Structure/Function Relationships of Several Biopolymers as Related to Invertase Stability in Dehydrated Systems
Structure/function relationships of different biopolymers (alginate, dextran, or β-cyclodextrin) were analyzed as single excipients or combined with trehalose in relation to their efficiency as enzyme stabilizers in freeze-dried formulations and compared to trehalose. Particularly, a novel synthesiz...
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| Veröffentlicht in: | Biomacromolecules 2008-02, Vol.9 (2), p.741-747 |
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| creator | Santagapita, Patricio R Brizuela, Leissy Gómez Mazzobre, M. Florencia Ramirez, Héctor L Corti, Horacio R Santana, Reynaldo Villalonga Buera, M. Pilar |
| description | Structure/function relationships of different biopolymers (alginate, dextran, or β-cyclodextrin) were analyzed as single excipients or combined with trehalose in relation to their efficiency as enzyme stabilizers in freeze-dried formulations and compared to trehalose. Particularly, a novel synthesized polymer β-cyclodextrin-branched alginate (β-CD-A) was employed as excipient. During freeze-drying, the polymers or their mixtures did not confer better protection to invertase compared to trehalose. β-CD-A (with or without trehalose), β-cyclodextrin (β-CD), or dextran with trehalose were the best protective agents during thermal treatment, while β-CD and alginate showed a negative effect on invertase activity preservation. The β-CD linked alginate combined the physical stability provided by alginate with the stabilization of hydrophobic regions of the enzyme provided by cyclodextrin. β-CD-A was effective even at conditions at which trehalose lost its protective effect. A relatively simple covalent combination of two biopolymers significantly affected their functionalities and, consequently, their interactions with proteins, modifying enzyme stability patterns. |
| doi_str_mv | 10.1021/bm7012108 |
| format | Article |
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Florencia ; Ramirez, Héctor L ; Corti, Horacio R ; Santana, Reynaldo Villalonga ; Buera, M. Pilar</creator><creatorcontrib>Santagapita, Patricio R ; Brizuela, Leissy Gómez ; Mazzobre, M. Florencia ; Ramirez, Héctor L ; Corti, Horacio R ; Santana, Reynaldo Villalonga ; Buera, M. Pilar</creatorcontrib><description>Structure/function relationships of different biopolymers (alginate, dextran, or β-cyclodextrin) were analyzed as single excipients or combined with trehalose in relation to their efficiency as enzyme stabilizers in freeze-dried formulations and compared to trehalose. Particularly, a novel synthesized polymer β-cyclodextrin-branched alginate (β-CD-A) was employed as excipient. During freeze-drying, the polymers or their mixtures did not confer better protection to invertase compared to trehalose. β-CD-A (with or without trehalose), β-cyclodextrin (β-CD), or dextran with trehalose were the best protective agents during thermal treatment, while β-CD and alginate showed a negative effect on invertase activity preservation. The β-CD linked alginate combined the physical stability provided by alginate with the stabilization of hydrophobic regions of the enzyme provided by cyclodextrin. β-CD-A was effective even at conditions at which trehalose lost its protective effect. A relatively simple covalent combination of two biopolymers significantly affected their functionalities and, consequently, their interactions with proteins, modifying enzyme stability patterns.</description><identifier>ISSN: 1525-7797</identifier><identifier>EISSN: 1526-4602</identifier><identifier>DOI: 10.1021/bm7012108</identifier><identifier>PMID: 18189362</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Applied sciences ; beta-Fructofuranosidase - analysis ; beta-Fructofuranosidase - chemistry ; Biological and medical sciences ; Biotechnology ; Desiccation - methods ; Drug Stability ; Enzyme engineering ; Enzyme Stability ; Exact sciences and technology ; Freeze Drying - methods ; Fundamental and applied biological sciences. Psychology ; Laminaria - isolation & purification ; Methods. Procedures. 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During freeze-drying, the polymers or their mixtures did not confer better protection to invertase compared to trehalose. β-CD-A (with or without trehalose), β-cyclodextrin (β-CD), or dextran with trehalose were the best protective agents during thermal treatment, while β-CD and alginate showed a negative effect on invertase activity preservation. The β-CD linked alginate combined the physical stability provided by alginate with the stabilization of hydrophobic regions of the enzyme provided by cyclodextrin. β-CD-A was effective even at conditions at which trehalose lost its protective effect. A relatively simple covalent combination of two biopolymers significantly affected their functionalities and, consequently, their interactions with proteins, modifying enzyme stability patterns.</description><subject>Applied sciences</subject><subject>beta-Fructofuranosidase - analysis</subject><subject>beta-Fructofuranosidase - chemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Desiccation - methods</subject><subject>Drug Stability</subject><subject>Enzyme engineering</subject><subject>Enzyme Stability</subject><subject>Exact sciences and technology</subject><subject>Freeze Drying - methods</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Laminaria - isolation & purification</subject><subject>Methods. Procedures. Technologies</subject><subject>Miscellaneous</subject><subject>Natural polymers</subject><subject>Physicochemistry of polymers</subject><subject>Polymers - analysis</subject><subject>Polymers - chemistry</subject><subject>Starch and polysaccharides</subject><subject>Structure-Activity Relationship</subject><issn>1525-7797</issn><issn>1526-4602</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0M1O3DAUBWCrKirDwIIXQN4UiUXg2onteFl-pkVCQmJgHTmOI4ySeOrrIOXtG5gRs-nqnsWnc6VDyCmDSwacXdW9AsYZlN_Iggkus0IC__6ZRaaUVofkCPENAHReiB_kkJWs1LnkCxLWKY42jdFdrcbBJh8G-uQ68xHw1W-Qhpau3buLpqPXPmxCN_UuIjW4da6hKdD7YRbJoKPrZGrf-TRRP9Bb9zo18ROtJ0yux2Ny0JoO3cnuLsnL6u755k_28Pj7_ubXQ2ZyVaSsgbYtVQsNmFry0taFagrBoVScMyMF01oBSAkir03JNWNQF1ooJmsolNX5kpxvezcx_B0dpqr3aF3XmcGFESsOQmrQYoYXW2hjQIyurTbR9yZOFYPqY93qa93Znu1Kx7p3zV7u5pzBzx0waE3XRjNYj1-OAwOtlNw7Y7F6C2Mc5i3-8_AfVECNOg</recordid><startdate>20080201</startdate><enddate>20080201</enddate><creator>Santagapita, Patricio R</creator><creator>Brizuela, Leissy Gómez</creator><creator>Mazzobre, M. 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Technologies</topic><topic>Miscellaneous</topic><topic>Natural polymers</topic><topic>Physicochemistry of polymers</topic><topic>Polymers - analysis</topic><topic>Polymers - chemistry</topic><topic>Starch and polysaccharides</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Santagapita, Patricio R</creatorcontrib><creatorcontrib>Brizuela, Leissy Gómez</creatorcontrib><creatorcontrib>Mazzobre, M. Florencia</creatorcontrib><creatorcontrib>Ramirez, Héctor L</creatorcontrib><creatorcontrib>Corti, Horacio R</creatorcontrib><creatorcontrib>Santana, Reynaldo Villalonga</creatorcontrib><creatorcontrib>Buera, M. 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During freeze-drying, the polymers or their mixtures did not confer better protection to invertase compared to trehalose. β-CD-A (with or without trehalose), β-cyclodextrin (β-CD), or dextran with trehalose were the best protective agents during thermal treatment, while β-CD and alginate showed a negative effect on invertase activity preservation. The β-CD linked alginate combined the physical stability provided by alginate with the stabilization of hydrophobic regions of the enzyme provided by cyclodextrin. β-CD-A was effective even at conditions at which trehalose lost its protective effect. A relatively simple covalent combination of two biopolymers significantly affected their functionalities and, consequently, their interactions with proteins, modifying enzyme stability patterns.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>18189362</pmid><doi>10.1021/bm7012108</doi><tpages>7</tpages></addata></record> |
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| subjects | Applied sciences beta-Fructofuranosidase - analysis beta-Fructofuranosidase - chemistry Biological and medical sciences Biotechnology Desiccation - methods Drug Stability Enzyme engineering Enzyme Stability Exact sciences and technology Freeze Drying - methods Fundamental and applied biological sciences. Psychology Laminaria - isolation & purification Methods. Procedures. Technologies Miscellaneous Natural polymers Physicochemistry of polymers Polymers - analysis Polymers - chemistry Starch and polysaccharides Structure-Activity Relationship |
| title | Structure/Function Relationships of Several Biopolymers as Related to Invertase Stability in Dehydrated Systems |
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