Factors affecting storage stability of various commercial phytase sources1,2

Abstract

SummaryA 360-d study was performed to evaluate the effects of environmental conditions on storage stability of exogenous phytases. Coated and uncoated products from 3 phytase sources (Ronozyme P, OptiPhos, and Phyzyme) were stored as pure forms, in a vitamin premix, or in a vitamin and trace mineral (VTM) premix. Pure products were stored at 0, 41, 73, and 99ºF (75% humidity). Premixes were stored at 73 and 99ºF. Sampling was performed on d 0, 30, 60, 90, 120, 180, 270, and 360. Sampling of the pure products stored at 0 and 41ºF was discontinued after d 120 due to mold growth in the 41ºF samples. Stability was measured as the residual phytase activity (% of initial) at each sampling point. For the stability of the pure forms, all interactive and main effects of phytase product, coating, time, and temperature of storage were significant (P < 0.01), except for time × coating interaction. When stored at 73ºF or less, pure phytases retained at least 91, 85, 78, and 71% of initial phytase activity at 30, 60, 90, and 120 d of storage, respectively. However, storing pure products at 99ºF reduced (P < 0.01) phytase stability, with OptiPhos retaining the most (P < 0.01) activity. Coating mitigated (P < 0.01) the negative effects of high storage temperature for Ronozyme and OptiPhos (from d 90 onward) but not for Phyzyme. For the stability of phytase in different forms of storage, all interactive and main effects of phytase product, form, coating, time, and temperature of storage were significant (P < 0.01). When stored at room temperature (73ºF), retained phytase activities for a majority of the phytase sources were more than 85, 73, and 60% of initial activity up to 180 d when stored as pure products, vitamin premixes, or VTM premixes, respectively. When stored at 99ºF, pure phytase products had greater (P < 0.01) retention of initial phytase activity than when phytases were mixed with the vitamin or VTM premixes. Coated phytases stored in any form had greater (P < 0.01) activity retention than the uncoated phytases at all sampling periods. In conclusion, storage stability of commercially available phytases is affected by duration of storage, temperature, product form, coating, and phytase source. Pure products held at 73ºF or less were the most stable. In premixes, longer storage time and higher temperature reduced phytase activity, but coating mitigated some of these negative effects.

Stability of Commercial Xylanases stored singly or Combined with Vitamins and/or Minerals Premix at different Temperatures

“…The results of the present study demonstrated that, there were no significant differences (P> 0.05) in enzyme stability between the two types of xylanase products examined here. This might be due to that the xylanase in both products had resulted from the dried extract of the same source of fungi (Trichoderma longibrachiatum).In harmony with the present results, Sulabo et al (2011) reported that when phytase is stored at room temperature (23 °C) or lower, the pure product retained most (approximately 85%) of its activity for up to 60 days of storage regardless of phytase source.…”

“…There are several enzyme products in the market; however, few scientific studies have been carried out to examine the potency of exogenous feed enzymes added as enzyme preparation, vitamin premix, mineral premix or vitamin and mineral premix (Iyer and Ananthanarayan, 2008;Sulabo et al, 2011). It will be more beneficial to include enzymes in a premix with vitamins, minerals or both as it makes them easier to test and may decrease the price of the diet formulation.…”

Immobilization of the Antarctic &lt;italic&gt;Bacillus&lt;/italic&gt; sp. LX-1 α-Galactosidase on Eudragit L-100 for the Production of a Functional Feed Additive

“…From a practical point of view, it is an important criterion that an enzyme designed for use in animal feed should survive storage at ambient temperature (Francesch and Perez-Vendrell, 1997; Sulabo et al, 2011). As shown in Figure 6, the storage stability at 37°C was greatly improved by immobilization.…”

Degradation of Phytate Pentamagnesium Salt by Bacillus sp. T4 Phytase as a Potential Eco-friendly Feed Additive

“…Today, the feed industry mainly ascribes the rapidly expanding global market for animal feed enzymes to increased use of exogenous phytases (Sulabo et al, 2011). In conclusion, the T4 phytase may have great potential for use as an eco-friendly feed additive to enhance the nutritive quality of phytate and reduce phosphorus pollution, because it possesses high selectivity on the genuine phytate substrate, Mg-InsP 6 , and desirable activity profiles at physiologically-relevant pH and temperature.…”

“…Virtually, phytases are now added routinely to swine and poultry diets as an economical aid in the digestibility of phosphorus and an important measure for environmental protection (Selle and Ravindran, 2007). Currently, a number of microbial phytases with different enzymatic properties are commercially available (Sulabo et al, 2011). Catalytically, most bacterial, fungal, and plant phytases belong to the family of histidine acid phosphatases (HAP) typically characterized by a conserved active site motif, RHGXRXP (Lei and Porres, 2003).…”