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organism: CLOCL
gene_id: Q9RGE8
gene_symbol: engK
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gene_info: Name=engK {ECO:0000313|EMBL:AAF06107.1};
organism_full: Clostridium cellulovorans.
protein_family: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
protein_domains: 6-hairpin_glycosidase_sf. (IPR008928); 6hp_glycosidase-like_sf.
(IPR012341); Cellulase_Ig-like. (IPR004197); CenC_carb-bd. (IPR003305); Dockerin_1_rpt.
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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q9RGE8
• Protein Description: RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361166}; EC=3.2.1.- {ECO:0000256|RuleBase:RU361166};
• Gene Information: Name=engK {ECO:0000313|EMBL:AAF06107.1};
• Organism (full): Clostridium cellulovorans.
• Protein Family: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
• Key Domains: 6-hairpin_glycosidase_sf. (IPR008928); 6hp_glycosidase-like_sf. (IPR012341); Cellulase_Ig-like. (IPR004197); CenC_carb-bd. (IPR003305); Dockerin_1_rpt. (IPR002105)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "engK" matches the protein description above
2. Verify the organism is correct: Clostridium cellulovorans.
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'engK' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene engK (gene ID: Q9RGE8, UniProt: Q9RGE8) in CLOCL.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q9RGE8
• Protein Description: RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361166}; EC=3.2.1.- {ECO:0000256|RuleBase:RU361166};
• Gene Information: Name=engK {ECO:0000313|EMBL:AAF06107.1};
• Organism (full): Clostridium cellulovorans.
• Protein Family: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
• Key Domains: 6-hairpin_glycosidase_sf. (IPR008928); 6hp_glycosidase-like_sf. (IPR012341); Cellulase_Ig-like. (IPR004197); CenC_carb-bd. (IPR003305); Dockerin_1_rpt. (IPR002105)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "engK" matches the protein description above
2. Verify the organism is correct: Clostridium cellulovorans.
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'engK' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene engK (gene ID: Q9RGE8, UniProt: Q9RGE8) in CLOCL.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Plan and verification summary
Objective 1 (identity) was completed. The gene symbol engK in Clostridium cellulovorans encodes a glycoside hydrolase family 9 (GH9) endoglucanase that is a dockerin-bearing cellulosomal subunit, matching UniProt Q9RGE8 and the domain expectations for GH9 cellulosomal enzymes. No conflicting use of engK in other organisms was found in the consulted literature (cho2010cellulosomicprofilingproduced pages 3-5, demain2005cellulaseclostridiaand pages 9-10).

Key concepts and definitions
Glycoside hydrolase family 9 (GH9) endoglucanases are modular cellulases that cleave internal β-1,4-glycosidic bonds of cellulose. In cellulosomal systems, GH9s often work with GH48 exoglucanases to convert cellulose to cellodextrins and cellobiose. Dockerin–cohesin interactions assemble these enzymes onto scaffoldins to form extracellular cellulosomes that can attach to cellulose and, in many species, to the bacterial surface (demain2005cellulaseclostridiaand pages 9-10, schwarz2004extracellularglycosylhydrolases pages 19-22, leis2017comparativecharacterizationof pages 12-13).

Recent developments and latest research (prioritize 2023–2024)
Two recent lines of evidence contextualize EngK. First, a 2024 review synthesizes current understanding of cellulase systems in soils and highlights the prevalence and roles of GH9 enzymes in cellulose depolymerization, reinforcing their centrality in natural lignocellulose conversion (Heliyon, 2024-01; https://doi.org/10.1016/j.heliyon.2024.e24022) (). Second, a 2024 genomic survey reveals continuing discovery of cellulosome-producing bacteria and diversity in their GH complements and regulation, underscoring the modular principles that also apply to C. cellulovorans cellulosomes (Frontiers in Microbiology, 2024-10; https://doi.org/10.3389/fmicb.2024.1473396) (). Within GH9s, mechanistic diversity in product patterns and processivity remains a focus, with comparative cellulosomal studies delineating four product-pattern types that inform cellulosome engineering (Biotechnology for Biofuels, 2017-10; https://doi.org/10.1186/s13068-017-0928-4) (leis2017comparativecharacterizationof pages 12-13).

Function, catalytic activity, and product profile of EngK
Biochemical assays of recombinant EngK from C. cellulovorans demonstrate endo-1,4-β-glucanase activity that yields predominantly cellobiose and short oligos; notably, products larger than cellotriose were not observed under the reported assay conditions. EngK acts on cellotriose and generates ≤DP3 products, consistent with a processive endoglucanase biased toward cellobiose release (AMB Express, 2016-01; https://doi.org/10.1186/s13568-015-0169-5) (yamamoto2016synergisticpropertiesof pages 3-4, yamamoto2016synergisticpropertiesof pages 1-3).

Domain architecture and cellulosomal status
Experimental proteomic profiling using a cohesin marker identified EngK as a dockerin-bearing, cellulosomal enzyme secreted by C. cellulovorans across multiple carbon sources, consistent with the GH9 catalytic core flanked by ancillary domains and a C-terminal dockerin. Classical architecture for GH9 cellulosomal enzymes includes an N-terminal Ig-like domain and a family 3c carbohydrate-binding module (CBM3c) adjacent to the catalytic domain, sometimes accompanied by CBM3b; the CBM3c is often essential for activity and can promote processivity by aligning substrate in the active-site cleft. These features align with the UniProt domain expectations (Ig-like, CBM/CBM-like, dockerin I) for EngK (Journal of Biotechnology, 2010-02; https://doi.org/10.1016/j.jbiotec.2009.11.020; Microbiol Mol Biol Rev, 2005-03; https://doi.org/10.1128/mmbr.69.1.124-154.2005; Adv Appl Microbiol, 2004-01; https://doi.org/10.1016/S0065-2164(04)56007-0) (cho2010cellulosomicprofilingproduced pages 3-5, demain2005cellulaseclostridiaand pages 9-10, schwarz2004extracellularglycosylhydrolases pages 19-22).

Cellular/extracellular localization
EngK is secreted and incorporated into extracellular cellulosome complexes via its dockerin domain, as demonstrated by cohesin-affinity profiling. Cellulosomes assemble on scaffoldins and can be cell-associated, positioning catalytic subunits like EngK in close proximity to cellulose at the cell–substrate interface (Journal of Biotechnology, 2010-02; https://doi.org/10.1016/j.jbiotec.2009.11.020; Microbiol Mol Biol Rev, 2005-03; https://doi.org/10.1128/mmbr.69.1.124-154.2005) (cho2010cellulosomicprofilingproduced pages 3-5, demain2005cellulaseclostridiaand pages 9-10).

Synergy with ExgS (GH48) and inhibition by cellobiose
EngK synergizes with the GH48 exoglucanase ExgS on acid-swollen cellulose. Although the ExgS+EngK pair showed lower maximal specific activity than ExgS+EngH, EngK+ExgS retained more activity in the presence of product inhibitor cellobiose: at 5 mg/mL cellobiose, EngK+ExgS activity was more than twice that of EngH+ExgS, whereas at 10 mg/mL activity was abolished for both. Structural modeling suggests EngK has fewer aromatic residues in the active-site cleft than EngH, potentially explaining its different product profile and reduced sensitivity to cellobiose (AMB Express, 2016-01; https://doi.org/10.1186/s13568-015-0169-5) (yamamoto2016synergisticpropertiesof pages 3-4, yamamoto2016synergisticpropertiesof pages 4-5).

GH9 roles in cellulosome efficiency and processivity
Comparative studies of cellulosomal GH9s reveal diverse hydrolysis modes, including processive endoglucanases that preferentially release cellobiose (pEG2) or cellotetraose (pEG4). A CBM3c adjoining the GH9 catalytic domain is often aligned with the active-site groove and reduces dissociation, increasing processivity. GH9–GH48 synergy on crystalline cellulose is strong and ratio-dependent; enforced proximity (e.g., in fusion constructs) enhances activity, highlighting the cellulosome’s architectural advantage (Biotechnol Biofuels, 2017-10; https://doi.org/10.1186/s13068-017-0928-4; Adv Appl Microbiol, 2004-01; https://doi.org/10.1016/S0065-2164(04)56007-0) (leis2017comparativecharacterizationof pages 12-13, schwarz2004extracellularglycosylhydrolases pages 19-22).

Regulation of cellulosomal composition in C. cellulovorans
Cohesin-affinity proteomics showed that dockerin-bearing subunit repertoires, including EngK, vary with carbon source (Avicel, xylan, AXP, cellobiose). Approximately 16–17 dockerin-containing proteins were detected depending on substrate, and relative abundances of core enzymes (e.g., EngH, ExgS) shifted, indicating environmental tuning of the cellulosome. EngK was identified among major, consistently produced cellulosomal enzymes across conditions, consistent with a role in core cellulose depolymerization (Journal of Biotechnology, 2010-02; https://doi.org/10.1016/j.jbiotec.2009.11.020) (cho2010cellulosomicprofilingproduced pages 3-5).

Current applications and real-world implementations
The mechanistic insights from GH9 diversity and GH9–GH48 synergy guide enzyme cocktail formulation and synthetic cellulosome design for biomass conversion. Reviews and surveys from 2024 emphasize GH9 prevalence in environmental cellulose turnover and the expanding catalog of cellulosome-producing bacteria, informing bioprospecting and engineering strategies for consolidated bioprocessing. The principles of dockerin–cohesin assembly and CBM3c-enhanced processivity are now widely used in constructing designer cellulosomes and fusion enzymes to improve activity on recalcitrant substrates (Heliyon, 2024-01; https://doi.org/10.1016/j.heliyon.2024.e24022; Front Microbiol, 2024-10; https://doi.org/10.3389/fmicb.2024.1473396; Biotechnol Biofuels, 2017-10; https://doi.org/10.1186/s13068-017-0928-4) (leis2017comparativecharacterizationof pages 12-13).

Expert opinions and authoritative analyses
Authoritative reviews synthesize that GH9 enzymes are core to cellulosome function, with CBM3c and Ig-like modules modulating catalysis and stability, and that enzyme diversity within the complex is essential for high cellulolytic efficiency on crystalline cellulose. The classical MMBR review and Advances in Applied Microbiology analysis articulate how cellulosomal proximity effects, substrate anchoring via scaffoldin CBMs, and dockerin–cohesin specificity translate into superior hydrolysis rates relative to free-enzyme systems (Microbiol Mol Biol Rev, 2005-03; https://doi.org/10.1128/mmbr.69.1.124-154.2005; Adv Appl Microbiol, 2004-01; https://doi.org/10.1016/S0065-2164(04)56007-0) (demain2005cellulaseclostridiaand pages 9-10, schwarz2004extracellularglycosylhydrolases pages 19-22).

Relevant statistics and data from recent studies
- EngK+ExgS maximal specific activity on swollen cellulose: 0.119 U/μmol; ExgS+EngH: 0.251 U/μmol. At 5 mg/mL cellobiose, EngK+ExgS retains >2× activity relative to EngH+ExgS; both inhibited completely at 10 mg/mL (AMB Express, 2016-01; https://doi.org/10.1186/s13568-015-0169-5) (yamamoto2016synergisticpropertiesof pages 3-4).
- Substrate-dependent composition: ~16 dockerin-containing proteins on Avicel; ~17 on xylan/AXP; EngK consistently detected among major subunits by cohesin marker profiling (Journal of Biotechnology, 2010-02; https://doi.org/10.1016/j.jbiotec.2009.11.020) (cho2010cellulosomicprofilingproduced pages 3-5).
- GH9 product-pattern classes in cellulosomes: exo/CBH-like, non-processive EG, processive EG producing cellotetraose (pEG4), and processive EG producing cellobiose (pEG2), with CBM3c promoting processivity (Biotechnol Biofuels, 2017-10; https://doi.org/10.1186/s13068-017-0928-4) (leis2017comparativecharacterizationof pages 12-13).

Limitations
Direct domain-mapping for EngK (e.g., exact presence of CBM3c and Ig-like modules) was inferred from family- and species-level patterns and dockerin-based proteomics; EngK’s precise domain composition in Q9RGE8 should be confirmed with full-length sequence/domain annotation resources or targeted structural studies. Nonetheless, the dockerin-bearing, cellulosomal GH9 identity and functional properties are well supported by experimental studies in C. cellulovorans (cho2010cellulosomicprofilingproduced pages 3-5, yamamoto2016synergisticpropertiesof pages 3-4, demain2005cellulaseclostridiaand pages 9-10).

Embedded artifact
| Aspect | Evidence / Details (citations) | Key data / statistics | Source (journal, year, URL) |
|---|---|---:|---|
| Identity / organism | EngK is a GH9 family endoglucanase from Clostridium cellulovorans; described as a cellulosomal subunit matching UniProt Q9RGE8 (engK). (cho2010cellulosomicprofilingproduced pages 3-5, demain2005cellulaseclostridiaand pages 9-10) | Gene/protein: engK (UniProt Q9RGE8); organism: Clostridium cellulovorans | Cho W. et al., Journal of Biotechnology, 2010. https://doi.org/10.1016/j.jbiotec.2009.11.020 (cho2010cellulosomicprofilingproduced pages 3-5) |
| Catalytic function & main products | Biochemical assays on recombinant EngK show endo-1,4-β-glucanase activity; products reported as primarily cellobiose and/or short oligos (no products > cellotriose reported in assays). (yamamoto2016synergisticpropertiesof pages 3-4, yamamoto2016synergisticpropertiesof pages 1-3) | Produces mainly cellobiose; acts on cellotriose and yields ≤ DP3 products in assay conditions | Yamamoto K. & Tamaru Y., AMB Express, 2016. https://doi.org/10.1186/s13568-015-0169-5 (yamamoto2016synergisticpropertiesof pages 3-4, yamamoto2016synergisticpropertiesof pages 1-3) |
| Synergy with ExgS (GH48) & cellobiose inhibition | EngK + ExgS show synergistic hydrolysis on swollen/acid-treated cellulose; combination is inhibited by cellobiose but the EngK+ExgS pair is less sensitive to 5 mg/mL cellobiose than EngH+ExgS. Structural modeling links fewer aromatic subsites in EngK to altered product profile and reduced inhibition. (yamamoto2016synergisticpropertiesof pages 3-4, yamamoto2016synergisticpropertiesof pages 4-5) | Reported specific activity: ExgS+EngK = 0.119 U/μmol vs ExgS+EngH = 0.251 U/μmol; EngK+ExgS retains >2× relative activity vs EngH+ExgS at 5 mg/mL cellobiose (no activity at 10 mg/mL). | Yamamoto K. & Tamaru Y., AMB Express, 2016. https://doi.org/10.1186/s13568-015-0169-5 (yamamoto2016synergisticpropertiesof pages 3-4, yamamoto2016synergisticpropertiesof pages 4-5) |
| Domain architecture & cellulosomal status | GH9 catalytic module commonly associated with CBM3c (or other CBMs), sometimes Ig-like modules and C-terminal dockerin; EngK is detected as dockerin-bearing (thus cellulosomal). Domain annotations consistent with GH9 modular patterns in clostridia. (demain2005cellulaseclostridiaand pages 9-10, schwarz2004extracellularglycosylhydrolases pages 19-22, cho2010cellulosomicprofilingproduced pages 3-5) | Modular organization: GH9 catalytic domain ± CBM3c/CBM3b and Ig-like module; C-terminal dockerin (cellulosome-targeting) reported for EngK | Demain A.L. et al., Microbiol Mol Biol Rev, 2005. https://doi.org/10.1128/mmbr.69.1.124-154.2005 (demain2005cellulaseclostridiaand pages 9-10); Schwarz W.H. et al., Adv Appl Microbiol, 2004. https://doi.org/10.1016/S0065-2164(04)56007-0 (schwarz2004extracellularglycosylhydrolases pages 19-22); Cho W. et al., 2010 (cho2010cellulosomicprofilingproduced pages 3-5) |
| Localization (extracellular / cellulosome association) | EngK detected among cohesin-binding (dockerin-containing) extracellular proteins; cellulosomal enzymes are secreted and assemble extracellularly on scaffoldins (e.g., CbpA/CipA) and can be cell-associated. (cho2010cellulosomicprofilingproduced pages 3-5, demain2005cellulaseclostridiaand pages 9-10) | Detected in extracellular proteome by cohesin marker; part of extracellular cellulosome complexes | Cho W. et al., Journal of Biotechnology, 2010. https://doi.org/10.1016/j.jbiotec.2009.11.020 (cho2010cellulosomicprofilingproduced pages 3-5); Demain A.L. et al., 2005 (demain2005cellulaseclostridiaand pages 9-10) |
| GH9 roles in processivity & product patterns | GH9 family shows four product-pattern classes (exo/CBH-like, non-processive EG, processive EG yielding cellotetraose pEG4, and processive pEG2 yielding cellobiose); CBM3c adjacent to GH9 often promotes processivity by aligning substrate and reducing koff. (leis2017comparativecharacterizationof pages 12-13, schwarz2004extracellularglycosylhydrolases pages 19-22) | GH9 diversity underpins processivity spectrum; CBM3c modulates processivity and product DP (Leis et al. 2017) | Leis B. et al., Biotechnol Biofuels, 2017. https://doi.org/10.1186/s13068-017-0928-4 (leis2017comparativecharacterizationof pages 12-13); Schwarz W.H. et al., 2004 (schwarz2004extracellularglycosylhydrolases pages 19-22) |
| Regulation of cellulosome composition vs carbon source | Proteomic/cohesin-marker profiling shows substrate-dependent variation in dockerin-bearing subunits; EngK is among major, consistently produced cellulosomal enzymes but relative abundances shift with carbon source (Avicel, xylan, cellobiose, etc.). (cho2010cellulosomicprofilingproduced pages 3-5, demain2005cellulaseclostridiaand pages 9-10) | Example: ~16 dockerin-containing proteins on Avicel; composition and relative intensities of EngH/ExgS/EngK vary by substrate. | Cho W. et al., Journal of Biotechnology, 2010. https://doi.org/10.1016/j.jbiotec.2009.11.020 (cho2010cellulosomicprofilingproduced pages 3-5); Demain A.L. et al., 2005 (demain2005cellulaseclostridiaand pages 9-10) |

Table: Compact evidence table summarizing EngK identity, function, modular architecture, localization, synergy/inhibition data, GH9 processivity roles, and substrate-dependent regulation; citations link each claim to the underlying literature contexts (yamamoto2016synergisticpropertiesof pages 3-4, cai2000analysisofcellulolytic pages 21-27).

References

1. (cho2010cellulosomicprofilingproduced pages 3-5): Woojae Cho, Sang Duck Jeon, Hyun Jung Shim, Roy H. Doi, and Sung Ok Han. Cellulosomic profiling produced by clostridium cellulovorans during growth on different carbon sources explored by the cohesin marker. Journal of biotechnology, 145 3:233-9, Feb 2010. URL: https://doi.org/10.1016/j.jbiotec.2009.11.020, doi:10.1016/j.jbiotec.2009.11.020. This article has 39 citations and is from a peer-reviewed journal.

2. (demain2005cellulaseclostridiaand pages 9-10): Arnold L. Demain, Michael Newcomb, and J. H. David Wu. Cellulase, clostridia, and ethanol. Microbiology and Molecular Biology Reviews, 69:124-154, Mar 2005. URL: https://doi.org/10.1128/mmbr.69.1.124-154.2005, doi:10.1128/mmbr.69.1.124-154.2005. This article has 1268 citations and is from a domain leading peer-reviewed journal.

3. (schwarz2004extracellularglycosylhydrolases pages 19-22): Wolfgang H. Schwarz, Vladimir V. Zverlov, and Hubert Bahl. Extracellular glycosyl hydrolases from clostridia. Advances in applied microbiology, 56:215-61, Jan 2004. URL: https://doi.org/10.1016/s0065-2164(04)56007-0, doi:10.1016/s0065-2164(04)56007-0. This article has 65 citations.

4. (leis2017comparativecharacterizationof pages 12-13): Benedikt Leis, Claudia Held, Fabian Bergkemper, Katharina Dennemarck, Robert Steinbauer, Alarich Reiter, Matthias Mechelke, Matthias Moerch, Sigrid Graubner, Wolfgang Liebl, Wolfgang H. Schwarz, and Vladimir V. Zverlov. Comparative characterization of all cellulosomal cellulases from clostridium thermocellum reveals high diversity in endoglucanase product formation essential for complex activity. Biotechnology for Biofuels, Oct 2017. URL: https://doi.org/10.1186/s13068-017-0928-4, doi:10.1186/s13068-017-0928-4. This article has 63 citations.

5. (yamamoto2016synergisticpropertiesof pages 3-4): Kosuke Yamamoto and Yutaka Tamaru. Synergistic properties of cellulases from clostridium cellulovorans in the presence of cellobiose. AMB Express, Jan 2016. URL: https://doi.org/10.1186/s13568-015-0169-5, doi:10.1186/s13568-015-0169-5. This article has 17 citations and is from a peer-reviewed journal.

6. (yamamoto2016synergisticpropertiesof pages 1-3): Kosuke Yamamoto and Yutaka Tamaru. Synergistic properties of cellulases from clostridium cellulovorans in the presence of cellobiose. AMB Express, Jan 2016. URL: https://doi.org/10.1186/s13568-015-0169-5, doi:10.1186/s13568-015-0169-5. This article has 17 citations and is from a peer-reviewed journal.

7. (yamamoto2016synergisticpropertiesof pages 4-5): Kosuke Yamamoto and Yutaka Tamaru. Synergistic properties of cellulases from clostridium cellulovorans in the presence of cellobiose. AMB Express, Jan 2016. URL: https://doi.org/10.1186/s13568-015-0169-5, doi:10.1186/s13568-015-0169-5. This article has 17 citations and is from a peer-reviewed journal.

8. (cai2000analysisofcellulolytic pages 21-27): J Cai. Analysis of cellulolytic activities of chimeric proteins from clostridium cellulovorans. Unknown journal, 2000.

Citations

1. leis2017comparativecharacterizationof pages 12-13
2. cho2010cellulosomicprofilingproduced pages 3-5
3. yamamoto2016synergisticpropertiesof pages 3-4
4. demain2005cellulaseclostridiaand pages 9-10
5. schwarz2004extracellularglycosylhydrolases pages 19-22
6. yamamoto2016synergisticpropertiesof pages 1-3
7. yamamoto2016synergisticpropertiesof pages 4-5
8. cai2000analysisofcellulolytic pages 21-27
9. https://doi.org/10.1016/j.heliyon.2024.e24022
10. https://doi.org/10.3389/fmicb.2024.1473396
11. https://doi.org/10.1186/s13068-017-0928-4
12. https://doi.org/10.1186/s13568-015-0169-5
13. https://doi.org/10.1016/j.jbiotec.2009.11.020;
14. https://doi.org/10.1128/mmbr.69.1.124-154.2005;
15. https://doi.org/10.1016/S0065-2164(04
16. https://doi.org/10.1128/mmbr.69.1.124-154.2005
17. https://doi.org/10.1186/s13068-017-0928-4;
18. https://doi.org/10.1016/j.jbiotec.2009.11.020
19. https://doi.org/10.1016/j.heliyon.2024.e24022;
20. https://doi.org/10.3389/fmicb.2024.1473396;
21. https://doi.org/10.1016/j.jbiotec.2009.11.020,
22. https://doi.org/10.1128/mmbr.69.1.124-154.2005,
23. https://doi.org/10.1016/s0065-2164(04
24. https://doi.org/10.1186/s13068-017-0928-4,
25. https://doi.org/10.1186/s13568-015-0169-5,