeseed meal were 66.28, 71.38, 73.12, 75.50 percent. In conclusion, SDS-PAGE indicated that four subunits of cruciferin when untreated rapeseed protein, wheareas two subunits of napin and four subunits of cruciferin when roasted rapeseed protein are fed to ruminants, make the bulk of escaped protein.

 
Keyword(s): RAPESEED MEAL, ROASTING PROCESS, PROTEIN DEGRADATION, IN SITU AND ELECTROPHORESIS
 
References: 
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