Details
| Original language | English |
|---|---|
| Pages (from-to) | 406-409 |
| Number of pages | 4 |
| Journal | Milchwissenschaft |
| Volume | 66 |
| Issue number | 4 |
| Publication status | Published - 2011 |
Abstract
An extracellular milk clotting peptidase from submerged culture of the basidiomycete Wolfiporia cocos was purified 22-fold to electrophoretical homogeneity with a recovery of 47% using preparative native-PAGE as the single purification step. The enzyme showed a molecular mass of 51 kDa with 17 kDa subunits indicating a homotrimer, an isoelectric point of 3.2, and an optimum clotting activity at 45 'C and 0.04 M CaCI 2. The enzyme was most stable in the range of pH 6 and at temperatures below 40 °C. The specific milk clotting activity (MCA) was 1.9 times higher than of commercial Mucor rennet. The enzyme was identified as an aspartic peptidase A1 by its complete inhibition by 0.02 mM pepstatin A and homology analysis of peptide sequences (ESI-Tandem MS). The peptides formed after hydrolysis of β-casein had a molecular mass of around 18 kDa, much larger than those of bitter peptides typically generated using rennet substitutes.
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Food Science
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In: Milchwissenschaft, Vol. 66, No. 4, 2011, p. 406-409.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The extracellular aspartic peptidase of basidiomycete Wolfiporia cocos is a highly efficient milk clotting enzyme
AU - Abd El-Baky, H.
AU - Linke, D.
AU - Nimtz, M.
AU - Metry, W.
AU - El-Demerdash, O.
AU - Berger, R. G.
PY - 2011
Y1 - 2011
N2 - An extracellular milk clotting peptidase from submerged culture of the basidiomycete Wolfiporia cocos was purified 22-fold to electrophoretical homogeneity with a recovery of 47% using preparative native-PAGE as the single purification step. The enzyme showed a molecular mass of 51 kDa with 17 kDa subunits indicating a homotrimer, an isoelectric point of 3.2, and an optimum clotting activity at 45 'C and 0.04 M CaCI 2. The enzyme was most stable in the range of pH 6 and at temperatures below 40 °C. The specific milk clotting activity (MCA) was 1.9 times higher than of commercial Mucor rennet. The enzyme was identified as an aspartic peptidase A1 by its complete inhibition by 0.02 mM pepstatin A and homology analysis of peptide sequences (ESI-Tandem MS). The peptides formed after hydrolysis of β-casein had a molecular mass of around 18 kDa, much larger than those of bitter peptides typically generated using rennet substitutes.
AB - An extracellular milk clotting peptidase from submerged culture of the basidiomycete Wolfiporia cocos was purified 22-fold to electrophoretical homogeneity with a recovery of 47% using preparative native-PAGE as the single purification step. The enzyme showed a molecular mass of 51 kDa with 17 kDa subunits indicating a homotrimer, an isoelectric point of 3.2, and an optimum clotting activity at 45 'C and 0.04 M CaCI 2. The enzyme was most stable in the range of pH 6 and at temperatures below 40 °C. The specific milk clotting activity (MCA) was 1.9 times higher than of commercial Mucor rennet. The enzyme was identified as an aspartic peptidase A1 by its complete inhibition by 0.02 mM pepstatin A and homology analysis of peptide sequences (ESI-Tandem MS). The peptides formed after hydrolysis of β-casein had a molecular mass of around 18 kDa, much larger than those of bitter peptides typically generated using rennet substitutes.
UR - http://www.scopus.com/inward/record.url?scp=80055078642&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:80055078642
VL - 66
SP - 406
EP - 409
JO - Milchwissenschaft
JF - Milchwissenschaft
SN - 0026-3788
IS - 4
ER -