Encapsulation of ligninolytic enzymes and its application in clarification of juice.
Identifieur interne : 000389 ( Main/Curation ); précédent : 000388; suivant : 000390Encapsulation of ligninolytic enzymes and its application in clarification of juice.
Auteurs : Fatma Gassara-Chatti [Canada] ; Satinder K. Brar ; C M Ajila ; M. Verma ; R D Tyagi ; J R ValeroSource :
- Food chemistry [ 1873-7072 ] ; 2013.
Descripteurs français
- KwdFr :
- MESH :
- analyse : Boissons.
- composition chimique : Peroxidases, Phanerochaete, Protéines fongiques.
- enzymologie : Phanerochaete.
- méthodes : Technologie alimentaire.
- Stabilité enzymatique, Taille de particule.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Fungal Proteins, Peroxidases.
- analysis : Beverages.
- chemistry : Phanerochaete.
- enzymology : Phanerochaete.
- methods : Food Technology.
- Enzyme Stability, Particle Size.
Abstract
The thermal stability, physico-chemical properties and effect on juice clarification of hydrogel formulations of ligninolytic enzymes from Phanerochaete chrysosporium were evaluated. The results showed that enzyme entrapment increase significantly (P<0.05) the thermal stability of enzymes at 4 and 75 °C. At 75 °C, maximum activity decreased to non detectable values of 7.9% for free laccase, manganese peroxidase (MnP), lignin peroxidase (LiP), respectively; to 94%, 97%, 93% for laccase, MnP and LiP entrapped into Polyacrylamide/pectin, 94%, 98%, 88% for laccase, MnP and LiP encapsulated respectively into polyacrylamide/ gelatine and to 87%, 91%, 87% for laccase, MnP and LiP entrapped, respectively into polyacrylamide/carboxymethylcellulose (CMC). When particle size and viscosity of the formulation increased, enzyme stability increased. The polyphenolic reduction and clarity amelioration in mixed juice of berry and pomegranate was more significant (p>0.05) using encapsulated enzymes treatment than free enzymes. This suggested that enzymatic treatment was efficient for the juice clarification.
DOI: 10.1016/j.foodchem.2012.09.083
PubMed: 23199985
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pubmed:23199985Le document en format XML
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<term>Enzyme Stability (MeSH)</term>
<term>Food Technology (methods)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Particle Size (MeSH)</term>
<term>Peroxidases (chemistry)</term>
<term>Phanerochaete (chemistry)</term>
<term>Phanerochaete (enzymology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Boissons (analyse)</term>
<term>Peroxidases (composition chimique)</term>
<term>Phanerochaete (composition chimique)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Stabilité enzymatique (MeSH)</term>
<term>Taille de particule (MeSH)</term>
<term>Technologie alimentaire (méthodes)</term>
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<term>Peroxidases</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Phanerochaete</term>
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<term>Phanerochaete</term>
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<term>Particle Size</term>
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<front><div type="abstract" xml:lang="en">The thermal stability, physico-chemical properties and effect on juice clarification of hydrogel formulations of ligninolytic enzymes from Phanerochaete chrysosporium were evaluated. The results showed that enzyme entrapment increase significantly (P<0.05) the thermal stability of enzymes at 4 and 75 °C. At 75 °C, maximum activity decreased to non detectable values of 7.9% for free laccase, manganese peroxidase (MnP), lignin peroxidase (LiP), respectively; to 94%, 97%, 93% for laccase, MnP and LiP entrapped into Polyacrylamide/pectin, 94%, 98%, 88% for laccase, MnP and LiP encapsulated respectively into polyacrylamide/ gelatine and to 87%, 91%, 87% for laccase, MnP and LiP entrapped, respectively into polyacrylamide/carboxymethylcellulose (CMC). When particle size and viscosity of the formulation increased, enzyme stability increased. The polyphenolic reduction and clarity amelioration in mixed juice of berry and pomegranate was more significant (p>0.05) using encapsulated enzymes treatment than free enzymes. This suggested that enzymatic treatment was efficient for the juice clarification.</div>
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<Abstract><AbstractText>The thermal stability, physico-chemical properties and effect on juice clarification of hydrogel formulations of ligninolytic enzymes from Phanerochaete chrysosporium were evaluated. The results showed that enzyme entrapment increase significantly (P<0.05) the thermal stability of enzymes at 4 and 75 °C. At 75 °C, maximum activity decreased to non detectable values of 7.9% for free laccase, manganese peroxidase (MnP), lignin peroxidase (LiP), respectively; to 94%, 97%, 93% for laccase, MnP and LiP entrapped into Polyacrylamide/pectin, 94%, 98%, 88% for laccase, MnP and LiP encapsulated respectively into polyacrylamide/ gelatine and to 87%, 91%, 87% for laccase, MnP and LiP entrapped, respectively into polyacrylamide/carboxymethylcellulose (CMC). When particle size and viscosity of the formulation increased, enzyme stability increased. The polyphenolic reduction and clarity amelioration in mixed juice of berry and pomegranate was more significant (p>0.05) using encapsulated enzymes treatment than free enzymes. This suggested that enzymatic treatment was efficient for the juice clarification.</AbstractText>
<CopyrightInformation>Copyright © 2012 Elsevier Ltd. All rights reserved.</CopyrightInformation>
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