Details
| Original language | English |
|---|---|
| Pages (from-to) | 10311-10316 |
| Number of pages | 6 |
| Journal | Journal of Agricultural and Food Chemistry |
| Volume | 59 |
| Issue number | 18 |
| Publication status | Published - 22 Aug 2011 |
Abstract
The first enzyme of the basidiomycete Piptoporus soloniensis, a peptidase (PsoP1), was characterized after isolation from submerged cultures, purification by fractional precipitation, and preparative native-polyarylamide gel electrophoresis (PAGE). The native molecular mass of PsoP1 was 38 kDa with an isoelectric point of 3.9. Similar to chymosin from milk calves, PsoP1 showed a maximum milk-clotting activity (MCA) at 35-40 °C and was most stable at pH 6 and below 40 °C. The complete inhibition by pepstatin A identified this enzyme as an aspartic peptidase. Electrospray ionization-tandem MS showed an amino acid partial sequence that was more homologous to mammalian milk clotting peptidases than to the chymosin substitute from a fungal species, such as the Zygomycete Mucor miehei. According to sodium dodecyl sulfate-PAGE patterns, the peptidase cleaved κ-casein in a way similar to chymosin and hydrolyzed β-casein slowly, as it would be expected from an efficient chymosin substitute.
Keywords
- β- and k-casein, aspartic peptidase, milk clotting, Piptoporus soloniensis, preparative PAGE
ASJC Scopus subject areas
- Chemistry(all)
- General Chemistry
- Agricultural and Biological Sciences(all)
- General Agricultural and Biological Sciences
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In: Journal of Agricultural and Food Chemistry, Vol. 59, No. 18, 22.08.2011, p. 10311-10316.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - PsoP1, a milk-clotting aspartic peptidase from the basidiomycete fungus Piptoporus soloniensis
AU - El-Baky, Hassan Abd
AU - Linke, Diana
AU - Nimtz, Manfred
AU - Berger, Ralf Günter
PY - 2011/8/22
Y1 - 2011/8/22
N2 - The first enzyme of the basidiomycete Piptoporus soloniensis, a peptidase (PsoP1), was characterized after isolation from submerged cultures, purification by fractional precipitation, and preparative native-polyarylamide gel electrophoresis (PAGE). The native molecular mass of PsoP1 was 38 kDa with an isoelectric point of 3.9. Similar to chymosin from milk calves, PsoP1 showed a maximum milk-clotting activity (MCA) at 35-40 °C and was most stable at pH 6 and below 40 °C. The complete inhibition by pepstatin A identified this enzyme as an aspartic peptidase. Electrospray ionization-tandem MS showed an amino acid partial sequence that was more homologous to mammalian milk clotting peptidases than to the chymosin substitute from a fungal species, such as the Zygomycete Mucor miehei. According to sodium dodecyl sulfate-PAGE patterns, the peptidase cleaved κ-casein in a way similar to chymosin and hydrolyzed β-casein slowly, as it would be expected from an efficient chymosin substitute.
AB - The first enzyme of the basidiomycete Piptoporus soloniensis, a peptidase (PsoP1), was characterized after isolation from submerged cultures, purification by fractional precipitation, and preparative native-polyarylamide gel electrophoresis (PAGE). The native molecular mass of PsoP1 was 38 kDa with an isoelectric point of 3.9. Similar to chymosin from milk calves, PsoP1 showed a maximum milk-clotting activity (MCA) at 35-40 °C and was most stable at pH 6 and below 40 °C. The complete inhibition by pepstatin A identified this enzyme as an aspartic peptidase. Electrospray ionization-tandem MS showed an amino acid partial sequence that was more homologous to mammalian milk clotting peptidases than to the chymosin substitute from a fungal species, such as the Zygomycete Mucor miehei. According to sodium dodecyl sulfate-PAGE patterns, the peptidase cleaved κ-casein in a way similar to chymosin and hydrolyzed β-casein slowly, as it would be expected from an efficient chymosin substitute.
KW - β- and k-casein
KW - aspartic peptidase
KW - milk clotting
KW - Piptoporus soloniensis
KW - preparative PAGE
UR - http://www.scopus.com/inward/record.url?scp=80053117372&partnerID=8YFLogxK
U2 - 10.1021/jf2021495
DO - 10.1021/jf2021495
M3 - Article
C2 - 21888369
AN - SCOPUS:80053117372
VL - 59
SP - 10311
EP - 10316
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 18
ER -