Novozymes A/s

Dsm IP Assets B.v.

Morten Fischer

Allan Svendsen

Carsten Sjoeholm

Soren Flensted Lassen

Carsten Schau Andersen

Kim Borch

Peter Rahbek Øestergaard

Peter Rahbek Oestergaard

Peter Rahbek Ostergaard

Dan Pettersson

Soeren Flensted Lassen

Peter Colin Gregory

Søren Flensted Lassen

Carsten Sjoholm

Wolfgang Steinberg

Irmgard Immig

Peter Rahbek Østergaard

Vibe Glitsoe

Immig Irmgard

Carsten Sjøholm

The invention relates to the use of at least one bacterial amylase in feed for ruminant animals of the subfamily Bovinae in particular for improving milk yield, apparent digestibility of the diet fed, feedstuff dry matter disappearance, weight gain, and/or Feed Conversion Ratio (FCR). Examples of bovine animals are dairy cows and beef cattle. The invention also relates to the use of such amylases in feed and feed additives such as premix, concentrates and total mixed ration (TMR). The amylase may be used in combination with cellulase for improving milk yield and/or back fat thickness. Preferred amylases are derived from, andand are preferably homologous toamylase.

Use of bacterial amylases in feed for bovine animals

Proteases derived fromsubsp.DSM 43235,DSM 15649,(previously) DSM 14010sp. DSM 16424,DSM 44657 andDSM 44048, as well as homologous proteases; their recombinant production in various hosts, including transgenic plants and non-human animals, and their use in animal feed and detergents. The proteases are acid-stable, alkali-stable, and/or thermostable.

Proteases

Proteases derived fromsubsp.DSM 43235,DSM 15649,(previously alba) DSM 14010sp. DSM 16424,DSM 44657 andDSM 44048, as well as homologous proteases; their recombinant production in various hosts, including transgenic plants and non-human animals, and their use in animal feed and detergents. The proteases are acid-stable, alkali-stable, and/or thermostable.

The present invention relates to thermostable proteases having an amino acid sequence which homologous to the amino acid sequence of proteases derived from, and the production thereof by wild-type and recombinant host cells including transgenic plants and non-human transgenic animals. The proteases are effective in animal feed, in particular fish feed, and detergents. The proteases are capable of degrading the soybean Bowman-Birk inhibitor, and other antinutritional factors such as soybean agglutinin and the Kunitz trypsin inhibitor, as well as the isolated soy storage proteins glycinin and beta-conglycinin. Characteristic structural features of relevance for the thermostability of these proteases of peptidase family S2A or S1E are disclosed.

Thermostable proteases

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Vedbaek, Denmark

Morten Fischer