The optimum active site of acidic phytase in the gastrointestinal tract of channel catfish (Ictalurus punctatus): in vitro and in vivo studies. (15th April 2015)

• Record Type: Journal Article
• Authors: Zhu, W.X.; Zhong, G.F.; Hua, X.M.; Ju, M.; Chen, X.M.; Du, Z.Y.
• Is Part Of: Aquaculture nutrition. Volume 22:Number 4(2016:Aug.)
• Page Start: 881
• Page End: 889
• Publication Date: 2015-04-15
• Subjects: absorption of phosphorus -- channel catfish -- gastrointestinal tract -- optimum site -- phytase -- phytic acid; Aquaculture -- Periodicals; Aquatic animals -- Feeding and feeds -- Periodicals; Fishes -- Feeding and feeds -- Periodicals; 639.3
• DOI: 10.1111/anu.12304
• Languages: English
• ISSNs: 1353-5773

Abstract

Abstract: This study was conducted to determine the optimum active site of acidic phytase in the gastrointestinal tract of channel catfish. The pH value, acidic phytase activity, resistance of acidic phytase against gastrointestinal protease, substrate availability, and enzymatic reaction products were measured in different gastrointestinal sections of channel catfish, respectively. The results indicated that in the whole gastrointestinal tract, only the pH value of stomach (4.2–4.7) lied in the optimum active pH range of acidic phytase (1.5–5.5). The resistant ability of acidic phytase against proteases in different sections of the gastrointestinal tract was comparable, and the highest activity of phytase was observed in the stomach compared with other gastrointestinal sections. Moreover, the highest concentration of soluble phytic acid as the substrate of phytase was also seen in the stomach. After feeding fish with the diet containing acidic phytase, the residual phytic acid in the stomach was significantly reduced. Correspondingly, the dietary addition of acidic phytase significantly improved the phosphorus absorption in the intestine. In short, this study verified that stomach is the optimum active site for acidic phytase in channel catfish, because it allows higher phytase activity and provides more soluble substrates of phytase than other gastrointestinal sections.