Lipase

Carbohydrate level in the diet of silver barb,Puntius gonionotus(Bleeker) fingerlings: effect on growth, nutrient utilization and whole body composition

“…Protease activity was measured following the methods of Moore & Stein (1948) using bovine serum albumin as a substrate and the specific activity of protease was expressed as microgram leucine liberated per milligram tissue protein per hour at 37 °C. Lipase activity was measured using α‐napthol released per milligram tissue protein per hour at 37 °C following the method developed by Seligman & Nachlas (1963). The α‐amylase activity was quantitatively determined using soluble starch as a substrate (Bernfeld 1955) and expressed as milligram maltose released milligramg tissue per protein per hour at 37 °C.…”

Effect of different oil cake sources on growth, nutrient retention and digestibility, muscle nucleic acid content, gut enzyme activities and whole-body composition in silver barb, Puntius gonionotus fingerlings

“…Protease activity of the gut was measured following Moore and Stein (1948) using bovine serum albumin as substrate and the specific activity of protease was expressed as μg leucine liberated mg −1 tissue protein h −1 at 37 °C. Lipase activity was measured using α‐napthol liberated mg −1 tissue protein h −1 at 37 °C following the method developed by Seligman and Nachlas (1963). α‐amylase activity was quantitatively determined using soluble starch as substrate (Bernfeld 1955) and expressed as mg maltose liberated mg −1 protein h −1 at 37 °C.…”

A dietary energy level of 14.6 MJ kg−1and protein-to-energy ratio of 20.2 g MJ−1results in best growth performance and nutrient accretion in silver barbPuntius gonionotusfingerlings

“…The protease activity was measured following the methods of Moore & Stein (1948) using bovine serum albumin (BSA) as substrate and the specific activity of protease was expressed as μg leucine liberated mg −1 tissue protein h −1 at 37 °C. The lipase activity was measured using α‐napthol liberated mg −1 tissue protein h −1 at 37 °C following the method developed by Seligman & Nachlas (1963). The α‐amylase activity was quantitatively determined using soluble starch as substrate (Bernfeld 1955) and expressed as mg maltose liberated mg tissue protein −1 h −1 at 37 °C.…”