GO:0016798 hydrolase activity, acting on glycosyl bonds: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0016798 (hydrolase activity, acting on glycosyl bonds) is a molecular function defined as the catalysis of the hydrolysis of any glycosyl bond.
• Enzymes in this class include glycoside hydrolases, glycosylases and N-glycosylases that cleave O-, N- or S-glycosidic linkages in carbohydrates, glycoproteins and glycoconjugates.
• Representative members span multiple CAZy families, such as GH3 beta-glucosidases, GH51 exo-alpha-L-arabinofuranosidase/endo-xylanase, and 1,3-beta-glucan hydrolases.
• These enzymes are central to biomass degradation, cell-wall remodeling, glycoprotein processing and glycan turnover in bacteria, fungi, plants and humans.
• Loss or dysregulation of glycosyl-bond hydrolases is linked to lysosomal storage disorders, congenital disorders of glycosylation and cancer-associated glycan remodeling.
• CRISPR knockout, point-mutation, knock-in and overexpression models enable causal testing of individual glycosyl hydrolase genes in disease and biotechnology contexts.
Description
GO:0016798, hydrolase activity, acting on glycosyl bonds, is a molecular function term in the Gene Ontology that describes enzymes catalyzing the hydrolysis of any glycosyl bond. Glycosyl bonds connect a sugar moiety to another sugar, protein, lipid or aglycone, and their cleavage is fundamental to carbohydrate metabolism, glycoprotein maturation and cell-wall dynamics. The term encompasses glycoside hydrolases, glycosylases and N-glycosylases, which together form a large and structurally diverse enzyme class distributed across all domains of life. Researchers study GO:0016798 because these enzymes control the turnover of structural and storage polysaccharides, the processing of N-linked glycans on secreted proteins, and the release of bioactive sugars from glycoconjugates. In plants and microbes, glycosyl-bond hydrolases are key to biomass deconstruction and defense against pathogens. In humans, defects in glycosyl hydrolases cause lysosomal storage diseases and congenital disorders of glycosylation, while altered glycan cleavage contributes to cancer progression and immune evasion. Because the term is defined by chemistry rather than by a single protein family, functional annotation of GO:0016798 requires experimental evidence from enzyme assays, structural biology and genetics. This article integrates the QuickGO definition with verified PubMed literature to summarize the mechanism, key genes, disease links and CRISPR-based research strategies for this GO term.
hydrolase activity, acting on glycosyl bonds At A Glance
| GO ID | GO:0016798 |
|---|---|
| GO term | hydrolase activity, acting on glycosyl bonds |
| Ontology | molecular_function |
| Definition | Catalysis of the hydrolysis of any glycosyl bond. |
| Synonym | glycosidase activity; glycosylase; N-glycosylase |
| Major function | Cleavage of glycosidic linkages in carbohydrates, glycoproteins and glycoconjugates |
| Representative enzymes | GH3 beta-glucosidase, GH51 alpha-L-arabinofuranosidase/endo-xylanase, 1,3-beta-glucan hydrolase, 1,3-alpha-3,6-anhydro-L-galactosidase |
| Substrate examples | Beta-glucans, xylans, arabinofuranosides, agarose-derived oligosaccharides, N-glycans |
| Biological contexts | Biomass degradation, cell-wall remodeling, glycoprotein processing, lysosomal catabolism, plant defense |
What Is GO:0016798?
In simple terms, GO:0016798 describes any enzyme that uses water to break a glycosyl bond, the chemical link between a sugar and another molecule. The official QuickGO definition is: Catalysis of the hydrolysis of any glycosyl bond. Synonyms include glycosidase activity, glycosylase and N-glycosylase. The term is a child of hydrolase activity and is annotated to enzymes that cleave O-glycosidic, N-glycosidic or S-glycosidic linkages in substrates such as oligosaccharides, polysaccharides, glycoproteins and nucleosides.
Why Is hydrolase activity, acting on glycosyl bonds Important in Cell Biology?
GO:0016798 is important because glycosyl-bond hydrolysis is a universal biochemical reaction required for carbon cycling, cell-wall metabolism, glycoprotein quality control and lysosomal degradation. In biotechnology, glycoside hydrolases are used for biofuel production, food processing and glycan engineering. In medicine, mutations in glycosyl hydrolases cause inherited metabolic disorders, and altered glycosidase expression is a hallmark of cancer and inflammatory disease. Understanding which enzyme acts on which glycosyl bond, and how its activity is regulated, is therefore essential for both basic biology and therapeutic development.
• Enables degradation of plant and microbial polysaccharides for biofuel and industrial biotechnology.
• Controls cell-wall remodeling and autolysis in fungi and plants.
• Participates in N-glycan processing and glycoprotein maturation in the secretory pathway.
• Mediates lysosomal catabolism of glycoconjugates; defects cause storage disorders.
• Supports plant defense responses against nematodes and other pathogens.
• Contributes to cold-stress adaptation and transcriptome reprogramming in plants.
• Provides cold-adapted enzymes for low-temperature industrial processes.
• Serves as a target class for inhibitor and activator discovery in metabolic disease.
• Enables glycoengineering of therapeutic proteins through controlled deglycosylation.
• Offers selectable markers and reporters in fungal and bacterial genetics.
Molecular Mechanism of hydrolase activity, acting on glycosyl bonds
Substrate recognition and glycosyl bond binding
In simple terms: The enzyme first grabs the sugar-linked substrate and positions the glycosyl bond in its active site.
Glycosyl-bond hydrolases contain substrate-binding clefts or pockets that recognize specific sugar configurations and aglycone moieties. Structural studies of Aspergillus GH3 beta-glucosidases show a TIM-barrel fold with conserved glutamate residues that contact the glucose moiety and the leaving group. In GH51 enzymes, a similar pocket accommodates arabinofuranoside or xylan substrates, determining exo versus endo specificity. Cold-adapted 1,3-alpha-3,6-anhydro-L-galactosidase Ahg558 displays a substrate-binding architecture tuned to agarose-derived oligosaccharides at low temperature.
Catalytic hydrolysis via acid/base and nucleophile residues
In simple terms: Two key acidic residues in the active site use water to split the glycosyl bond.
The canonical mechanism involves two carboxylate residues, one acting as a general acid/base and the other as a nucleophile or base, stabilizing an oxocarbenium-ion-like transition state. In GH3 beta-glucosidases, the catalytic pair is typically two glutamates within the TIM-barrel, and mutation of either abolishes activity. GH51 enzymes use a retaining mechanism in which the anomeric configuration is preserved after hydrolysis. The 1,3-beta-glucan hydrolases from Coprinopsis cinerea cleave beta-1,3 linkages with retention of configuration, consistent with a double-displacement mechanism.
Cofactors, metal dependence and pH optima
In simple terms: Some of these enzymes need metal ions or specific pH conditions to work efficiently.
Many glycosyl-bond hydrolases are metal-independent, but some family members require calcium or other ions for folding or catalysis. The cold-adapted alkaline 1,3-alpha-3,6-anhydro-L-galactosidase Ahg558 is active at alkaline pH and low temperature, reflecting adaptation to its marine environment. The human C-alpha-formylglycine-generating enzyme, which acts on sulfatase substrates, illustrates that glycosyl-bond-related chemistry can be coupled to oxidative cofactor generation in the endoplasmic reticulum. Optimal pH and temperature vary widely and are key parameters for industrial application.
Processive versus distributive action and synergy
In simple terms: Some enzymes cut one bond at a time, while others slide along the chain; mixtures can act synergistically.
Exo-acting enzymes remove terminal sugars processively, whereas endo-acting enzymes cleave internal linkages distributively. A group of 1,3-beta-glucan hydrolases from Coprinopsis cinerea pilei acts synergistically during autolysis, combining exo and endo activities to degrade the cell wall efficiently. In biomass saccharification, GH51 exo-alpha-L-arabinofuranosidase/endo-xylanase bifunctional enzymes enhance xylan breakdown by removing arabinose decorations and cleaving the xylan backbone. Such synergy is exploited in industrial enzyme cocktails.
Transcriptional regulation of glycosyl hydrolase genes
In simple terms: Cells switch these enzymes on or off depending on the available carbon source or stress.
In the thermophilic fungus Myceliophthora thermophila, the forkhead transcription factor MtFKH1 controls expression of cellulase and xylanase genes, linking glycosyl-bond hydrolase production to carbon-source sensing. In tomato, Paraburkholderia tropica primes a multilayered transcriptional defense response against Meloidogyne nematodes, involving glycosyl hydrolase genes among the induced transcripts. Cold stress in Rhododendron chrysanthum reprogrammes transcript and protein levels of carbohydrate-active enzymes, including glycosyl hydrolases. These examples show that GO:0016798 activity is dynamically regulated at the transcriptional level in response to environmental and developmental cues.
Key Genes Involved in GO:0016798 hydrolase activity, acting on glycosyl bonds
The following genes and proteins represent experimentally characterized members of GO:0016798 across microbial, plant and human systems.
| Gene | Major Role | Research Relevance |
|---|---|---|
| GH3 beta-glucosidase (Aspergillus sp.) | Hydrolyzes beta-D-glucosidic bonds in cellobiose and glucosides | Structural model for GH3 family; heavily N-glycosylated |
| GH51 exo-alpha-L-arabinofuranosidase/endo-xylanase (Alicyclobacillus sp. A4) | Bifunctional cleavage of arabinofuranoside and xylan linkages | Biomass-degrading enzyme for biofuel research |
| 1,3-beta-glucan hydrolase (Coprinopsis cinerea) | Degrades beta-1,3-glucan during fruiting-body autolysis | Model for fungal cell-wall remodeling and synergy |
| Ahg558 (Gayadomonas joobiniege G7) | Cold-adapted alkaline 1,3-alpha-3,6-anhydro-L-galactosidase | Marine agarose degradation; cold-adapted biocatalyst |
| MtFKH1 (Myceliophthora thermophila) | Forkhead transcription factor controlling cellulase and xylanase genes | Regulator of glycosyl hydrolase gene expression |
| C-alpha-formylglycine-generating enzyme (human) | Generates formylglycine in sulfatases; linked to glycosylation pathways | Congenital disorder of glycosylation research |
| Tomato glycosyl hydrolase genes (Solanum lycopersicum) | Defense-related glycan cleavage during nematode infection | Plant immunity and priming studies |
| Rhododendron chrysanthum carbohydrate-active enzymes | Cold-responsive glycan turnover | Plant cold-stress transcriptomics and proteomics |
| Cellulase genes (M. thermophila) | Cellulose deconstruction | Industrial saccharification and MtFKH1 target |
| Xylanase genes (M. thermophila) | Xylan backbone cleavage | Hemicellulose utilization and MtFKH1 target |
| Beta-glucosidase (GH3 family) | Terminal glucose release from glucosides | Rate-limiting step in cellulose hydrolysis |
| Endo-xylanase (GH51) | Internal xylan cleavage | Synergy with arabinofuranosidase |
| Exo-alpha-L-arabinofuranosidase (GH51) | Removes arabinose decorations | Hemicellulose accessibility |
| 1,3-beta-glucanase (fungal) | Cell-wall beta-glucan turnover | Autolysis and morphogenesis |
| Agarase-related 1,3-alpha-3,6-anhydro-L-galactosidase | Cleaves agarose-derived glycosyl bonds | Marine polysaccharide biotechnology |
| N-glycosylase (conceptual class) | Cleaves N-glycosidic bonds in nucleotides or glycoproteins | DNA repair and glycoprotein processing |
How Is hydrolase activity, acting on glycosyl bonds Regulated?
GO:0016798 activity is regulated at multiple levels. Transcriptionally, the forkhead factor MtFKH1 controls cellulase and xylanase gene expression in Myceliophthora thermophila in response to carbon source. In plants, biotic stress such as Meloidogyne infection primes a multilayered defense transcriptome that includes glycosyl hydrolase genes, and cold stress reprograms carbohydrate-active enzyme transcripts and proteins in Rhododendron chrysanthum. Post-translationally, N-glycosylation of fungal GH3 beta-glucosidases affects folding and secretion. Enzyme activity is also tuned by pH, temperature and metal availability, as shown for the cold-adapted alkaline Ahg558. In humans, the C-alpha-formylglycine-generating enzyme illustrates how glycosylation-related chemistry is coupled to ER quality control.
hydrolase activity, acting on glycosyl bonds and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| C-alpha-formylglycine-generating enzyme | Multiple sulfatase deficiency / congenital disorder of glycosylation | Knockout HEK293 or patient iPSC-derived fibroblasts |
| GH3 beta-glucosidase | Glycan remodeling in cancer and lysosomal dysfunction | Overexpression and point-mutation in cancer cell lines |
| 1,3-beta-glucan hydrolase | Fungal cell-wall integrity and virulence | Knockout in Coprinopsis cinerea or Candida albicans |
| Tomato glycosyl hydrolase genes | Nematode resistance and plant immunity | Knockout and overexpression in tomato roots |
| MtFKH1-regulated cellulase/xylanase | Carbon-source sensing and biomass degradation | Knockout and tagged knock-in in M. thermophila |
Lysosomal storage disorders and glycosidase deficiencies
Deficiencies in glycosyl-bond hydrolases that degrade glycoconjugates in the lysosome cause accumulation of undigested substrates and multisystem disease. The human C-alpha-formylglycine-generating enzyme is required for activation of sulfatases, and its dysfunction leads to congenital disorders of glycosylation and multiple sulfatase deficiency. These conditions illustrate the clinical importance of proper glycosyl-bond hydrolysis in catabolic pathways.
Cancer and altered glycan remodeling
Tumor cells frequently display altered glycosylation patterns, and glycosidases that remodel N-glycans contribute to invasion, metastasis and immune evasion. Structural and biochemical studies of GH3 beta-glucosidases and related enzymes provide templates for designing inhibitors that could modulate glycan processing in cancer. Although direct clinical evidence for GO:0016798 in cancer is still emerging, the pathway is a plausible therapeutic target.
Infectious disease and host-pathogen interactions
Plant-parasitic nematodes such as Meloidogyne induce defense responses in tomato that include glycosyl hydrolase genes, highlighting the role of these enzymes in host-pathogen interactions. In fungi, autolytic 1,3-beta-glucan hydrolases are required for cell-wall remodeling during morphogenesis and may influence virulence. Understanding these enzymes could inform crop protection and antifungal strategies.
Metabolic and cold-stress adaptation
Cold stress in Rhododendron chrysanthum alters the abundance of carbohydrate-active enzymes, including glycosyl hydrolases, as part of a broader metabolic reprogramming. In marine bacteria, cold-adapted alkaline glycosidases such as Ahg558 enable growth on agarose at low temperatures. These examples link GO:0016798 to environmental adaptation and biotechnological enzyme discovery.
From hydrolase activity, acting on glycosyl bonds-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is the glycosyl hydrolase essential for substrate utilization? | CRISPR knockout in bacterial or fungal host |
| Does a catalytic residue mutation abolish activity? | Point mutation of predicted acid/base or nucleophile |
| Can a fluorescent tag report enzyme localization? | Knock-in of GFP or mCherry at the endogenous locus |
| Does overexpression enhance biomass degradation? | Overexpression of GH51 or GH3 enzyme in industrial strain |
| Which transcription factors regulate the enzyme? | Knockout of MtFKH1 followed by RNA-seq |
| Does the enzyme contribute to plant defense? | Knockout in tomato and nematode infection assay |
How to Study the hydrolase activity, acting on glycosyl bonds Process
| Method | What It Measures | Typical Application |
|---|---|---|
| pNP-glycoside assay | Hydrolytic activity and kinetics | Characterization of GH3 beta-glucosidase |
| Xylan-azure assay | Endo-xylanase activity | GH51 bifunctional enzyme testing |
| X-ray crystallography | Three-dimensional structure and catalytic residues | GH3 beta-glucosidase structure |
| RNA-seq | Transcript abundance of glycosyl hydrolase genes | MtFKH1 regulon and plant defense |
| Proteomics | Protein abundance and post-translational modifications | Cold-stress carbohydrate-active enzymes |
| CRISPR knockout | Gene essentiality and phenotype | Fungal cellulase regulation |
| Site-directed mutagenesis | Catalytic residue function | GH3 and GH51 mechanism |
| Enzyme synergy assay | Combined activity of multiple hydrolases | Fungal autolysis and biomass degradation |
Enzyme activity assays
Glycosyl-bond hydrolase activity is measured using chromogenic or fluorogenic substrates such as pNP-glycosides or resorufin glycosides. For beta-glucosidases, pNP-beta-D-glucopyranoside is standard; for xylanases, xylan-azure or DNS assays are used. Cold-adapted enzymes like Ahg558 require assays at low temperature and alkaline pH. These assays provide kinetic parameters (Km, kcat) and confirm GO:0016798 annotation.
Structural biology and homology modeling
X-ray crystallography and cryo-EM reveal the TIM-barrel or other folds, catalytic residues and N-glycosylation sites of glycosyl hydrolases. Structures of GH3 beta-glucosidases from Aspergillus sp. show heavily N-glycosylated surfaces that influence stability and secretion. Homology models of GH51 and agarase-related enzymes guide mutagenesis of catalytic residues.
Transcriptomics and proteomics
RNA-seq and proteomics identify glycosyl hydrolase genes induced by carbon source, cold or pathogen attack. In M. thermophila, MtFKH1 knockout followed by RNA-seq revealed its regulon of cellulase and xylanase genes. In tomato, transcriptomics of Paraburkholderia tropica-primed roots showed defense-related glycosyl hydrolases. Rhododendron cold-stress studies integrated transcriptomic and proteomic data to find carbohydrate-active enzymes.
CRISPR screens and functional genomics
Pooled CRISPR knockout libraries can systematically test which glycosyl hydrolase genes are required for growth on specific carbon sources or for stress survival. In filamentous fungi, CRISPR-based editing of transcription factor genes such as MtFKH1 enables causal testing of regulatory networks. In plants, CRISPR knockout of candidate glycosyl hydrolases can be combined with pathogen infection assays to link genotype to defense phenotype.
How CRISPR Can Be Used to Study GO:0016798 hydrolase activity, acting on glycosyl bonds
Knockout
CRISPR knockout of a glycosyl hydrolase gene is used to test whether the enzyme is required for growth on a specific polysaccharide, for cell-wall integrity or for host defense. In M. thermophila, knockout of the transcription factor MtFKH1 reduces cellulase and xylanase expression, demonstrating its role in regulating GO:0016798 genes. In tomato, knockout of defense-related glycosyl hydrolases can be tested in nematode infection assays.
Point Mutation
Point mutation of predicted catalytic acid/base or nucleophile residues is used to confirm the enzymatic mechanism of glycosyl-bond hydrolysis. For GH3 beta-glucosidases, mutation of the conserved glutamate pair abolishes activity, validating the double-displacement mechanism. Similar approaches apply to GH51 and agarase-related enzymes.
Knock-in
Knock-in of fluorescent or affinity tags at the endogenous locus enables real-time localization and purification of glycosyl hydrolases. Tagged knock-in of 1,3-beta-glucan hydrolases in Coprinopsis cinerea allows tracking during autolysis. Knock-in of epitope tags in human glycosidases facilitates interactome studies.
Overexpression
Overexpression of glycosyl hydrolases is used to enhance biomass degradation, improve glycan remodeling or produce recombinant enzymes for industry. Overexpression of GH51 bifunctional enzyme in a heterologous host increases xylan breakdown. In M. thermophila, overexpression of MtFKH1 or its targets can boost cellulase and xylanase production.
How EDITGENE Supports hydrolase activity, acting on glycosyl bonds Research
Researchers studying hydrolase activity, acting on glycosyl bonds-related genes often need to determine whether a candidate gene is causally involved in substrate utilization, glycan processing or disease. EDITGENE provides end-to-end CRISPR services to generate precisely engineered cell models for such functional studies.
Contact EDITGENE today to design your custom CRISPR model for hydrolase activity, acting on glycosyl bonds research.
Frequently Asked Questions About hydrolase activity, acting on glycosyl bonds
What is GO:0016798?
GO:0016798 is the Gene Ontology molecular function term for hydrolase activity, acting on glycosyl bonds, defined as catalysis of the hydrolysis of any glycosyl bond.
What enzymes belong to hydrolase activity, acting on glycosyl bonds?
The term includes glycoside hydrolases, glycosylases and N-glycosylases such as GH3 beta-glucosidases, GH51 exo-alpha-L-arabinofuranosidase/endo-xylanase, 1,3-beta-glucan hydrolases and agarases.
What genes are involved in hydrolase activity, acting on glycosyl bonds?
Examples include GH3 beta-glucosidase, GH51 bifunctional arabinofuranosidase/xylanase, 1,3-beta-glucan hydrolase, Ahg558, MtFKH1-regulated cellulases and xylanases, and the human C-alpha-formylglycine-generating enzyme.
What is the mechanism of glycosyl bond hydrolysis?
Most enzymes use two carboxylate residues, one as acid/base and one as nucleophile, to cleave the glycosyl bond via an oxocarbenium-ion-like transition state, often with retention of anomeric configuration.
Why is GO:0016798 important for biotechnology?
These enzymes are used for biomass saccharification, biofuel production, food processing and glycan engineering, and cold-adapted variants enable low-temperature industrial processes.
How is hydrolase activity, acting on glycosyl bonds regulated?
Regulation occurs transcriptionally, for example by MtFKH1 in M. thermophila, and in response to biotic and abiotic stress in plants, as well as post-translationally via N-glycosylation.
What diseases are linked to glycosyl hydrolase defects?
Defects in glycosyl hydrolases and related enzymes cause lysosomal storage disorders and congenital disorders of glycosylation, and altered glycosidase activity is associated with cancer.
How can I study GO:0016798 in the lab?
Common methods include pNP-glycoside activity assays, X-ray crystallography, RNA-seq, proteomics, CRISPR knockout and site-directed mutagenesis.
Can CRISPR be used to study glycosyl hydrolase genes?
Yes, CRISPR knockout, point mutation, knock-in and overexpression are widely used to test the function of glycosyl hydrolase genes in microbes, plants and human cells.
What model organisms are used for glycosyl hydrolase research?
Model systems include Aspergillus sp., Alicyclobacillus sp., Coprinopsis cinerea, Gayadomonas joobiniege, Myceliophthora thermophila, tomato and human cell lines.
Conclusion
GO:0016798, hydrolase activity, acting on glycosyl bonds, defines a large and functionally diverse enzyme class that cleaves glycosidic linkages in carbohydrates, glycoproteins and glycoconjugates. Its members are central to biomass degradation, cell-wall remodeling, glycoprotein processing and lysosomal catabolism, with direct relevance to biotechnology and human disease. CRISPR-based knockout, point-mutation, knock-in and overexpression models now allow precise causal testing of individual glycosyl hydrolase genes in physiologically relevant systems. Continued integration of structural, biochemical and functional genomics approaches will clarify how these enzymes are regulated and how they can be harnessed or inhibited therapeutically.
References
- 1. González-Cardona C et al.. 2024. Paraburkholderia tropica Primes a Multilayered Transcriptional Defense Response to the Nematode Meloidogyne spp. in Tomato.. Int J Mol Sci 25(23) PMID: 39684296
- 2. Zhang Q et al.. 2023. Integration of transcriptomic and proteomic analyses of Rhododendron chrysanthum Pall. in response to cold stress in the Changbai Mountains.. Mol Biol Rep 50(4):3607-3616 PMID: 36418773
- 3. Yang W et al.. 2015. A novel bifunctional GH51 exo-α-l-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity.. Biotechnol Biofuels 8:197 PMID: 26628911
- 4. Agirre J et al.. 2016. Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. family GH3 β-D-glucosidases.. Acta Crystallogr D Struct Biol 72(Pt 2):254-65 PMID: 26894673
- 5. Zhou Y et al.. 2015. Purification, characterization and synergism in autolysis of a group of 1,3-β-glucan hydrolases from the pilei of Coprinopsis cinerea fruiting bodies.. Microbiology (Reading) 161(10):1978-1989 PMID: 26199012
- 6. Preusser-Kunze A et al.. 2005. Molecular characterization of the human Calpha-formylglycine-generating enzyme.. J Biol Chem 280(15):14900-10 PMID: 15657036
- 7. Lai Y et al.. 2025. Identification of a novel forkhead transcription factor MtFKH1 for cellulase and xylanase gene expression in Myceliophthora thermophila (ATCC 42464).. Microbiol Res 294:128097 PMID: 39970722
- 8. Asghar S et al.. 2019. Molecular Cloning and Characterization of a Novel Cold-Adapted Alkaline 1,3-α-3,6-Anhydro-L-galactosidase, Ahg558, from Gayadomonas joobiniege G7.. Appl Biochem Biotechnol 188(4):1077-1095 PMID: 30788710
