biblio24 has 1 private note and 0 public notes for this article.
If you are biblio24 then you can log in to see the private note.
The proteolytic activity of 34 commercial lipase preparations (CLP) was determined using a labeled casein substrate. Only three CLP were free from proteolytic activity. Porcine pancreatic lipases exhibited levels of proteolytic activity comparable to or greater than that of a reference porcine trypsin. Bacterial lipases contained up to 10% of the proteolytic activity of commercial trypsin. Proteolytic activities in lipases from fungal species were present at low levels (<1% of the activity in trypsin). Among preparations of fungal origin, lipases from <i>Aspergillus niger</i> and <i>Mucor javanicus</i> were highest in proteolytic activity; <i>Aspergillus oryzae</i> and <i>Pseudomonas cepacia</i> lipases were lowest. Proteins in CLP were separated by non-denaturing PAGE; between 4 and 17 protein bands in the range ≤6.5- ≥200 kDa were observed. With the exception of a single pair of Rhizomucor miehei lipases, the distribution of apparent molecular weights (AMW) was unique to each preparation. Bands of caseinolytic activity in commercial lipases were visualized by applying a zymographic technique. CLP contained between 0 (<i>P. cepacia</i> lipases) and 6 (porcine pancreas lipase and <i>Rhizopus oryzae</i> lipase) discrete proteolytic bands. Common themes of proteolytic AMW emerged, including 21-23 kDa and 30-35 kDa bands.
Search
Reviews
[Write a review of this article]
Notes for this article
