On the purification and characterization of three anionic, serine-type peptide hydrolases from antarctic krill, Euphausia Superba☆
作者： Knut Kr. Osnes , Viggo Mohr
DOI: 10.1016/0305-0491(85)90497-3
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摘要: Abstract 1. Three enzymes effecting hydrolysis of TAME have been purified from E. superba using gel filtration, affinity chromatography and FPLC-anion exchange chromatography. 2. The had molecular weights 30,000 (Enzyme I), 31,000 (Enzymes II III), respectively, as estimated SDS-PAGE. 3. pH-optima about 8.2 were observed for all three enzymes. 4. inhibited by phenyl methyl sulphonyl fluoride (PMSF), tosyl lysyl chloromethyl ketone (TLCK) soybean trypsin inhibitor (SBTI), whereas (TPCK) no effect on the activity. 5. stable at neutral pH, only slowly inactivated highly alkaline pH. Low pH rapidly 6. Enzyme I liberated amino acids casein, Enzymes III did not; latter two being true endopeptidases which effected enhanced acid production casein when mixed with I.
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