Degradation of Cry1Ab Protein Within Transgenic Bt Maize Tissue by Composite Microbial System of MC1

Environmental safety issues involved in transgenic plants have become the concern of researchers, practitioners and policy makers in recent years. Potential differences between Bt maize（ND1324 and ND2353 expressing the insecticidal Cry1Ab protein） and near-isogenic non-Bt varieties（ND1392 and ND223） in their influence on the composite microbial system of MC1 during the fermentation process were studied during 2011-2012. Cry1Ab protein in Bt maize residues didn＇t affect characteristics of lignocellulose degradation by MC1, pH of fermentation broth decreasing at initial stage and increasing at later stage of degradation. The quality of various volatile products in fermentation broth showed that no signifi cant difference of residues fermentation existed between Bt maize and non-Bt maize. During the fermentation MC1 efficiently degraded maize residues by 83%-88%, and cellulose, hemicelluloses and lignin content decreased by 70%-72%, 72%-75% and 30%-37%, respectively. Besides that, no consistent difference was found between Bt and non-Bt maize residues lignocellulose degradation by MC1 during the fermentation process. MC1 degraded 88%-89% Cry1Ab protein in Bt maize residues, and in the fermentation broth of MC1 and bacteria of MC1 Cry1Ab protein was not detected. DGGE profi le analyses revealed that the microbial community drastically changed during 1-3 days and became stable until the 9th day. Though the dominant strains at different fermentation stages had signifi cantly changed, no difference on the dominant strains was observed between Bt and non-Bt maize at different stages. Our study indicated that Cry1Ab protein did not infl uence the growth characteristic of MC1.

Exploration of the key functional proteins from an efficient cellulolytic microbial consortium using dilution-to-extinction approach

In the present study, the cellulose binding proteins（CBPs） secreted by a putative cellulolytic microbial consortium were isolated and purified by affinity digestion. The purified CBPs were subsequently separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis（SDS-PAGE）. Using mass spectrometric analyses, eight CBPs were identified and annotated to be similar to known proteins secreted by Clostridium clariflavum DSM 19732 and Paenibacillus sp. W-61. In addition, in combination with dilution-to-extinction approach and zymogram analysis technique, CBPs 6（97 k Da） and 12（52 k Da） were confirmed to be the key functional proteins that influence cellulolytic activities. Moreover, structural domain analyses and enzymatic activity detection indicated that CBPs 6 and 12 contained glycoside hydrolase families（GH） 9 and 48 catalytic modules, which both revealed endoglucandase and xylanase activities. It was suggested that the coexistence of GH9 and GH48 catalytic domains present in these two proteins could synergistically promote the efficient degradation of cellulose.

Performance and ruminal parameters of fattening Moghani lambs fed recycled poultry bedding

This study investigated the effects of recycled poultry bedding(RPB) on performance and protozoa population, microbial enzyme activity and microbial protein synthesis(MPS) in rumen contents of fattening lambs. Thirty-six male Moghani lambs(31.4 ± 3.2 kg body weight) were fed iso-energetic and iso-nitrogenous diets containing 0, 70,140 or 210 g/kg dry matter(DM) RPB in a balanced randomized design(9 lambs per treatment). Results showed that final body weight, DM intake, average daily gain and feed conversion ratio were unchanged(P > 0.05) by RPB inclusion. Total protozoa population and subfamily of Entoniniinae and Diplodiniiae were linearly decreased by RPB(L, P < 0.05). For rumen fibrolytic enzymes including carboxymethyl-cellulase, microcrystalline-cellulase and filter paper degrading activity, the extra cellular, cellular and total(extra cellular plus cellular fraction) activity were similar(P > 0.05) by feeding the experimental diets. Inclusion of RPB in the diet linearly decreased extra cellular and total a-amylase activity(L, P < 0.05), while cellular activity was unchanged(P > 0.05). The extra cellular activity of proteases tended to increase(L, P=0.07) and their total and cellular activity increased(P > 0.05) in lambs fed RPB. Incorporation of RPB into the diet had no effect(L, P > 0.05) on urinary purine derivative excretion and MPS. In conclusion, inclusion of RPB up to 210 g/kg DM had no negative impact on performance, ruminal fibrolytic enzyme activity and MPS, while it increased rumen protease activity and decreased protozoa population in fattening Moghani lambs.