Abstract: The invention provides a nucleotide sequence of bovine epidermal growth factor (bEGF) and the deduced amino acid sequence of the encoded protein. The invention further provides the nucleotide sequence of mature bEGF and the deduced mature bEGF protein. The invention extends to homologous nucleic acids, proteins, and fragments functionally equivalent to the nucleotide sequence of the bEGF gene and bEGF protein, respectively. Bovine EGF may be expressed in microorganisms such as E. coli or P. pastoris, and plant hosts, such as potato. Activity of recombinant bEGF may be confirmed using a cell proliferation/DNA synthesis assay. Bovine EGF demonstrates utility in livestock and dairy productions as a supplement in farm animal feed to promote growth; to prevent or treat intestinal infections; to stimulate precocious maturation of gut cells to secrete an appropriate spectrum of digestive enzymes; and to increase nutrient absorption.

Abstract: The invention provides a nucleotide sequence of bovine epidermal growth factor (bEGF) and the deduced amino acid sequence of the encoded protein. The invention further provides the nucleotide sequence of mature bEGF and the deduced mature bEGF protein. The invention extends to homologous nucleic acids, proteins, and fragments functionally equivalent to the nucleotide sequence of the bEGF gene and bEGF protein, respectively. Bovine EGF may be expressed in microorganisms such as E. coli or P. pastoris, and plant hosts, such as potato. Activity of recombinant bEGF may be confirmed using a cell proliferation/DNA synthesis assay. Bovine EGF demonstrates utility in livestock and dairy productions as a supplement in farm animal feed to promote growth; to prevent or treat intestinal infections; to stimulate precocious maturation of gut cells to secrete an appropriate spectrum of digestive enzymes; and to increase nutrient absorption.

Abstract: A xylanase gene, denoted xynC, encoding a novel xylanase (XynC) obtained from the anaerobic fungus Neocallimastix patriciarum is provided. The DNA sequence of the xynC gene is also provided. Transformation of microbial and plant hosts with the xynC gene is described. The xynC gene may be used to design probes for use in hybridization experiments to isolate xylanase genes from other anaerobic fungi. The xynC gene has been used to construct an oleosin-xynC expression construct encoding an oleosin-xylanase fusion protein which retains xylanase activity. Transgenic Brassica napus (canola), transformed with the oleosin-xynC expression construct, expresses the oleosin-xylanase fusion protein which is immobilized in the oil-body membrane of the B. napus seeds. Canola meal, the protein-rich residue left after canola oil is extracted from canola plants, when derived from the transgenic B. napus of the present invention, retains substantial xylanase activity, making it an ideal animal feed supplement.

Abstract: Novel phytases derived from ruminal microorganisms are provided. The phytases are capable of catalyzing the release of inorganic phosphorus from phytic acid. Preferred sources of phytases include Selenomonas, Prevotella, Treponema and Megasphaera. A purified and isolated DNA encoding a phytase of Selenomonas ruminantium JY35 (ATCC 55785) is provided. Recombinant expression vectors containing DNA's encoding the novel phytases and host cells transformed with DNA's encoding the novel phytases are also provided. The novel phytases are useful in a wide range of applications involving the dephosphorylation of phytate, including, among other things, use in animal feed supplements.

Abstract: Novel phytases derived from ruminal microorganisms are provided. The phytases are capable of catalyzing the release of inorganic phosphorus from phytic acid. Preferred sources of phytases include Selenomonas, Prevotella, Treponema and Megasphaera. A purified and isolated DNA encoding a phytase of Selenomonas ruminantium JY35 (ATCC 55785) is provided. Recombinant expression vectors containing DNA's encoding the novel phytases and host cells transformed with DNA's encoding the novel phytases are also provided. The novel phytases are useful in a wide range of applications involving the dephosphorylation of phytate, including, among other things, use in animal feed supplements.