Biocatalysis by Transglutaminases: A Review of Biotechnological Applications

The biocatalytic activity of transglutaminases (TGs) leads to the synthesis of new covalent isopeptide bonds (crosslinks) between peptide-bound glutamine and lysine residues, but also the transamidation of primary amines to glutamine residues, which ultimately can result into protein polymerisation....
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Autor*in:	Maria Pia Savoca [verfasserIn] Elisa Tonoli [verfasserIn] Adeola G. Atobatele [verfasserIn] Elisabetta A. M. Verderio [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2018

Schlagwörter:	transglutaminases crosslinking polymerisation food industry biomedicine

Übergeordnetes Werk:	In: Micromachines - MDPI AG, 2010, 9(2018), 11, p 562
Übergeordnetes Werk:	volume:9 ; year:2018 ; number:11, p 562

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/mi9110562

Katalog-ID:	DOAJ036039438

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spelling	10.3390/mi9110562 doi (DE-627)DOAJ036039438 (DE-599)DOAJ4d5ef370be334d7d8beb2215c540c191 DE-627 ger DE-627 rakwb eng TJ1-1570 Maria Pia Savoca verfasserin aut Biocatalysis by Transglutaminases: A Review of Biotechnological Applications 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The biocatalytic activity of transglutaminases (TGs) leads to the synthesis of new covalent isopeptide bonds (crosslinks) between peptide-bound glutamine and lysine residues, but also the transamidation of primary amines to glutamine residues, which ultimately can result into protein polymerisation. Operating with a cysteine/histidine/aspartic acid (Cys/His/Asp) catalytic triad, TGs induce the post-translational modification of proteins at both physiological and pathological conditions (e.g., accumulation of matrices in tissue fibrosis). Because of the disparate biotechnological applications, this large family of protein-remodelling enzymes have stimulated an escalation of interest. In the past 50 years, both mammalian and microbial TGs polymerising activity has been exploited in the food industry for the improvement of aliments’ quality, texture, and nutritive value, other than to enhance the food appearance and increased marketability. At the same time, the ability of TGs to crosslink extracellular matrix proteins, like collagen, as well as synthetic biopolymers, has led to multiple applications in biomedicine, such as the production of biocompatible scaffolds and hydrogels for tissue engineering and drug delivery, or DNA-protein bio-conjugation and antibody functionalisation. Here, we summarise the most recent advances in the field, focusing on the utilisation of TGs-mediated protein multimerisation in biotechnological and bioengineering applications. transglutaminases crosslinking polymerisation food industry biomedicine Mechanical engineering and machinery Elisa Tonoli verfasserin aut Adeola G. Atobatele verfasserin aut Elisabetta A. M. Verderio verfasserin aut In Micromachines MDPI AG, 2010 9(2018), 11, p 562 (DE-627)665016069 (DE-600)2620864-7 2072666X nnns volume:9 year:2018 number:11, p 562 https://doi.org/10.3390/mi9110562 kostenfrei https://doaj.org/article/4d5ef370be334d7d8beb2215c540c191 kostenfrei https://www.mdpi.com/2072-666X/9/11/562 kostenfrei https://doaj.org/toc/2072-666X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018 11, p 562
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allfieldsSound	10.3390/mi9110562 doi (DE-627)DOAJ036039438 (DE-599)DOAJ4d5ef370be334d7d8beb2215c540c191 DE-627 ger DE-627 rakwb eng TJ1-1570 Maria Pia Savoca verfasserin aut Biocatalysis by Transglutaminases: A Review of Biotechnological Applications 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The biocatalytic activity of transglutaminases (TGs) leads to the synthesis of new covalent isopeptide bonds (crosslinks) between peptide-bound glutamine and lysine residues, but also the transamidation of primary amines to glutamine residues, which ultimately can result into protein polymerisation. Operating with a cysteine/histidine/aspartic acid (Cys/His/Asp) catalytic triad, TGs induce the post-translational modification of proteins at both physiological and pathological conditions (e.g., accumulation of matrices in tissue fibrosis). Because of the disparate biotechnological applications, this large family of protein-remodelling enzymes have stimulated an escalation of interest. In the past 50 years, both mammalian and microbial TGs polymerising activity has been exploited in the food industry for the improvement of aliments’ quality, texture, and nutritive value, other than to enhance the food appearance and increased marketability. At the same time, the ability of TGs to crosslink extracellular matrix proteins, like collagen, as well as synthetic biopolymers, has led to multiple applications in biomedicine, such as the production of biocompatible scaffolds and hydrogels for tissue engineering and drug delivery, or DNA-protein bio-conjugation and antibody functionalisation. Here, we summarise the most recent advances in the field, focusing on the utilisation of TGs-mediated protein multimerisation in biotechnological and bioengineering applications. transglutaminases crosslinking polymerisation food industry biomedicine Mechanical engineering and machinery Elisa Tonoli verfasserin aut Adeola G. Atobatele verfasserin aut Elisabetta A. M. Verderio verfasserin aut In Micromachines MDPI AG, 2010 9(2018), 11, p 562 (DE-627)665016069 (DE-600)2620864-7 2072666X nnns volume:9 year:2018 number:11, p 562 https://doi.org/10.3390/mi9110562 kostenfrei https://doaj.org/article/4d5ef370be334d7d8beb2215c540c191 kostenfrei https://www.mdpi.com/2072-666X/9/11/562 kostenfrei https://doaj.org/toc/2072-666X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018 11, p 562
language	English
source	In Micromachines 9(2018), 11, p 562 volume:9 year:2018 number:11, p 562
sourceStr	In Micromachines 9(2018), 11, p 562 volume:9 year:2018 number:11, p 562
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topic_facet	transglutaminases crosslinking polymerisation food industry biomedicine Mechanical engineering and machinery
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container_title	Micromachines
authorswithroles_txt_mv	Maria Pia Savoca @@aut@@ Elisa Tonoli @@aut@@ Adeola G. Atobatele @@aut@@ Elisabetta A. M. Verderio @@aut@@
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callnumber-first	T - Technology
author	Maria Pia Savoca
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topic_title	TJ1-1570 Biocatalysis by Transglutaminases: A Review of Biotechnological Applications transglutaminases crosslinking polymerisation food industry biomedicine
topic	misc TJ1-1570 misc transglutaminases misc crosslinking misc polymerisation misc food industry misc biomedicine misc Mechanical engineering and machinery
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title	Biocatalysis by Transglutaminases: A Review of Biotechnological Applications
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title_sort	biocatalysis by transglutaminases: a review of biotechnological applications
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title_auth	Biocatalysis by Transglutaminases: A Review of Biotechnological Applications
abstract	The biocatalytic activity of transglutaminases (TGs) leads to the synthesis of new covalent isopeptide bonds (crosslinks) between peptide-bound glutamine and lysine residues, but also the transamidation of primary amines to glutamine residues, which ultimately can result into protein polymerisation. Operating with a cysteine/histidine/aspartic acid (Cys/His/Asp) catalytic triad, TGs induce the post-translational modification of proteins at both physiological and pathological conditions (e.g., accumulation of matrices in tissue fibrosis). Because of the disparate biotechnological applications, this large family of protein-remodelling enzymes have stimulated an escalation of interest. In the past 50 years, both mammalian and microbial TGs polymerising activity has been exploited in the food industry for the improvement of aliments’ quality, texture, and nutritive value, other than to enhance the food appearance and increased marketability. At the same time, the ability of TGs to crosslink extracellular matrix proteins, like collagen, as well as synthetic biopolymers, has led to multiple applications in biomedicine, such as the production of biocompatible scaffolds and hydrogels for tissue engineering and drug delivery, or DNA-protein bio-conjugation and antibody functionalisation. Here, we summarise the most recent advances in the field, focusing on the utilisation of TGs-mediated protein multimerisation in biotechnological and bioengineering applications.
abstractGer	The biocatalytic activity of transglutaminases (TGs) leads to the synthesis of new covalent isopeptide bonds (crosslinks) between peptide-bound glutamine and lysine residues, but also the transamidation of primary amines to glutamine residues, which ultimately can result into protein polymerisation. Operating with a cysteine/histidine/aspartic acid (Cys/His/Asp) catalytic triad, TGs induce the post-translational modification of proteins at both physiological and pathological conditions (e.g., accumulation of matrices in tissue fibrosis). Because of the disparate biotechnological applications, this large family of protein-remodelling enzymes have stimulated an escalation of interest. In the past 50 years, both mammalian and microbial TGs polymerising activity has been exploited in the food industry for the improvement of aliments’ quality, texture, and nutritive value, other than to enhance the food appearance and increased marketability. At the same time, the ability of TGs to crosslink extracellular matrix proteins, like collagen, as well as synthetic biopolymers, has led to multiple applications in biomedicine, such as the production of biocompatible scaffolds and hydrogels for tissue engineering and drug delivery, or DNA-protein bio-conjugation and antibody functionalisation. Here, we summarise the most recent advances in the field, focusing on the utilisation of TGs-mediated protein multimerisation in biotechnological and bioengineering applications.
abstract_unstemmed	The biocatalytic activity of transglutaminases (TGs) leads to the synthesis of new covalent isopeptide bonds (crosslinks) between peptide-bound glutamine and lysine residues, but also the transamidation of primary amines to glutamine residues, which ultimately can result into protein polymerisation. Operating with a cysteine/histidine/aspartic acid (Cys/His/Asp) catalytic triad, TGs induce the post-translational modification of proteins at both physiological and pathological conditions (e.g., accumulation of matrices in tissue fibrosis). Because of the disparate biotechnological applications, this large family of protein-remodelling enzymes have stimulated an escalation of interest. In the past 50 years, both mammalian and microbial TGs polymerising activity has been exploited in the food industry for the improvement of aliments’ quality, texture, and nutritive value, other than to enhance the food appearance and increased marketability. At the same time, the ability of TGs to crosslink extracellular matrix proteins, like collagen, as well as synthetic biopolymers, has led to multiple applications in biomedicine, such as the production of biocompatible scaffolds and hydrogels for tissue engineering and drug delivery, or DNA-protein bio-conjugation and antibody functionalisation. Here, we summarise the most recent advances in the field, focusing on the utilisation of TGs-mediated protein multimerisation in biotechnological and bioengineering applications.
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