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Literature summary for 3.4.23.21 extracted from

  • da Silva, R.R.; Souto, T.B.; de Oliveira, T.B.; de Oliveira, L.C.; Karcher, D.; Juliano, M.A.; Juliano, L.; de Oliveira, A.H.; Rodrigues, A.; Rosa, J.C.; Cabral, H.
    Evaluation of the catalytic specificity, biochemical properties, and milk clotting abilities of an aspartic peptidase from Rhizomucor miehei (2016), J. Ind. Microbiol. Biotechnol., 43, 1059-1069 .
    View publication on PubMed
Search for more literature for 3.4.23.21

Application

Application Comment Organism
food industry the peptidase may function as an important alternative enzyme in milk clotting during the preparation of cheese Rhizomucor miehei

Inhibitors

Inhibitors Comment Organism Structure
Al3+ 16% residual activity at 10 mM Rhizomucor miehei
Ba2+ about 64 residual activity at 10 mM Rhizomucor miehei
Ca2+ about 44% residual activity at 10 mM Rhizomucor miehei
Co2+ 0.3% residual activity at 10 mM; about 36% residual activity at 10 mM Rhizomucor miehei
CTAB in the presence of CTAB, 20 and 10 % relative activities are maintained at concentrations of 0.1% (w/v) and 1% (w/v), respectively Rhizomucor miehei
dithiothreitol the peptidase shows residual activities of 50 and 40% following incubation with 100 or 150 mM dithiothreitol, respectively Rhizomucor miehei
guanidine the enzyme maintains approximately 70 and 60% of proteolytic activity at 100 and 150 mM guanidine, respectively Rhizomucor miehei
K+ about 56% residual activity at 10 mM Rhizomucor miehei
Mg2+ about 36% residual activity at 10 mM Rhizomucor miehei
Mn2+ about 36% residual activity at 10 mM Rhizomucor miehei
additional information not inhibited by urea Rhizomucor miehei
pepstatin A 40% residual activity at 0.2 mM Rhizomucor miehei
SDS the peptidase maintains approximately 50 % of activity in the presence of 0.02 % (w/v) SDS andloses nearly all activity during incubation with 0.08 % (w/v) SDS Rhizomucor miehei
Triton X-100 approximately 60% residual activity at 0.2 % (v/v) Triton X-100 Rhizomucor miehei
Tween 20 approximately 60% residual activity at 0.2 % (v/v) Tween 20 Rhizomucor miehei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.036
-
 Abz-LSFMAIQ-EDDnp at pH 5.5 and 50°C Rhizomucor miehei

Organism

Organism UniProt Comment Textmining
Rhizomucor miehei
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Sephacryl S-100 gel filtration and Sephadex G-50 resin gel filtration Rhizomucor miehei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Abz-LSFMAIQ-EDDnp + H2O
-
 Rhizomucor miehei Abz-LSF + MAIQ-EDDnp
-
 ?
casein + H2O
-
 Rhizomucor miehei ?
-
 ?
milk powder + H2O
-
 Rhizomucor miehei ?
-
 ?
additional information the coagulant activity of the peptidase is higher than the proteolytic activity and there is a preference for aromatic, basic, and nonpolar amino acids, particularly methionine, with specific cleavage of the peptide bond between phenylalanine and methionine Rhizomucor miehei ?
-
 ?

Subunits

Subunits Comment Organism
? x * 37000, SDS-PAGE Rhizomucor miehei
? x * 37102, calculated from amino acid sequence Rhizomucor miehei

Synonyms

Synonyms Comment Organism
aspartic peptidase
-
 Rhizomucor miehei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Rhizomucor miehei

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 65 the enzyme maintains around 80% activity at 40-50°C. 90 and 80% proteolytic activities are maintained at 60 and 65°C, respectively Rhizomucor miehei

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 the peptidase is stable at temperatures of up 45°C for 1 h Rhizomucor miehei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
 Rhizomucor miehei

pH Range

pH Minimum pH Maximum Comment Organism
4.5 6 more than 80% activity between pH 4.5 and 6.0 Rhizomucor miehei

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 5 the peptidase is stable at pH values ranging from 3.0 to 5.0 for 1 h Rhizomucor miehei

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4722
-
 Abz-LSFMAIQ-EDDnp at pH 5.5 and 50°C Rhizomucor miehei