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Pancreatin phospholipase

Relevant quality control should not be restricted to the usual triad of activities of pancreas lipase, a-amylase, and trypsin, but should be extended to the content of colipasc, the activities of the two other lipolytic enzymes present in pancreatine (phospholipase Aj and carboxylester lipase), and the dissolution characteristics of enteric-coated preparations as a function of time and pH (Fig. 16). The availability of such information will certainly contribute to a better tailoring of flic management of maldigestion in the individual patient and to a more appropriate correction of the obligate nonphysio logical route of delivery of these enzyme supplements. [Pg.214]

Lipase (Microbial) Activity for Medium- and Long-Chain Fatty Acids, (S3)105 Lysozyme Activity, (S3)106 Maltogenic Amylase Activity, 804 Milk-Clotting Activity, 805 Pancreatin Activity, 805 Pepsin Activity, 807 Phospholipase A2 Activity, 808 Phytase Activity, 808 Plant Proteolytic Activity, 810 Proteolytic Activity, Bacterial (PC), 811 Proteolytic Activity, Fungal (HUT), 812 Proteolytic Activity, Fungal (SAP), 813 Pullulanase Activity, 814 Trypsin Activity, 814 Enzyme Assays, 786 Enzyme-Hydrolyzed (Source) Protein,... [Pg.123]

Pancreatin is described in the different pharmacopeia as a slightly brown, amorphous powder with a faint, characteristic odor. It is slowly and incompletely soluble in water it is not recommended to filter the solution as the lipolytic enzymes and part of the proteolytic activity may be retained on the filter. Most pharmacopeia stipulate the minimum units of amylase (12,000 FIP units/g), lipase (15,000 FIP units/g), and protease (1000 FIP units/g) activity, but give no specifications on the content of the other components such as phospholipase A2, carboxylester lipase, colipase, and individual proteolytic enzymes. It... [Pg.208]


See other pages where Pancreatin phospholipase is mentioned: [Pg.973]    [Pg.973]    [Pg.75]    [Pg.152]    [Pg.22]    [Pg.124]    [Pg.209]    [Pg.92]   


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