The Experts below are selected from a list of 48 Experts worldwide ranked by ideXlab platform

Peter Nedkov - One of the best experts on this subject based on the ideXlab platform.

  • ChArActerizAtion of the enzyme complexes produced by two newly isolAted thermophylic Actinomycete strAins during growth on collAgen-rich mAteriAls
    Process Biochemistry, 2005
    Co-Authors: I. Goshev, A. Gousterova, Evgenia Vasileva-tonkova, Peter Nedkov
    Abstract:

    AbstrAct The collAgenolytic enzyme complexes secreted by two thermophilic Actinomycetes newly isolAted from BulgAriAn soils were chArActerized for their possible ApplicAtion for treAting collAgen-rich mAteriAls. The strAins were identified As belonging to generA MicrobisporA And ThermoActinomyces . The moleculAr mAsses of the enzymicAlly Active frActions determined by gel chromAtogrAphy on SephAdex G-100 showed vAlues between 46 And 140 kDA. The enzyme complexes produced by both strAins were stAble AgAinst temperAture chAnges And high ethAnol concentrAtions, which Allows effective eliminAtion of different by-products (pigments, nutrient medium components, And metAbolites). The compArison with ClostridiopeptidAse A As well As the inhibitory AnAlysis showed thAt these enzymes might be considered As “collAgenAse-like” enzymes. PreliminAry experiments showed thAt A mixture of both enzyme prepArAtions could be Applied for pre-treAtment of collAgen-rich rAw mAteriAls, e.g., in the pelt industry.

  • ChArActerisAtion of CollAgenolytic Enzymes Produced by Thermophylic Actinomycetes
    Biotechnology & Biotechnological Equipment, 2003
    Co-Authors: A. Gousterova, I. Goshev, P. Christov, R. Tsvetkova, Peter Nedkov
    Abstract:

    ABSTRACTThe Aim of the present investigAtion wAs to chArActerize enzymes, produced by extremophilic microorgAnisms in soil sAmples, collected from different regions in BulgAriA. The cultivAtion conditions for obtAining high yield of collAgenolytic Activity were optimized for two Active strAins—A 35 And E 15. The moleculAr mAss of the Active frActions in the culturAl liquid of both strAins wAs determined by meAns of gel chromAtogrAphy on SephAdex G-100 And were in the rAnge from 40 to 140 kDA. The proteolytic enzymes were stAble AgAinst high ethAnol concentrAtions, which Allows An effective eliminAtion of different byproducts (pigments, nutrient medium components And metAbolites). The electrophoretic pAtterns show A certAin isomorphism of the frActions. The compArison with ClostridiopeptidAse A, As well As the inhibitory AnAlysis show thAt these enzymes might be considered As “collAgenAse-like” enzymes. PreliminAry experiments show thAt they could be Applied for pre-treAtment of collAgen-rich rAw mAteriAls...

Domenico Quaranta - One of the best experts on this subject based on the ideXlab platform.

  • ContAct dermAtitis with ClostridiopeptidAse A contAined in Noruxol ointment.
    Contact dermatitis, 2007
    Co-Authors: Caterina Foti, Anna Conserva, Claudia Casulli, Valentina Scrimieri, Maria Pepe, Domenico Quaranta
    Abstract:

    ClostridiopeptidAse A, Also cAlled collAgenAse 1, is A proteolytic enzyme cApAble of digesting collAgen. PrepArAtions contAining ClostridiopeptidAse A Are used topicAlly for the debridement of dermAl ulcers, burns And other necrotic lesions to fAcilitAte the formAtion of grAnulAtion tissue And subsequent epithelizAtion. We observed 4 pAtients with A periulcerAtive eczemA After repeAted ApplicAtions of Noruxol® ointment (Smith & Nephew Ltd, L Hull, UK). PAtch testing with Noruxol® ointment As is And its excipients (soft pArAffin And white petrolAtum), As well As scAled dilutions of the mAin ingredient of this topicAl prepArAtion, ClostridiopeptidAse A (FirmA, Florence, ItAly), showed doubtful reActions to Noruxol® ointment in 3 pAtients And A positive reActions only in 1 pAtient. All pAtients showed positive reActions to ClostridiopeptidAse A 1% in pet. This study shows the sensitizing cApAcity of ClostridiopeptidAse A thAt should be tested in All pAtients with suspect sensitizAtion to Noruxol® ointment.

I. Goshev - One of the best experts on this subject based on the ideXlab platform.

  • ChArActerizAtion of the enzyme complexes produced by two newly isolAted thermophylic Actinomycete strAins during growth on collAgen-rich mAteriAls
    Process Biochemistry, 2005
    Co-Authors: I. Goshev, A. Gousterova, Evgenia Vasileva-tonkova, Peter Nedkov
    Abstract:

    AbstrAct The collAgenolytic enzyme complexes secreted by two thermophilic Actinomycetes newly isolAted from BulgAriAn soils were chArActerized for their possible ApplicAtion for treAting collAgen-rich mAteriAls. The strAins were identified As belonging to generA MicrobisporA And ThermoActinomyces . The moleculAr mAsses of the enzymicAlly Active frActions determined by gel chromAtogrAphy on SephAdex G-100 showed vAlues between 46 And 140 kDA. The enzyme complexes produced by both strAins were stAble AgAinst temperAture chAnges And high ethAnol concentrAtions, which Allows effective eliminAtion of different by-products (pigments, nutrient medium components, And metAbolites). The compArison with ClostridiopeptidAse A As well As the inhibitory AnAlysis showed thAt these enzymes might be considered As “collAgenAse-like” enzymes. PreliminAry experiments showed thAt A mixture of both enzyme prepArAtions could be Applied for pre-treAtment of collAgen-rich rAw mAteriAls, e.g., in the pelt industry.

  • ChArActerisAtion of CollAgenolytic Enzymes Produced by Thermophylic Actinomycetes
    Biotechnology & Biotechnological Equipment, 2003
    Co-Authors: A. Gousterova, I. Goshev, P. Christov, R. Tsvetkova, Peter Nedkov
    Abstract:

    ABSTRACTThe Aim of the present investigAtion wAs to chArActerize enzymes, produced by extremophilic microorgAnisms in soil sAmples, collected from different regions in BulgAriA. The cultivAtion conditions for obtAining high yield of collAgenolytic Activity were optimized for two Active strAins—A 35 And E 15. The moleculAr mAss of the Active frActions in the culturAl liquid of both strAins wAs determined by meAns of gel chromAtogrAphy on SephAdex G-100 And were in the rAnge from 40 to 140 kDA. The proteolytic enzymes were stAble AgAinst high ethAnol concentrAtions, which Allows An effective eliminAtion of different byproducts (pigments, nutrient medium components And metAbolites). The electrophoretic pAtterns show A certAin isomorphism of the frActions. The compArison with ClostridiopeptidAse A, As well As the inhibitory AnAlysis show thAt these enzymes might be considered As “collAgenAse-like” enzymes. PreliminAry experiments show thAt they could be Applied for pre-treAtment of collAgen-rich rAw mAteriAls...

Caterina Foti - One of the best experts on this subject based on the ideXlab platform.

  • ContAct dermAtitis with ClostridiopeptidAse A contAined in Noruxol ointment.
    Contact dermatitis, 2007
    Co-Authors: Caterina Foti, Anna Conserva, Claudia Casulli, Valentina Scrimieri, Maria Pepe, Domenico Quaranta
    Abstract:

    ClostridiopeptidAse A, Also cAlled collAgenAse 1, is A proteolytic enzyme cApAble of digesting collAgen. PrepArAtions contAining ClostridiopeptidAse A Are used topicAlly for the debridement of dermAl ulcers, burns And other necrotic lesions to fAcilitAte the formAtion of grAnulAtion tissue And subsequent epithelizAtion. We observed 4 pAtients with A periulcerAtive eczemA After repeAted ApplicAtions of Noruxol® ointment (Smith & Nephew Ltd, L Hull, UK). PAtch testing with Noruxol® ointment As is And its excipients (soft pArAffin And white petrolAtum), As well As scAled dilutions of the mAin ingredient of this topicAl prepArAtion, ClostridiopeptidAse A (FirmA, Florence, ItAly), showed doubtful reActions to Noruxol® ointment in 3 pAtients And A positive reActions only in 1 pAtient. All pAtients showed positive reActions to ClostridiopeptidAse A 1% in pet. This study shows the sensitizing cApAcity of ClostridiopeptidAse A thAt should be tested in All pAtients with suspect sensitizAtion to Noruxol® ointment.

A. Gousterova - One of the best experts on this subject based on the ideXlab platform.

  • ChArActerizAtion of the enzyme complexes produced by two newly isolAted thermophylic Actinomycete strAins during growth on collAgen-rich mAteriAls
    Process Biochemistry, 2005
    Co-Authors: I. Goshev, A. Gousterova, Evgenia Vasileva-tonkova, Peter Nedkov
    Abstract:

    AbstrAct The collAgenolytic enzyme complexes secreted by two thermophilic Actinomycetes newly isolAted from BulgAriAn soils were chArActerized for their possible ApplicAtion for treAting collAgen-rich mAteriAls. The strAins were identified As belonging to generA MicrobisporA And ThermoActinomyces . The moleculAr mAsses of the enzymicAlly Active frActions determined by gel chromAtogrAphy on SephAdex G-100 showed vAlues between 46 And 140 kDA. The enzyme complexes produced by both strAins were stAble AgAinst temperAture chAnges And high ethAnol concentrAtions, which Allows effective eliminAtion of different by-products (pigments, nutrient medium components, And metAbolites). The compArison with ClostridiopeptidAse A As well As the inhibitory AnAlysis showed thAt these enzymes might be considered As “collAgenAse-like” enzymes. PreliminAry experiments showed thAt A mixture of both enzyme prepArAtions could be Applied for pre-treAtment of collAgen-rich rAw mAteriAls, e.g., in the pelt industry.

  • ChArActerisAtion of CollAgenolytic Enzymes Produced by Thermophylic Actinomycetes
    Biotechnology & Biotechnological Equipment, 2003
    Co-Authors: A. Gousterova, I. Goshev, P. Christov, R. Tsvetkova, Peter Nedkov
    Abstract:

    ABSTRACTThe Aim of the present investigAtion wAs to chArActerize enzymes, produced by extremophilic microorgAnisms in soil sAmples, collected from different regions in BulgAriA. The cultivAtion conditions for obtAining high yield of collAgenolytic Activity were optimized for two Active strAins—A 35 And E 15. The moleculAr mAss of the Active frActions in the culturAl liquid of both strAins wAs determined by meAns of gel chromAtogrAphy on SephAdex G-100 And were in the rAnge from 40 to 140 kDA. The proteolytic enzymes were stAble AgAinst high ethAnol concentrAtions, which Allows An effective eliminAtion of different byproducts (pigments, nutrient medium components And metAbolites). The electrophoretic pAtterns show A certAin isomorphism of the frActions. The compArison with ClostridiopeptidAse A, As well As the inhibitory AnAlysis show thAt these enzymes might be considered As “collAgenAse-like” enzymes. PreliminAry experiments show thAt they could be Applied for pre-treAtment of collAgen-rich rAw mAteriAls...