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By Michael R. Bedford, Gary G. Partridge

Masking all features of the addition of enzymes to animal feeds, this booklet discusses issues together with interactions with animal body structure, fiscal and environmental affects and expertise. This re-creation brings the reader brand new with the huge advances in feed enzyme know-how of the decade. It contains a dialogue of recent periods of enzymes brought into the industry position, an exploration of the way those items functionality and the dimensions and scope in their use within the worldwide with new tools for review of enzyme responses.

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Extra info for Enzymes in Farm Animal Nutrition

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The thermostability of this T. 0. , 2001). Pelleting results were not found in the literature. 1; Vahjen and Simon, 1999; 26 M. Paloheimo et al. Zhang and Lynd, 2004). , 1991; Planas, 2000). The Ronozyme® enzyme preparation derived from B. , 2002). Industrial mutants of Bacillus spp. (B. subtilis, B. amyloliquefaciens and B. , 2004). , 2009). The different Bacillus spp. GH 5 endoglucanases share about 60% identity at the sequence level (Schülein, 2000). Carbohydrate-binding modules of the families CBM 3, CBM 4, CBM 5, CBM 17 and CBM 28 have been assigned to these cellulases, and a tandem arrangement has been described for Bacillus sp.

Org/) the commercial xylanases in feed products are produced by both classical and genetically modified strains. The well-known bacterial expression system, Bacillus and the filamentous fungi Aspergillus, Humicola, Penicillium and Trichoderma, are used for xylanase production (see below). 1). g. , 2001). 0) and from 50 to 75°C, respectively, depending on the source organism. Some xylanases derived from thermophilic Bacillus species are stable at high temperatures. B. , 2006). No family 10 glycosyl hydrolase homologues have been found from B.

Reesei xylanases contain a CBM domain or domains. In addition to the above four xylanases, the T. , 1991). 5, respectively. Xyn3 is the most neutral of the T. 0. Xyn1 and Xyn2 are the major xylanases in wildtype T. reesei culture supernatants in standard laboratory cultivations. , 1992). Xyn2 is included as having the major xylanase activity in at least some of the first-generation recombinant feed xylanase products. All T. reesei xylanases are mesophilic enzymes, having their temperature optima at around 50°C.

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