Abstract：
:Glutamyl endopeptidase (GE) from Alcalase™ 2.4 L was purified using hydrophobic interaction (HIC) and ion-exchange (IEX) chromatography. The yield of GE obtained was approximately 42%. Bovine α-casein (containing α(s1)- and α(s2)-casein) was digested with GE at 37 and 50°C for 4h. Samples were withdrawn at various time intervals and the peptides generated were analysed using mass spectrometry. GE activity was highly specific and hydrolysed the peptide bond predominantly on the carboxy side of Glu residues while hydrolysis on the carboxyl side of Asp residues was also observed. Hydrolysis did not occur when Pro was at the P(1)' position. In Glu-Glu-X (X=Arg, Asn, Ile and Ser) and Glu-Glu-Glu-Lys sequences, hydrolysis of Glu-X and Glu-Lys was preferred. The results are relevant to our understanding of the hydrolytic specificity of Alcalase, a food-grade proteolytic preparation containing GE activity which is used in the generation of casein hydrolysates.
journal_name
Food Chemjournal_title
Food chemistryauthors
Kalyankar P,Zhu Y,O'Keeffe M,O'Cuinn G,FitzGerald RJdoi
10.1016/j.foodchem.2012.08.038subject
Has Abstractpub_date
2013-01-15 00:00:00pages
501-12issue
2eissn
0308-8146issn
1873-7072pii
S0308-8146(12)01322-2journal_volume
136pub_type
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