Abstract: The presently disclosed subject matter relates to feed additive formulations for fish. The disclosed formulations may comprise an isolated xylanase enzyme and a B. licheniformis strain PWD-1. The feed additive formulations may further include B. amyloliquefaciens strain Ba-BPD1. The disclosed formulations are useful for addition to feeds for fish to synergistically improve the performance of the fish.

Abstract: The presently disclosed subject matter relates to feed additive formulations for monogastric animal feed. Particularly, the disclosed formulations comprise an isolated xylanase enzyme and a B. licheniformis strain PWD-1. The feed additive formulations may further include B. amyloliquefaciens strain Ba-BPD1. The disclosed formulations are useful for addition to feeds for monogastric animals to synergistically improve the performance of the animals.

Abstract: The presently disclosed subject matter relates to feed additive formulations for monogastric animal feed. Particularly, the disclosed formulations comprise an isolated xylanase enzyme and a B. licheniformis strain PWD-1. The feed additive formulations may further include B. amyloliquefaciens strain Ba-BPD1. The disclosed formulations are useful for addition to feeds for monogastric animals to synergistically improve the performance of the animals.

Abstract: Proteolytic enzyme variants that exhibit improved thermal stability relative to the wild type protease Bacillus licheniformis PWD-1 protease kerA are provided. The protease variants are derived by the mutation of at least one amino acid residue of the mature Bacillus licheniformis PWD-1 protease kerA. The variant proteases are useful as animal feed additives to improve the digestibility and/or the nutritional value of the animal feed.

Abstract: The presently disclosed subject matter relates to feed additive formulations for monogastric animal feed. Particularly, the disclosed formulations comprise an isolated xylanase enzyme and a B. licheniformis strain PWD-1. The feed additive formulations may further include B. amyloliquefaciens strain Ba-BPD1. The disclosed formulations are useful for addition to feeds for monogastric animals to synergistically improve the performance of the animals.

Abstract: Proteolytic enzyme variants that exhibit improved thermal stability relative to the wild type protease Bacillus licheniformis PWD-1 protease kerA are provided. The protease variants are derived by the mutation of at least one amino acid residue of the mature Bacillus licheniformis PWD-1 protease kerA. The variant proteases are useful as animal feed additives to improve the digestibility and/or the nutritional value of the animal feed.

Abstract: Methods and kits are provided for measuring protease activity in samples such as feed or food samples. The methods include adding a water insoluble substrate with a signal producing group to a feed or food sample containing the protease activity to be measured, incubating the sample in phosphate-free buffer such that the signal is produced, and measuring the amount of protease activity in the sample. The methods do not require separation of the incubation buffer from the feed or food and allow for visual inspection of a colorimetric signal for a semi-quantitative measurement of the in-feed/in-food protease activity. Thus, the assay is advantageous as it can be performed on-site without the use of laboratory equipment.

Abstract: Methods and kits are provided for measuring protease activity in samples such as feed or food samples. The methods include adding a water insoluble substrate with a signal producing group to a feed or food sample containing the protease activity to be measured, incubating the sample in phosphate-free buffer such that the signal is produced, and measuring the amount of protease activity in the sample. The methods do not require separation of the incubation buffer from the feed or food and allow for visual inspection of a colorimetric signal for a semi-quantitative measurement of the in-feed/in-food protease activity. Thus, the assay is advantageous as it can be performed on-site without the use of laboratory equipment.

Abstract: A recombinant nucleic acid encoding a fusion protein wherein the recombinant nucleic acid comprises a nucleic acid encoding a keratinase fused to a nucleic acid encoding a first member of a specific binding pair is described. An immobilized keratinase comprising a fusion protein and a solid support is also described. A method of digesting substrates such as keratin (e.g., feather) or protein (e.g., casein) is also described herein.