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Main Authors:	Martínez-Ranz, María, Kidibule, Peter E, Jiménez-Ortega, Elena, Valcárcel, Jesús, Vázquez, José Antonio, Sanz-Aparicio, Julia, Fernández-Lobato, María
Format:	Artículo científico
Language:	en
Published:	Journal of agricultural and food chemistry 2025
Subjects:	Chitin Chitinases Cellulose Biocatalysis Protein Engineering Fungal Proteins Protein Domains Oligosaccharides Hydrolysis Substrate Specificity Chitosan
Online Access:	https://pubmed.ncbi.nlm.nih.gov/40279401/
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author	Martínez-Ranz, María Kidibule, Peter E Jiménez-Ortega, Elena Valcárcel, Jesús Vázquez, José Antonio Sanz-Aparicio, Julia Fernández-Lobato, María
author_facet	Martínez-Ranz, María Kidibule, Peter E Jiménez-Ortega, Elena Valcárcel, Jesús Vázquez, José Antonio Sanz-Aparicio, Julia Fernández-Lobato, María Martínez-Ranz, María Kidibule, Peter E Jiménez-Ortega, Elena Valcárcel, Jesús Vázquez, José Antonio Sanz-Aparicio, Julia Fernández-Lobato, María
collection	PubMed - marine biology
contents	Boosting Biocatalytic Efficiency: Engineering of Chitinase Chit33 with Chitin and Cellulose Binding Domains for Sustainable Chitin Conversion. Martínez-Ranz, María Kidibule, Peter E Jiménez-Ortega, Elena Valcárcel, Jesús Vázquez, José Antonio Sanz-Aparicio, Julia Fernández-Lobato, María Chitin Chitinases Cellulose Biocatalysis Protein Engineering Fungal Proteins Protein Domains Oligosaccharides Hydrolysis Substrate Specificity Chitosan Endochitinase Chit33 has shown great potential in converting chitin, a recalcitrant waste, into bioactive chitooligosaccharides (COS). This study evaluates how cellulose-binding domain (CBD) and chitin-binding domain (ChBD) affect the hydrolytic activity and product specificity of Chit33. Recombinant proteins were produced and isolated with a simple yeast extracellular medium concentration. The domain functionality was proved using chitin and cellulose supports. ChBD provided more stable immobilization than CBD but reduced the Chit33 activity. CBD enhanced the enzyme activity on both colloidal (α-/β-allomorphs) and crystalline chitin, doubling it on α-chitin, although not on their deacetylated forms. Besides, CBD increased the COS production from the colloidal forms of α-/β-chitin (by 30% and 85%, respectively) and expanded the product diversity from 1 to 9 -acetylglucosamine units. In contrast, Chit33-ChBD predominantly yielded chitin tetrasaccharides. These findings highlight the importance of selecting appropriate binding domains to tailor product specificity, as polymerization and acetylation degrees directly impact the COS biological properties.
format	Artículo científico
id	pubmed_40279401
institution	PubMed
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publishDate	2025
publisher	Journal of agricultural and food chemistry
record_format	pubmed
spellingShingle	Boosting Biocatalytic Efficiency: Engineering of Chitinase Chit33 with Chitin and Cellulose Binding Domains for Sustainable Chitin Conversion. Martínez-Ranz, María Kidibule, Peter E Jiménez-Ortega, Elena Valcárcel, Jesús Vázquez, José Antonio Sanz-Aparicio, Julia Fernández-Lobato, María Chitin Chitinases Cellulose Biocatalysis Protein Engineering Fungal Proteins Protein Domains Oligosaccharides Hydrolysis Substrate Specificity Chitosan Boosting Biocatalytic Efficiency: Engineering of Chitinase Chit33 with Chitin and Cellulose Binding Domains for Sustainable Chitin Conversion. Martínez-Ranz, María Kidibule, Peter E Jiménez-Ortega, Elena Valcárcel, Jesús Vázquez, José Antonio Sanz-Aparicio, Julia Fernández-Lobato, María Chitin Chitinases Cellulose Biocatalysis Protein Engineering Fungal Proteins Protein Domains Oligosaccharides Hydrolysis Substrate Specificity Chitosan Endochitinase Chit33 has shown great potential in converting chitin, a recalcitrant waste, into bioactive chitooligosaccharides (COS). This study evaluates how cellulose-binding domain (CBD) and chitin-binding domain (ChBD) affect the hydrolytic activity and product specificity of Chit33. Recombinant proteins were produced and isolated with a simple yeast extracellular medium concentration. The domain functionality was proved using chitin and cellulose supports. ChBD provided more stable immobilization than CBD but reduced the Chit33 activity. CBD enhanced the enzyme activity on both colloidal (α-/β-allomorphs) and crystalline chitin, doubling it on α-chitin, although not on their deacetylated forms. Besides, CBD increased the COS production from the colloidal forms of α-/β-chitin (by 30% and 85%, respectively) and expanded the product diversity from 1 to 9 -acetylglucosamine units. In contrast, Chit33-ChBD predominantly yielded chitin tetrasaccharides. These findings highlight the importance of selecting appropriate binding domains to tailor product specificity, as polymerization and acetylation degrees directly impact the COS biological properties.
title	Boosting Biocatalytic Efficiency: Engineering of Chitinase Chit33 with Chitin and Cellulose Binding Domains for Sustainable Chitin Conversion.
topic	Chitin Chitinases Cellulose Biocatalysis Protein Engineering Fungal Proteins Protein Domains Oligosaccharides Hydrolysis Substrate Specificity Chitosan
url	https://pubmed.ncbi.nlm.nih.gov/40279401/

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