On the public citation graph

Production of Thermostable Lipolytic Activity by Thermus Species

0 signed · 76 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

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

inferredcites →https://doi.org/10.1007/978-3-662-13187-9_77openalex-snapshot
Extreme Thermophiles of the Genera Thermus and Sulfolobus
inferredcites →https://doi.org/10.1007/bf00128277openalex-snapshot
Lipase activity of thermophilic bacteria from icelandic hot springs
inferredcites →https://doi.org/10.1007/bf00164484openalex-snapshot
Identification of new enzyme activities of several strains of Thermus species
inferredcites →https://doi.org/10.1007/bf00499510openalex-snapshot
Growth kinetics of Thermus thermophilus
inferredcites →https://doi.org/10.1007/s00253-001-0843-1openalex-snapshot
Biotechnologically relevant enzymes from Thermus thermophilus
inferredcites →https://doi.org/10.1007/s002530000353openalex-snapshot
Purification and characterization of a thermostable esterase from the moderate thermophile Bacillus circulans
inferredcites →https://doi.org/10.1007/s002530051036openalex-snapshot
Determination of the kinetic parameters during continuous cultivation of the lipase-producing thermophile Bacillus sp. IHI-91 on olive oil
inferredcites →https://doi.org/10.1007/s002530051190openalex-snapshot
High-level expression of the thermoalkalophilic lipase from Bacillus thermocatenulatus in Escherichia coli
inferredcites →https://doi.org/10.1007/s002530051650openalex-snapshot
Response of the thermophile Thermus sp. RQ-1 to hyperbaric air in batch and fed-batch cultivation
inferredcites →https://doi.org/10.1007/s00792-001-0246-3openalex-snapshot
The periplasmic space in Thermus thermophilus : evidence from a regulation-defective S-layer mutant overexpressing an alkaline phosphatase
inferredcites →https://doi.org/10.1007/s007920070006openalex-snapshot
Isolation and characterization of lipid-degrading Bacillus thermoleovorans IHI-91 from an icelandic hot spring
inferredcites →https://doi.org/10.1016/0005-2760(96)00027-6openalex-snapshot
Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. Molecular cloning, nucleotide sequence, purification and some properties
inferredcites →https://doi.org/10.1016/0960-8524(93)90170-gopenalex-snapshot
Characterization of microbial biomasses and amylolytic preparations obtained from mussel processing waste treatment
inferredcites →https://doi.org/10.1016/j.gene.2003.12.029openalex-snapshot
Molecular cloning and characterization of two thermostable carboxyl esterases from Geobacillus stearothermophilus
inferredcites →https://doi.org/10.1016/j.jbiotec.2005.01.019openalex-snapshot
Identification of extracellular lipases/esterases produced by Thermus thermophilus HB27: Partial purification and preliminary biochemical characterisation
inferredcites →https://doi.org/10.1016/s0076-6879(97)84013-xopenalex-snapshot
[11] Two novel lipases from thermophile Bacillus thermocatenulatus: Screening, purification, cloning, overexpression, and properties
inferredcites →https://doi.org/10.1016/s0141-0229(98)00127-6openalex-snapshot
A thermostable esterase activity from newly isolated moderate thermophilic bacterial strains
inferredcites →https://doi.org/10.1016/s0141-0229(99)00075-7openalex-snapshot
Biocatalysis in organic media using enzymes from extremophiles
inferredcites →https://doi.org/10.1016/s0167-7799(02)02073-5openalex-snapshot
The production of biocatalysts and biomolecules from extremophiles
inferredcites →https://doi.org/10.1016/s0308-8146(98)00069-7openalex-snapshot
Isolation and some properties of β-galactosidase from the thermophilic bacterium Thermus thermophilus
inferredcites →https://doi.org/10.1016/s1367-5931(00)00183-6openalex-snapshot
Enzymes from extremophiles
inferredcites →https://doi.org/10.1016/s1389-1723(03)80114-7openalex-snapshot
Effect of Aeration and Agitation on Growth Rate of Thermus thermophilus in Batch Mode.
inferredcites →https://doi.org/10.1021/op020019hopenalex-snapshot
High-Throughput Screening of Thermostable Esterases for Industrial Bioconversions
inferredcites →https://doi.org/10.1023/a:1025076121700openalex-snapshot
Thermostable esterase from Thermoanaerobacter tengcongensis: high-level expression, purification and characterization
inferredcites →https://doi.org/10.1023/b:bile.0000024092.27943.75openalex-snapshot
Quantification of intra- and extra-cellular thermophilic lipase/esterase production by Thermus sp.
inferredcites →https://doi.org/10.1023/b:wibi.0000007330.84569.39openalex-snapshot
Screening and identification of extracellular lipase-producing thermophilic bacteria from a Malaysian hot spring
inferredcites →https://doi.org/10.1042/bj3320203openalex-snapshot
Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily
inferredcites →https://doi.org/10.1111/j.1470-8744.1997.tb00411.xopenalex-snapshot
Purification, properties and characterization of a high‐molecular‐mass b‐galactosidase isoenzyme from Thermusaquaticus YT‐I
inferredcites →https://doi.org/10.1111/j.1574-6968.1994.tb07030.xopenalex-snapshot
A thermophilic, lipolyticBacillussp., and continuous assay of itsp-nitrophenyl-palmitate esterase activity
inferredcites →https://doi.org/10.1128/aem.68.8.3925-3931.2002openalex-snapshot
Extremely Stable and Versatile Carboxylesterase from a Hyperthermophilic Archaeon
inferredcites →https://doi.org/10.1128/aem.71.2.817-825.2005openalex-snapshot
New Thermophilic and Thermostable Esterase with Sequence Similarity to the Hormone-Sensitive Lipase Family, Cloned from a Metagenomic Library
inferredcites →https://doi.org/10.1128/br.33.4.476-504.1969openalex-snapshot
Thermophilic blue-green algae and the thermal environment
inferredcites →https://doi.org/10.1128/jb.180.12.3137-3143.1998openalex-snapshot
Anaerobic Growth, a Property Horizontally Transferred by an Hfr-Like Mechanism among Extreme Thermophiles
inferredcites →https://doi.org/10.1128/jb.98.1.289-297.1969openalex-snapshot
Thermus aquaticus gen. n. and sp. n., a Nonsporulating Extreme Thermophile
inferredcites →https://doi.org/10.1271/bbb.62.2035openalex-snapshot
P1-Specificity of Aqualysin I (a Subtilisin-type Serine Protease) fromThermus aquaticusYT-1, using P1-Substituted Derivatives ofStreptomycesSubtilisin Inhibitor
inferredcites →https://doi.org/10.1271/bbb.62.2375openalex-snapshot
Cloning, Sequencing, High Expression, and Crystallization of the ThermophileThermus aquaticusGlycerol Kinase
inferredcites →https://doi.org/10.1271/bbb.64.280openalex-snapshot
Thermostable Lipase ofBacillus stearothermophilus: High-level Production, Purification, and Calcium-dependent Thermostability
inferredcites →https://doi.org/10.1271/bbb.68.2289openalex-snapshot
Thermostable Esterase from a Thermoacidophilic Archaeon: Purification and Characterization for Enzymatic Resolution of a Chiral Compound
inferredcites →https://doi.org/10.1271/bbb1961.52.1755openalex-snapshot
Isolation and characterization of a thermostable aminopeptidase(aminopeptidase T) from Thermus aquaticus YT-1, an extremely thermophilic bacterium.

What points at this work

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

inferred← citeshttps://doi.org/10.2139/ssrn.4153352openalex-extracted
Harnessing Extremophilic Lipases for Biodiesel Production in Biocompatible Ionic Liquids
inferred← citeshttps://doi.org/10.1002/ceat.200800613openalex-snapshot
Assessment of Relevant Factors Influencing Lipolytic Enzyme Production by Thermus thermophilus HB27 in Laboratory‐Scale Bioreactors
inferred← citeshttps://doi.org/10.1002/ceat.201100528openalex-snapshot
Targeting the Production of Biomolecules by Extremophiles at Bioreactor Scale
inferred← citeshttps://doi.org/10.1002/jctb.2211openalex-snapshot
Evaluation of a novel Bacillus strain from a north‐western Spain hot spring as a source of extracellular thermostable lipase
inferred← citeshttps://doi.org/10.1002/jctb.2301openalex-snapshot
A comprehensive study of lipase production by Yarrowia lipolytica CECT 1240 (ATCC 18942): from shake flask to continuous bioreactor
inferred← citeshttps://doi.org/10.1002/jctb.2597openalex-snapshot
On the hyperthermostability of lipolytic enzymes from Thermus aquaticus YT‐1: exploring their application to polymer degradation
inferred← citeshttps://doi.org/10.1007/978-1-61779-600-5_15openalex-snapshot
Lipases and Esterases from Extremophiles: Overview and Case Example of the Production and Purification of an Esterase from Thermus thermophilus HB27
inferred← citeshttps://doi.org/10.1007/978-981-19-1288-7_12openalex-snapshot
Enzymes in Flavor Development and Food Preservation
inferred← citeshttps://doi.org/10.1007/s00253-014-5775-7openalex-snapshot
A novel thermoalkalostable esterase from Acidicaldus sp. strain USBA-GBX-499 with enantioselectivity isolated from an acidic hot springs of Colombian Andes
inferred← citeshttps://doi.org/10.1007/s00449-009-0331-zopenalex-snapshot
Thermostable lipolytic enzymes production in batch and continuous cultures of Thermus thermophilus HB27
inferred← citeshttps://doi.org/10.1007/s00449-012-0686-4openalex-snapshot
Scaling-up the production of thermostable lipolytic enzymes from Thermus aquaticus YT1
inferred← citeshttps://doi.org/10.1007/s00449-012-0780-7openalex-snapshot
North Western Spain hot springs are a source of lipolytic enzyme-producing thermophilic microorganisms
inferred← citeshttps://doi.org/10.1007/s00792-009-0260-4openalex-snapshot
Carboxylic ester hydrolases from hyperthermophiles
inferred← citeshttps://doi.org/10.1007/s12257-008-0040-5openalex-snapshot
Effects of oxygen volumetric mass transfer coefficient and pH on lipase production by Staphylococcus warneri EX17
inferred← citeshttps://doi.org/10.1007/s12257-011-0481-0openalex-snapshot
Lipase activity in Thermus thermophilus HB8: Purification and characterization of the extracellular enzyme
inferred← citeshttps://doi.org/10.1016/b978-0-12-813280-7.00046-3openalex-snapshot
Food Enzymes From Extreme Environments: Sources and Bioprocessing
inferred← citeshttps://doi.org/10.1016/j.bej.2016.01.015openalex-snapshot
New sources of halophilic lipases: Isolation of bacteria from Spanish and Turkish saltworks
inferred← citeshttps://doi.org/10.1016/j.biortech.2015.03.075openalex-snapshot
Ionic liquids for the concomitant use in extremophiles lysis and extremozymes extraction
inferred← citeshttps://doi.org/10.1016/j.biortech.2017.04.128openalex-snapshot
Unravelling the suitability of biological induction for halophilic lipase production by Halomonas sp. LM1C cultures
inferred← citeshttps://doi.org/10.1016/j.biortech.2018.05.017openalex-snapshot
Demonstrating the viability of halolipase production at a mechanically stirred tank biological reactor
inferred← citeshttps://doi.org/10.1016/j.ecmx.2023.100456openalex-snapshot
Creating a new biocatalytic complex with extremolipases and biocompatible ionic liquids for improved transesterification reactions
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2006.09.006openalex-snapshot
Stimulation of novel thermostable extracellular lipolytic enzyme in cultures of Thermus sp.
inferred← citeshttps://doi.org/10.1016/j.jbiotec.2007.07.929openalex-snapshot
An approach to the scaling-up of esterases production by Thermus thermophilus HB27
inferred← citeshttps://doi.org/10.1016/j.jbiotec.2009.11.017openalex-snapshot
Heterologous expression of an esterase from Thermus thermophilus HB27 in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/j.jbiotec.2014.07.448openalex-snapshot
Genetic analysis of lipolytic activities in Thermus thermophilus HB27
inferred← citeshttps://doi.org/10.1016/j.molcatb.2011.02.017openalex-snapshot
An esterase from Thermus thermophilus HB27 with hyper-thermoalkalophilic properties: Purification, characterisation and structural modelling
inferred← citeshttps://doi.org/10.1016/j.pep.2011.04.002openalex-snapshot
Production and characterization of two N-terminal truncated esterases from Thermus thermophilus HB27 in a mesophilic yeast: Effect of N-terminus in thermal activity and stability
inferred← citeshttps://doi.org/10.1016/j.procbio.2008.08.008openalex-snapshot
Thermal spring water enhances lipolytic activity in Thermus thermophilus HB27
inferred← citeshttps://doi.org/10.1016/s0065-2164(06)61007-1openalex-snapshot
Lipases from Extremophiles and Potential for Industrial Applications
inferred← citeshttps://doi.org/10.1186/1476-511x-10-209openalex-snapshot
Strategy for improving extracellular lipolytic activities by a novel thermotolerant Staphylococcus sp. strain
inferred← citeshttps://doi.org/10.1201/9780429441837-15openalex-snapshot
Production of Food Aroma Compounds (Microbial and Enzymatic Methodologies)
inferred← citeshttps://doi.org/10.1371/journal.pone.0047665openalex-snapshot
The Metagenome-Derived Enzymes LipS and LipT Increase the Diversity of Known Lipases
inferred← citeshttps://doi.org/10.18174/11782openalex-snapshot
Biochemical and structural analysis of thermostable esterases
inferred← citeshttps://doi.org/10.2174/1874091x01004010022openalex-snapshot
Effects of Detergents on Activity, Thermostability and Aggregation of Two Alkalithermophilic Lipases from Thermosyntropha lipolytica
inferred← citeshttps://doi.org/10.3389/fbioe.2015.00148openalex-snapshot
Cold and Hot Extremozymes: Industrial Relevance and Current Trends
inferred← citeshttps://doi.org/10.3390/microorganisms10050915openalex-snapshot
Reactivity of a Recombinant Esterase from Thermus thermophilus HB27 in Aqueous and Organic Media
inferred← citeshttps://doi.org/10.5352/jls.2013.23.1.110openalex-snapshot
Culture Conditions for Improving Extracellular Lipolytic Enzyme Production by a Novel Thermophilic Geobacillus sp. AR1
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.