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Disorder prediction-based construct optimization improves activity and catalytic efficiency of Bacillus naganoensis pullulanase

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Practical protocols for production of very high yields of recombinant proteins using Escherichia coli

inferredcites →https://doi.org/10.1002/prot.22416openalex-snapshot

Structure of a pullulanase from Bacillus acidopullulyticus

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Functional and structural studies of pullulanase from Anoxybacillus sp. LM18-11

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Secretory and extracellular production of recombinant proteins using Escherichia coli

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Heterologous expression, secretion and characterization of the Geobacillus thermoleovorans US105 type I pullulanase

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Truncation of N- and C-terminal regions of Streptococcus mutans dextranase enhances catalytic activity

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Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification

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Influence of N-Terminal Truncations on the Functional Expression of Bacillus licheniformis γ-Glutamyltranspeptidase in Recombinant Escherichia coli

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A GH57 Family Amylopullulanase from Deep-Sea Thermococcus siculi: Expression of the Gene and Characterization of the Recombinant Enzyme

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Statistical Optimization of Pullulanase Production by Raoultella planticola DSMZ 4617 Using Sago Starch as Carbon and Peptone as Nitrogen Sources

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Signal Peptide-Independent Secretory Expression and Characterization of Pullulanase from a Newly Isolated Klebsiella variicola SHN-1 in Escherichia coli

inferredcites →https://doi.org/10.1007/s12010-015-1675-2openalex-snapshot

Single Amino Acid Substitution in the Pullulanase of Klebsiella variicola for Enhancing Thermostability and Catalytic Efficiency

inferredcites →https://doi.org/10.1016/j.bbapap.2013.01.010openalex-snapshot

FlgM proteins from different bacteria exhibit different structural characteristics

inferredcites →https://doi.org/10.1016/j.biochi.2013.12.010openalex-snapshot

Truncation of N-terminal regions of Digitalis lanata progesterone 5β-reductase alters catalytic efficiency and substrate preference

inferredcites →https://doi.org/10.1016/j.biortech.2008.06.001openalex-snapshot

Truncation of the cellulose binding domain improved thermal stability of endo-β-1,4-glucanase from Bacillus subtilis JA18

inferredcites →https://doi.org/10.1016/j.enzmictec.2003.07.001openalex-snapshot

Hydrolysis of starch by a mixture of glucoamylase and pullulanase entrapped individually in calcium alginate beads

inferredcites →https://doi.org/10.1016/j.enzmictec.2010.11.006openalex-snapshot

Molecular cloning and biochemical characterization of a heat-stable type I pullulanase from Thermotoga neapolitana

inferredcites →https://doi.org/10.1016/j.jbiosc.2008.10.019openalex-snapshot

Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137

inferredcites →https://doi.org/10.1016/j.jbiotec.2004.08.004openalex-snapshot

Advanced genetic strategies for recombinant protein expression in Escherichia coli

inferredcites →https://doi.org/10.1016/j.jbiotec.2015.06.406openalex-snapshot

Structure and sequence analysis-based engineering of pullulanase from Anoxybacillus sp. LM18-11 for improved thermostability

inferredcites →https://doi.org/10.1016/j.jmb.2006.03.058openalex-snapshot

Crystal Structure of Pullulanase: Evidence for Parallel Binding of Oligosaccharides in the Active Site

inferredcites →https://doi.org/10.1016/j.jmb.2006.10.018openalex-snapshot

The Structural Basis of α-Glucan Recognition by a Family 41 Carbohydrate-binding Module from Thermotoga maritima

inferredcites →https://doi.org/10.1016/j.jsb.2010.07.011openalex-snapshot

The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium

inferredcites →https://doi.org/10.1016/j.molcatb.2013.04.002openalex-snapshot

N-terminal truncation of a maleate cis–trans isomerase from Rhodococcus jostii RHA1 results in a highly active enzyme for the biocatalytic production of fumaric acid

inferredcites →https://doi.org/10.1016/j.pep.2005.01.016openalex-snapshot

Protein production by auto-induction in high-density shaking cultures

inferredcites →https://doi.org/10.1016/j.phytochem.2005.11.013openalex-snapshot

Molecular cloning and heterologous expression of progesterone 5β-reductase from Digitalis lanata Ehrh.

inferredcites →https://doi.org/10.1093/bioinformatics/bth476openalex-snapshot

DisProt: a database of protein disorder

inferredcites →https://doi.org/10.1107/s1744309106007901openalex-snapshot

Overexpression, purification and preliminary X-ray analysis of pullulanase fromBacillus subtilisstrain 168

inferredcites →https://doi.org/10.1128/aem.00457-13openalex-snapshot

Improving the Thermostability and Catalytic Efficiency of Bacillus deramificans Pullulanase by Site-Directed Mutagenesis

inferredcites →https://doi.org/10.1128/aem.03714-14openalex-snapshot

Enhancing the Secretion Efficiency and Thermostability of a Bacillusderamificans Pullulanase Mutant (D437H/D503Y) by N-Terminal Domain Truncation

inferredcites →https://doi.org/10.1128/aem.70.6.3407-3416.2004openalex-snapshot

Cloning, Sequencing, and Characterization of a Heat- and Alkali-Stable Type I Pullulanase from Anaerobranca gottschalkii

inferredcites →https://doi.org/10.1186/s12934-014-0138-8openalex-snapshot

High-quality production of human α-2,6-sialyltransferase in Pichia pastoris requires control over N-terminal truncations by host-inherent protease activities

inferredcites →https://doi.org/10.1371/journal.pone.0078416openalex-snapshot

High-Level Expression of Bacillus naganoensis Pullulanase from Recombinant Escherichia coli with Auto-Induction: Effect of lac Operator

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Rational Engineering of Homospermidine Synthase for Enhanced Catalytic Efficiency Toward Spermidine Synthesis

inferred← citeshttps://doi.org/10.1002/1873-3468.13652openalex-snapshot

Evolutionary coupling saturation mutagenesis: Coevolution‐guided identification of distant sites influencing Bacillus naganoensis pullulanase activity

inferred← citeshttps://doi.org/10.1002/jcc.26562openalex-snapshot

Modifying the catalytic preference of alpha‐amylase toward n‐alkanes for bioremediation purposes using in silico strategies

inferred← citeshttps://doi.org/10.1007/978-981-19-7026-9_2openalex-snapshot

Classification and Enzyme Properties of Starch Debranching Enzymes

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Sequence, Structure, and Engineering of Microbial Starch Debranching Enzymes

inferred← citeshttps://doi.org/10.1007/s11274-021-03010-9openalex-snapshot

Biotechnology and bioengineering of pullulanase: state of the art and perspectives

inferred← citeshttps://doi.org/10.1007/s12010-020-03419-2openalex-snapshot

Improve Production of Pullulanase of Bacillus subtilis in Batch and Fed-Batch Cultures

inferred← citeshttps://doi.org/10.1016/j.biortech.2019.01.098openalex-snapshot

Industrially produced pullulanases with thermostability: Discovery, engineering, and heterologous expression

inferred← citeshttps://doi.org/10.1016/j.biotechadv.2021.107786openalex-snapshot

Microbial starch debranching enzymes: Developments and applications

inferred← citeshttps://doi.org/10.1016/j.enzmictec.2019.01.010openalex-snapshot

Hydrogen-bond-based protein engineering for the acidic adaptation of Bacillus acidopullulyticus pullulanase

inferred← citeshttps://doi.org/10.1016/j.enzmictec.2023.110290openalex-snapshot

Improved thermostability of type I pullulanase from Bacillus thermoliquefaciens by error-prone PCR

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.06.151openalex-snapshot

Modulating the pH profile of the pullulanase from Pyrococcus yayanosii CH1 by synergistically engineering the active center and surface

inferred← citeshttps://doi.org/10.1016/j.jmgm.2021.108043openalex-snapshot

Exploring the factors that affect the themostability of barley limit dextrinase – Inhibitor complex

inferred← citeshttps://doi.org/10.1016/j.pep.2018.09.011openalex-snapshot

Improvement of extracellular secretion efficiency of Bacillus naganoensis pullulanase from recombinant Escherichia coli: Peptide fusion and cell wall modification

inferred← citeshttps://doi.org/10.1016/j.synbio.2024.04.012openalex-snapshot

Rational engineering of homospermidine synthase for enhanced catalytic efficiency toward spermidine synthesis

inferred← citeshttps://doi.org/10.1021/acs.jafc.8b03331openalex-snapshot

N-Terminal Domain Truncation and Domain Insertion-Based Engineering of a Novel Thermostable Type I Pullulanase from Geobacillus thermocatenulatus

inferred← citeshttps://doi.org/10.1021/acs.jafc.8b06002openalex-snapshot

Improvement of the Activity and Stability of Starch-Debranching Pullulanase from Bacillus naganoensis via Tailoring of the Active Sites Lining the Catalytic Pocket

inferred← citeshttps://doi.org/10.1021/acs.jafc.9b03376openalex-snapshot

A Hyperthermostable Type II Pullulanase from a Deep-Sea Microorganism Pyrococcus yayanosii CH1

inferred← citeshttps://doi.org/10.1039/c7fo01381gopenalex-snapshot

In vitro inhibition of pancreatic α-amylase by spherical and polygonal starch nanoparticles

inferred← citeshttps://doi.org/10.1186/s12934-018-1011-yopenalex-snapshot

Efficient production of extracellular pullulanase in Bacillus subtilis ATCC6051 using the host strain construction and promoter optimization expression system

inferred← citeshttps://doi.org/10.3389/fmolb.2020.00051openalex-snapshot

Understanding Thermostability Factors of Barley Limit Dextrinase by Molecular Dynamics Simulations

inferred← citeshttps://doi.org/10.3390/catal12020143openalex-snapshot

A Bibliometric Analysis and Review of Pullulan-Degrading Enzymes—Past and Current Trends

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