PhanerochaeteV1, Main, Exploration, bibRecord, 000189

Biochemical and milk-clotting properties and mapping of catalytic subsites of an extracellular aspartic peptidase from basidiomycete fungus Phanerochaete chrysosporium.

Identifieur interne : 000189 ( Main/Exploration ); précédent : 000188; suivant : 000190

Biochemical and milk-clotting properties and mapping of catalytic subsites of an extracellular aspartic peptidase from basidiomycete fungus Phanerochaete chrysosporium.

Auteurs : Ronivaldo Rodrigues Da Silva [Brésil] ; Lilian Caroline Gonçalves De Oliveira [Brésil] ; Maria Aparecida Juliano [Brésil] ; Luiz Juliano [Brésil] ; Arthur H C. De Oliveira [Brésil] ; Jose C. Rosa [Brésil] ; Hamilton Cabral [Brésil]

Source :

Food chemistry [ 1873-7072 ] ; 2017.

RBID : pubmed:28193432

Descripteurs français

KwdFr :
- Animaux (MeSH), Aspartic acid proteases (métabolisme), Fromage (microbiologie), Industrie de la transformation des aliments (MeSH), Lait (microbiologie), Phanerochaete (enzymologie), Protéines fongiques (métabolisme), Température (MeSH).
MESH :
- enzymologie : Phanerochaete.
- microbiologie : Fromage, Lait.
- métabolisme : Aspartic acid proteases, Protéines fongiques.
- Animaux, Industrie de la transformation des aliments, Température.

English descriptors

KwdEn :
- Animals (MeSH), Aspartic Acid Proteases (metabolism), Cheese (microbiology), Food-Processing Industry (MeSH), Fungal Proteins (metabolism), Milk (microbiology), Phanerochaete (enzymology), Temperature (MeSH).
MESH :
- chemical , metabolism : Aspartic Acid Proteases, Fungal Proteins.
- enzymology : Phanerochaete.
- microbiology : Cheese, Milk.
- Animals, Food-Processing Industry, Temperature.

Abstract

For a long time, proteolytic enzymes have been employed as key tools of industrial processes, especially in the dairy industry. In the present work, we used Phanerochaete chrysosporium for biochemical characterization and analysis of catalytic specificity of an aspartic peptidase. Our results revealed an aspartic peptidase with molecular mass ∼38kDa, maximal activity at pH 4.5 and 50°C, and stability above 80% in the pH range of 3-8 and temperature up to 55°C for 1h. In a milk-clotting assay, this peptidase showed maximal milk clotting activity at 60-65°C and maintenance of enzymatic activity above 80% in the presence of 20mM CaCl₂. In a specificity assay, we observed stronger restriction of catalysis at the S₁ subsite, with a preference for lysine, arginine, leucine, tyrosine, and phenylalanine residues. The restricted proteolysis and milk-clotting potential are attractive properties for the use in cheese production.

DOI: 10.1016/j.foodchem.2017.01.009
PubMed: 28193432

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000171
to stream Main, to step Curation: 000171

Le document en format XML

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<front><div type="abstract" xml:lang="en">For a long time, proteolytic enzymes have been employed as key tools of industrial processes, especially in the dairy industry. In the present work, we used Phanerochaete chrysosporium for biochemical characterization and analysis of catalytic specificity of an aspartic peptidase. Our results revealed an aspartic peptidase with molecular mass ∼38kDa, maximal activity at pH 4.5 and 50°C, and stability above 80% in the pH range of 3-8 and temperature up to 55°C for 1h. In a milk-clotting assay, this peptidase showed maximal milk clotting activity at 60-65°C and maintenance of enzymatic activity above 80% in the presence of 20mM CaCl<sub>2</sub>
. In a specificity assay, we observed stronger restriction of catalysis at the S<sub>1</sub>
 subsite, with a preference for lysine, arginine, leucine, tyrosine, and phenylalanine residues. The restricted proteolysis and milk-clotting potential are attractive properties for the use in cheese production.</div>
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<Abstract><AbstractText>For a long time, proteolytic enzymes have been employed as key tools of industrial processes, especially in the dairy industry. In the present work, we used Phanerochaete chrysosporium for biochemical characterization and analysis of catalytic specificity of an aspartic peptidase. Our results revealed an aspartic peptidase with molecular mass ∼38kDa, maximal activity at pH 4.5 and 50°C, and stability above 80% in the pH range of 3-8 and temperature up to 55°C for 1h. In a milk-clotting assay, this peptidase showed maximal milk clotting activity at 60-65°C and maintenance of enzymatic activity above 80% in the presence of 20mM CaCl<sub>2</sub>
. In a specificity assay, we observed stronger restriction of catalysis at the S<sub>1</sub>
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<tree><country name="Brésil"><region name="État de São Paulo"><name sortKey="Da Silva, Ronivaldo Rodrigues" sort="Da Silva, Ronivaldo Rodrigues" uniqKey="Da Silva R" first="Ronivaldo Rodrigues" last="Da Silva">Ronivaldo Rodrigues Da Silva</name>
</region>
<name sortKey="Cabral, Hamilton" sort="Cabral, Hamilton" uniqKey="Cabral H" first="Hamilton" last="Cabral">Hamilton Cabral</name>
<name sortKey="De Oliveira, Arthur H C" sort="De Oliveira, Arthur H C" uniqKey="De Oliveira A" first="Arthur H C" last="De Oliveira">Arthur H C. De Oliveira</name>
<name sortKey="De Oliveira, Lilian Caroline Goncalves" sort="De Oliveira, Lilian Caroline Goncalves" uniqKey="De Oliveira L" first="Lilian Caroline Gonçalves" last="De Oliveira">Lilian Caroline Gonçalves De Oliveira</name>
<name sortKey="Juliano, Luiz" sort="Juliano, Luiz" uniqKey="Juliano L" first="Luiz" last="Juliano">Luiz Juliano</name>
<name sortKey="Juliano, Maria Aparecida" sort="Juliano, Maria Aparecida" uniqKey="Juliano M" first="Maria Aparecida" last="Juliano">Maria Aparecida Juliano</name>
<name sortKey="Rosa, Jose C" sort="Rosa, Jose C" uniqKey="Rosa J" first="Jose C" last="Rosa">Jose C. Rosa</name>
</country>
</tree>
</affiliations>
</record>

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HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000189 | SxmlIndent | more

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{{Explor lien
   |wiki=    Bois
   |area=    PhanerochaeteV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:28193432
   |texte=   Biochemical and milk-clotting properties and mapping of catalytic subsites of an extracellular aspartic peptidase from basidiomycete fungus Phanerochaete chrysosporium.
}}

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	Serveur d'exploration sur le phanerochaete
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur le phanerochaete

Biochemical and milk-clotting properties and mapping of catalytic subsites of an extracellular aspartic peptidase from basidiomycete fungus Phanerochaete chrysosporium.

Biochemical and milk-clotting properties and mapping of catalytic subsites of an extracellular aspartic peptidase from basidiomycete fungus Phanerochaete chrysosporium.

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