TY - JOUR
T1 - Purification and characterization of a proteinase from Lactobacillus plantarum DPC2739
AU - Magboul, Abdallah A.A.
AU - Fox, Patrick F.
AU - McSweeney, Paul L.H.
PY - 1997/10/24
Y1 - 1997/10/24
N2 - A proteinase from Lactobacillus plantarum DPC2739 was purified by a combination of ion exchange chromatography on DEAE-Sephacel and gel filtration on Sephacryl-S-300 HR and TSK G3000SW. The enzyme had properties typical of an alkaline serine proteinase. It was optimally active at pH 9.5 and between 45 and 50°C. The enzyme was monomeric with a molecular mass of ~ 42 kDa. It was strongly inhibited by phenylmethylsulphonyl fluoride, Cu2+ and Zn2+. The N-terminal amino acid sequence showed no homology with known Lactococcus or Lactobacillus proteinases. The proteinase hydrolysed both χ(s1)- and β-caseins at approximately the same rate.
AB - A proteinase from Lactobacillus plantarum DPC2739 was purified by a combination of ion exchange chromatography on DEAE-Sephacel and gel filtration on Sephacryl-S-300 HR and TSK G3000SW. The enzyme had properties typical of an alkaline serine proteinase. It was optimally active at pH 9.5 and between 45 and 50°C. The enzyme was monomeric with a molecular mass of ~ 42 kDa. It was strongly inhibited by phenylmethylsulphonyl fluoride, Cu2+ and Zn2+. The N-terminal amino acid sequence showed no homology with known Lactococcus or Lactobacillus proteinases. The proteinase hydrolysed both χ(s1)- and β-caseins at approximately the same rate.
UR - https://www.scopus.com/pages/publications/0031585421
U2 - 10.1016/S0958-6946(97)00086-1
DO - 10.1016/S0958-6946(97)00086-1
M3 - Article
AN - SCOPUS:0031585421
SN - 0958-6946
VL - 7
SP - 693
EP - 700
JO - International Dairy Journal
JF - International Dairy Journal
IS - 11
ER -