Osmolyte-specific counteraction of ethanol-induced aggregation and structure-function distortion of catalase
•Ethanol induces aggregation with altered structure-function integrity of catalase.•Among osmolytes only sucrose, trehalose and betaine counteracted the ethanol effects on catalase structure and aggregation.•None of the osmolytes counteracted ethanol effects on catalase activity.•Results suggest for...
Saved in:
Published in | Journal of molecular liquids Vol. 400; p. 124506 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Elsevier B.V
15.04.2024
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | •Ethanol induces aggregation with altered structure-function integrity of catalase.•Among osmolytes only sucrose, trehalose and betaine counteracted the ethanol effects on catalase structure and aggregation.•None of the osmolytes counteracted ethanol effects on catalase activity.•Results suggest for utilization of the identified osmolytes as co-formulations for industrial enzymes.
Catalase, an industrially important enzyme, was found to unfold and aggregate in presence of ethanol. Aggregation of catalase was observed in 20% and higher ethanol concentrations as evident by typical light scattering aggregation profile with complete absence of lag phase, enhanced Thioflavin T fluorescence, increased 8-anilinonaphthalene-1-sulfonic acid binding depicting enhanced hydrophobic exposure, unfolded tertiary structure with an altered Fourier transform infrared and soret spectra. To prevent ethanol-induced aggregation of catalase, osmolytes were screened for their ability to counteract the ethanol effects on catalase. Among all the osmolytes tested, only three i.e., betaine, trehalose and sucrose counteracted the ethanol-induced aggregation of catalase by about 30–50%. Results infer that addition of osmolytes to ethanol-treated catalase persuaded changes in solvent polarity and protein microenvironment leading to overall counteraction of ethanol-induced structural changes in catalase responsible for its aggregation. Fluorescence microscopy also confirmed the counteraction of ethanol-induced aggregation by osmolytes as evident from the decreased presence of aggregates in osmolyte-incubated ethanol-treated catalase. Overall, the osmolyte-induced counteraction of ethanol effects on catalase is biologically significant as it provides significant insights regarding the prevention of organic solvent induced aggregation of industrially important enzymes, being otherwise vulnerable to the solvent-induced distortion of their structure-function integrity. |
---|---|
AbstractList | •Ethanol induces aggregation with altered structure-function integrity of catalase.•Among osmolytes only sucrose, trehalose and betaine counteracted the ethanol effects on catalase structure and aggregation.•None of the osmolytes counteracted ethanol effects on catalase activity.•Results suggest for utilization of the identified osmolytes as co-formulations for industrial enzymes.
Catalase, an industrially important enzyme, was found to unfold and aggregate in presence of ethanol. Aggregation of catalase was observed in 20% and higher ethanol concentrations as evident by typical light scattering aggregation profile with complete absence of lag phase, enhanced Thioflavin T fluorescence, increased 8-anilinonaphthalene-1-sulfonic acid binding depicting enhanced hydrophobic exposure, unfolded tertiary structure with an altered Fourier transform infrared and soret spectra. To prevent ethanol-induced aggregation of catalase, osmolytes were screened for their ability to counteract the ethanol effects on catalase. Among all the osmolytes tested, only three i.e., betaine, trehalose and sucrose counteracted the ethanol-induced aggregation of catalase by about 30–50%. Results infer that addition of osmolytes to ethanol-treated catalase persuaded changes in solvent polarity and protein microenvironment leading to overall counteraction of ethanol-induced structural changes in catalase responsible for its aggregation. Fluorescence microscopy also confirmed the counteraction of ethanol-induced aggregation by osmolytes as evident from the decreased presence of aggregates in osmolyte-incubated ethanol-treated catalase. Overall, the osmolyte-induced counteraction of ethanol effects on catalase is biologically significant as it provides significant insights regarding the prevention of organic solvent induced aggregation of industrially important enzymes, being otherwise vulnerable to the solvent-induced distortion of their structure-function integrity. |
ArticleNumber | 124506 |
Author | Ali Dar, Tanveer Bashir Hajam, Ishfaq Manzoor, Usma |
Author_xml | – sequence: 1 givenname: Usma surname: Manzoor fullname: Manzoor, Usma – sequence: 2 givenname: Ishfaq surname: Bashir Hajam fullname: Bashir Hajam, Ishfaq – sequence: 3 givenname: Tanveer surname: Ali Dar fullname: Ali Dar, Tanveer email: tanveerali@kashmiruniversity.ac.in |
BookMark | eNp9kMtOwzAQRS1UJNrCH7DIDyT4maQbJFTxkip1A2vLscfFVWoX20Hq35MS2LKaxZ1zNXMWaOaDB4RuCa4IJvXdvjqEvnefFcWUV4RygesLNCdtw0pG6nqG5uNaUzaM0iu0SGmPMRaixXPUb9PInjKU6QjaWacLHQafISqdXfBFsAXkD-VDXzpvBg2mULtdhJ36iZU3Rcpx0HmIUNrBT5RxKYf4V6BVVr1KcI0ureoT3PzOJXp_enxbv5Sb7fPr-mFTaipELhusiG14ww1Z4a5rwJqO2s4CZVpw0q5sR1rGNVNGCSYI562usW0FaQAT3rEl4lOvjiGlCFYeozuoeJIEy7MxuZeTMXk2JidjI3Y_YTDe9uUgyqQd-PFlF0FnaYL7v-AbM517gA |
Cites_doi | 10.1111/febs.16312 10.1021/acs.jpcb.6b10119 10.1016/j.ijbiomac.2021.04.060 10.1073/pnas.0606236103 10.18388/abp.2012_2158 10.1016/j.foodchem.2017.04.022 10.2174/0929866511009011542 10.1097/00004872-200306000-00009 10.1021/bi050281t 10.1002/adem.202101797 10.1016/j.ijbiomac.2017.11.096 10.1039/D0MA00760A 10.1016/j.jphotobiol.2013.08.006 10.3109/10242422.2011.635301 10.1016/S0268-005X(01)00080-7 10.1002/(SICI)1097-0282(199906)49:7<635::AID-BIP8>3.0.CO;2-8 10.1186/1471-2105-8-65 10.1038/nbt1096-1283 10.1007/s00592-022-01949-1 10.1159/000045897 10.1016/j.crfs.2022.08.012 10.1529/biophysj.104.051797 10.1016/B978-0-12-813280-7.00005-0 10.1021/acsomega.2c06199 10.18433/jpps30572 10.1080/15592324.2021.1913306 10.1016/j.foodhyd.2022.107985 10.1007/BF02893047 10.1039/D2TB02605H 10.1021/acsbiomaterials.3c00763 10.1016/j.abb.2006.08.014 10.1021/bi001782b 10.1016/j.aca.2020.03.038 10.1021/acs.biochem.6b00403 10.1016/S0076-6879(84)05016-3 10.1016/j.bcab.2018.07.035 10.1021/jf801383m 10.1016/j.btre.2018.e00258 10.1098/rsfs.2017.0030 10.1021/acs.jpcb.5b04931 10.1038/s41598-020-60430-7 10.3748/wjg.v20.i40.14672 10.1007/978-1-61779-927-3_16 10.1016/j.ijbiomac.2022.04.013 10.1016/j.foodhyd.2020.106379 10.1007/s00249-021-01502-y 10.1074/jbc.M212540200 10.1021/ja0400685 |
ContentType | Journal Article |
Copyright | 2024 Elsevier B.V. |
Copyright_xml | – notice: 2024 Elsevier B.V. |
DBID | AAYXX CITATION |
DOI | 10.1016/j.molliq.2024.124506 |
DatabaseName | CrossRef |
DatabaseTitle | CrossRef |
DatabaseTitleList | |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Chemistry Physics |
EISSN | 1873-3166 |
ExternalDocumentID | 10_1016_j_molliq_2024_124506 S0167732224005622 |
GroupedDBID | --K --M -~X .~1 0R~ 1B1 1RT 1~. 1~5 4.4 457 4G. 53G 5GY 5VS 7-5 71M 8P~ 9JN AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AARLI AAXUO ABJNI ABMAC ABNEU ACDAQ ACFVG ACGFS ACRLP ADBBV ADECG ADEZE AEBSH AEKER AENEX AFKWA AFTJW AFZHZ AGHFR AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AIVDX AJOXV AJSZI AKRWK ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ AXJTR BKOJK BLXMC CS3 DU5 EBS EFJIC EO8 EO9 EP2 EP3 F5P FDB FIRID FLBIZ FNPLU FYGXN G-Q GBLVA IHE J1W KOM M36 M41 MO0 N9A O-L O9- OAUVE OGIMB OZT P-8 P-9 P2P PC. Q38 RIG RNS ROL RPZ SDF SDG SES SEW SPC SPCBC SSK SSQ SSZ T5K TN5 YK3 ZMT ~G- 29L AAQXK AAXKI AAYXX ABEFU ABFNM ABXDB ACNNM ADMUD AFFNX AFJKZ AJQLL ASPBG AVWKF AZFZN CITATION EJD FEDTE FGOYB HMU HVGLF HZ~ R2- SCB SCH WUQ XPP |
ID | FETCH-LOGICAL-c255t-70a1f7474d190bb7efdb2fbfe23c54189fb1834c3ada5351448c60f8517e014b3 |
IEDL.DBID | AIKHN |
ISSN | 0167-7322 |
IngestDate | Thu Sep 26 21:09:20 EDT 2024 Sat Jul 20 16:35:57 EDT 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Keywords | Solvent polarity Organic solvent Trehalose Betaine Protein unfolding |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c255t-70a1f7474d190bb7efdb2fbfe23c54189fb1834c3ada5351448c60f8517e014b3 |
ParticipantIDs | crossref_primary_10_1016_j_molliq_2024_124506 elsevier_sciencedirect_doi_10_1016_j_molliq_2024_124506 |
PublicationCentury | 2000 |
PublicationDate | 2024-04-15 |
PublicationDateYYYYMMDD | 2024-04-15 |
PublicationDate_xml | – month: 04 year: 2024 text: 2024-04-15 day: 15 |
PublicationDecade | 2020 |
PublicationTitle | Journal of molecular liquids |
PublicationYear | 2024 |
Publisher | Elsevier B.V |
Publisher_xml | – name: Elsevier B.V |
References | Wilcox, Blanch, Doig (b0155) 2016; 55 Li (b0035) 2022; 59 Singh (b0195) 2010; 78 Sethuraman, Belfort (b0130) 2005; 88 Farrell (b0175) 2001; 15 Mojtabavi, Samadi, Faramarzi (b0265) 2019; 18 Das, Vasudevan (b0070) 2005; 20 Ghosh (b0075) 2021; 16 Mousavi (b0230) 2008; 56 Nikolaidis, Andreadis, Moschakis (b0055) 2017; 232 Ali (b0255) 2022; 209 Conchillo-Solé (b0110) 2007; 8 Fatima (b0245) 2006; 454 Sharma, Pathak, Chattopadhyay (b0090) 2013; 3 Yang (b0140) 2013; 128 Abada (b0010) 2019; Elsevier Banik (b0235) 2015; 119 Kaushal (b0005) 2018; 16 Dudkaitė, Kairys, Bagdžiūnas (b0025) 2023; 11 Saito (b0040) 2003; 21 Handler, Kwon (b0085) 2001; 87 Derenne (b0150) 2020; 1112 Feng (b0045) 2021; 111 Zeeshan, Tabbassum, Kesharwani (b0170) 2019; 38 Sarkar (b0080) 2023; 9 Rehm (b0030) 2011; 34 De Meutter, Goormaghtigh (b0145) 2021; 50 Andreadis, Moschakis (b0050) 2023; 134 Khurana (b0185) 2001; 40 Natalello, Ami, Doglia (b0180) 2012 Soares (b0015) 2011; 29 Housmans (b0215) 2023; 290 Kant Yadav, Pande Prajakt, Bala Chauhan (b0105) 2010; 17 Le Dare, Gicquel (b0065) 2019; 22 Singh (b0240) 2010; 78 Rajan (b0120) 2021; 2 Bhat (b0115) 2021; 182 Balabushevich (b0020) 2022; 24 Dzwolak (b0200) 2005; 44 Dutta, Roy, Sengupta (b0190) 2022; 7 Aebi (b0280) 1984 Ahmad, Mishra (b0100) 2022; 1870 Zapadka (b0135) 2017; 7 Street, Bolen, Rose (b0250) 2006; 103 Szymańska, Hornowski, Ślósarek (b0205) 2012; 59 Panuszko (b0270) 2016; 120 Feng (b0275) 2022; 5 Speed, Wang, King (b0125) 1996; 14 Brauner, Flach, Mendelsohn (b0160) 2005; 127 Varma (b0220) 2018; 109 Dwyer (b0225) 1999; 49 Kim (b0210) 2003; 278 Bhat, Singh, Dar (b0260) 2020; 10 Liu (b0060) 2014; 20 Suprasanna, Nikalje, Rai (b0095) 2016 Kaushal, Singh, Arya (b0165) 2018; 18 Feng (10.1016/j.molliq.2024.124506_b0045) 2021; 111 Wilcox (10.1016/j.molliq.2024.124506_b0155) 2016; 55 Housmans (10.1016/j.molliq.2024.124506_b0215) 2023; 290 Balabushevich (10.1016/j.molliq.2024.124506_b0020) 2022; 24 Rehm (10.1016/j.molliq.2024.124506_b0030) 2011; 34 Kaushal (10.1016/j.molliq.2024.124506_b0005) 2018; 16 Dudkaitė (10.1016/j.molliq.2024.124506_b0025) 2023; 11 Sarkar (10.1016/j.molliq.2024.124506_b0080) 2023; 9 Nikolaidis (10.1016/j.molliq.2024.124506_b0055) 2017; 232 Zeeshan (10.1016/j.molliq.2024.124506_b0170) 2019; 38 Varma (10.1016/j.molliq.2024.124506_b0220) 2018; 109 Singh (10.1016/j.molliq.2024.124506_b0240) 2010; 78 Suprasanna (10.1016/j.molliq.2024.124506_b0095) 2016 Dwyer (10.1016/j.molliq.2024.124506_b0225) 1999; 49 Ahmad (10.1016/j.molliq.2024.124506_b0100) 2022; 1870 Speed (10.1016/j.molliq.2024.124506_b0125) 1996; 14 Kaushal (10.1016/j.molliq.2024.124506_b0165) 2018; 18 Soares (10.1016/j.molliq.2024.124506_b0015) 2011; 29 Panuszko (10.1016/j.molliq.2024.124506_b0270) 2016; 120 Sethuraman (10.1016/j.molliq.2024.124506_b0130) 2005; 88 Ali (10.1016/j.molliq.2024.124506_b0255) 2022; 209 Street (10.1016/j.molliq.2024.124506_b0250) 2006; 103 Fatima (10.1016/j.molliq.2024.124506_b0245) 2006; 454 Das (10.1016/j.molliq.2024.124506_b0070) 2005; 20 Saito (10.1016/j.molliq.2024.124506_b0040) 2003; 21 Zapadka (10.1016/j.molliq.2024.124506_b0135) 2017; 7 De Meutter (10.1016/j.molliq.2024.124506_b0145) 2021; 50 Brauner (10.1016/j.molliq.2024.124506_b0160) 2005; 127 Farrell (10.1016/j.molliq.2024.124506_b0175) 2001; 15 Le Dare (10.1016/j.molliq.2024.124506_b0065) 2019; 22 Derenne (10.1016/j.molliq.2024.124506_b0150) 2020; 1112 Kim (10.1016/j.molliq.2024.124506_b0210) 2003; 278 Mojtabavi (10.1016/j.molliq.2024.124506_b0265) 2019; 18 Andreadis (10.1016/j.molliq.2024.124506_b0050) 2023; 134 Rajan (10.1016/j.molliq.2024.124506_b0120) 2021; 2 Natalello (10.1016/j.molliq.2024.124506_b0180) 2012 Feng (10.1016/j.molliq.2024.124506_b0275) 2022; 5 Bhat (10.1016/j.molliq.2024.124506_b0260) 2020; 10 Yang (10.1016/j.molliq.2024.124506_b0140) 2013; 128 Abada (10.1016/j.molliq.2024.124506_b0010) 2019; Elsevier Mousavi (10.1016/j.molliq.2024.124506_b0230) 2008; 56 Dzwolak (10.1016/j.molliq.2024.124506_b0200) 2005; 44 Sharma (10.1016/j.molliq.2024.124506_b0090) 2013; 3 Bhat (10.1016/j.molliq.2024.124506_b0115) 2021; 182 Szymańska (10.1016/j.molliq.2024.124506_b0205) 2012; 59 Dutta (10.1016/j.molliq.2024.124506_b0190) 2022; 7 Ghosh (10.1016/j.molliq.2024.124506_b0075) 2021; 16 Li (10.1016/j.molliq.2024.124506_b0035) 2022; 59 Handler (10.1016/j.molliq.2024.124506_b0085) 2001; 87 Kant Yadav (10.1016/j.molliq.2024.124506_b0105) 2010; 17 Singh (10.1016/j.molliq.2024.124506_b0195) 2010; 78 Khurana (10.1016/j.molliq.2024.124506_b0185) 2001; 40 Conchillo-Solé (10.1016/j.molliq.2024.124506_b0110) 2007; 8 Liu (10.1016/j.molliq.2024.124506_b0060) 2014; 20 Banik (10.1016/j.molliq.2024.124506_b0235) 2015; 119 Aebi (10.1016/j.molliq.2024.124506_b0280) 1984 |
References_xml | – volume: 18 start-page: e00258 year: 2018 ident: b0165 article-title: Immobilization of catalase onto chitosan and chitosan–bentonite complex: a comparative study publication-title: Biotechnol. Rep, contributor: fullname: Arya – volume: 5 start-page: 1386 year: 2022 end-page: 1394 ident: b0275 article-title: Structural changes and exposed amino acids of ethanol-modified whey proteins isolates promote its antioxidant potential publication-title: Current Research in Food Science contributor: fullname: Feng – volume: 182 start-page: 921 year: 2021 end-page: 930 ident: b0115 article-title: Trimethylamine N-oxide alters structure-function integrity of β-casein: structural disorder co-regulates the aggregation propensity and chaperone activity publication-title: Int. J. Biol. Macromol. contributor: fullname: Bhat – volume: 1112 start-page: 62 year: 2020 end-page: 71 ident: b0150 article-title: FTIR spectroscopy as an analytical tool to compare glycosylation in therapeutic monoclonal antibodies publication-title: Anal. Chim. Acta contributor: fullname: Derenne – start-page: 1 year: 2016 end-page: 12 ident: b0095 article-title: Osmolyte accumulation and implications in plant abiotic stress tolerance publication-title: Osmolytes and Plants Acclimation to Changing Environment: Emerging Omics Technologies contributor: fullname: Rai – volume: 128 start-page: 35 year: 2013 end-page: 42 ident: b0140 article-title: Binding of chrysoidine to catalase: spectroscopy, isothermal titration calorimetry and molecular docking studies publication-title: Journal of Photochemistry Photobiology b: Biology contributor: fullname: Yang – volume: 10 start-page: 3503 year: 2020 ident: b0260 article-title: Taurine induces an ordered but functionally inactive conformation in intrinsically disordered casein proteins publication-title: Sci. Rep. contributor: fullname: Dar – volume: 120 start-page: 11159 year: 2016 end-page: 11169 ident: b0270 article-title: General mechanism of osmolytes’ influence on protein stability irrespective of the type of osmolyte cosolvent publication-title: J. Phys. Chem. B contributor: fullname: Panuszko – volume: 14 start-page: 1283 year: 1996 end-page: 1287 ident: b0125 article-title: Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition publication-title: Nat. Biotechnol. contributor: fullname: King – volume: 55 start-page: 3794 year: 2016 end-page: 3802 ident: b0155 article-title: Determination of protein secondary structure from infrared spectra using partial least-squares regression publication-title: Biochemistry contributor: fullname: Doig – volume: 59 start-page: 1531 year: 2022 end-page: 1537 ident: b0035 article-title: Liver enzymes, alcohol consumption and the risk of diabetes: the Suita study publication-title: Acta Diabetol. contributor: fullname: Li – volume: 1870 year: 2022 ident: b0100 article-title: Polyol and sugar osmolytes stabilize the molten globule state of α-lactalbumin and inhibit amyloid fibril formation publication-title: Biochimica Et Biophysica Acta -Proteins contributor: fullname: Mishra – volume: 88 start-page: 1322 year: 2005 end-page: 1333 ident: b0130 article-title: Protein structural perturbation and aggregation on homogeneous surfaces publication-title: Biophys. J. contributor: fullname: Belfort – volume: 59 year: 2012 ident: b0205 article-title: Denaturation and aggregation of lysozyme in water-ethanol solution publication-title: Acta Biochim. Pol. contributor: fullname: Ślósarek – volume: 7 start-page: 44556 year: 2022 end-page: 44572 ident: b0190 article-title: Effects of external perturbations on protein systems: a microscopic view publication-title: ACS Omega contributor: fullname: Sengupta – volume: 278 start-page: 10842 year: 2003 end-page: 10850 ident: b0210 article-title: Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation publication-title: J. Biol. Chem. contributor: fullname: Kim – volume: 44 start-page: 8948 year: 2005 end-page: 8958 ident: b0200 article-title: Ethanol-perturbed amyloidogenic self-assembly of insulin: looking for origins of amyloid strains publication-title: Biochemistry contributor: fullname: Dzwolak – volume: 20 start-page: 14672 year: 2014 ident: b0060 article-title: Ethanol and liver: recent insights into the mechanisms of ethanol-induced fatty liver publication-title: World J Gastroenterol: WJG contributor: fullname: Liu – volume: 87 start-page: 106 year: 2001 end-page: 110 ident: b0085 article-title: Cell and molecular biology of organic osmolyte accumulation in hypertonic renal cells publication-title: Nephron contributor: fullname: Kwon – volume: 290 start-page: 554 year: 2023 end-page: 583 ident: b0215 article-title: A guide to studying protein aggregation publication-title: FEBS J. contributor: fullname: Housmans – volume: 22 start-page: 525 year: 2019 end-page: 535 ident: b0065 article-title: Therapeutic applications of ethanol: a review publication-title: J. Pharm. Pharm. Sci. contributor: fullname: Gicquel – volume: 232 start-page: 425 year: 2017 end-page: 433 ident: b0055 article-title: Effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra publication-title: Food Chem. contributor: fullname: Moschakis – volume: 8 start-page: 1 year: 2007 end-page: 17 ident: b0110 article-title: AGGRESCAN: a server for the prediction and evaluation of“ hot spots” of aggregation in polypeptides publication-title: BMC Bioinf. contributor: fullname: Conchillo-Solé – volume: 50 start-page: 613 year: 2021 end-page: 628 ident: b0145 article-title: Evaluation of protein secondary structure from FTIR spectra improved after partial deuteration publication-title: Eur. Biophys. J. contributor: fullname: Goormaghtigh – volume: 40 start-page: 3525 year: 2001 end-page: 3535 ident: b0185 article-title: Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates publication-title: Biochemistry contributor: fullname: Khurana – volume: 209 start-page: 198 year: 2022 end-page: 210 ident: b0255 article-title: Effect of polyol osmolytes on the structure-function integrity and aggregation propensity of catalase: a comprehensive study based on spectroscopic and molecular dynamic simulation measurements publication-title: Int. J. Biol. Macromol. contributor: fullname: Ali – volume: 454 start-page: 170 year: 2006 end-page: 180 ident: b0245 article-title: Fluoroalcohols induced unfolding of succinylated con a: native like β-structure in partially folded intermediate and α-helix in molten globule like state publication-title: Arch. Biochem. contributor: fullname: Fatima – volume: 9 start-page: 5639 year: 2023 end-page: 5652 ident: b0080 article-title: Osmolytes as cryoprotectants under salt stress publication-title: ACS Biomaterials Science Engineering contributor: fullname: Sarkar – start-page: 121 year: 1984 end-page: 126 ident: b0280 article-title: Catalase in vitro publication-title: Methods in Enzymology contributor: fullname: Aebi – volume: 21 start-page: 1097 year: 2003 end-page: 1105 ident: b0040 article-title: Do the ethanol metabolizing enzymes modify the relationship between alcohol consumption and blood pressure? publication-title: J. Hypertens. contributor: fullname: Saito – volume: 49 start-page: 635 year: 1999 end-page: 645 ident: b0225 article-title: Molecular simulation of the effects of alcohols on peptide structure publication-title: Biopolymers: Original Research on Biomolecules contributor: fullname: Dwyer – volume: 18 start-page: 13 year: 2019 ident: b0265 article-title: Osmolyte-induced folding and stability of proteins: concepts and characterization publication-title: Iranian Journal of Pharmaceutical Research contributor: fullname: Faramarzi – volume: 17 start-page: 1542 year: 2010 end-page: 1546 ident: b0105 article-title: Counter effect of sucrose on ethanol-induced aggregation of protein publication-title: Protein Peptide Letters contributor: fullname: Bala Chauhan – volume: 56 start-page: 8680 year: 2008 end-page: 8684 ident: b0230 article-title: Ethanol effect on the structure of β-lactoglobulin b and its ligand binding publication-title: Journal of Agricultural Food Chemistry contributor: fullname: Mousavi – volume: 11 start-page: 2409 year: 2023 end-page: 2416 ident: b0025 article-title: Understanding the activity of glucose oxidase after exposure to organic solvents publication-title: J. Mater. Chem. B contributor: fullname: Bagdžiūnas – volume: 16 start-page: 1913306 year: 2021 ident: b0075 article-title: Understanding the roles of osmolytes for acclimatizing plants to changing environment: a review of potential mechanism publication-title: Plant Signaling Behavior contributor: fullname: Ghosh – volume: 127 start-page: 100 year: 2005 end-page: 109 ident: b0160 article-title: A quantitative reconstruction of the amide I contour in the IR spectra of globular proteins: from structure to spectrum publication-title: J. Am. Chem. Soc. contributor: fullname: Mendelsohn – volume: Elsevier start-page: 61 year: 2019 end-page: 72 ident: b0010 article-title: Application of microbial enzymes in the dairy industry publication-title: Enzymes in Food Biotechnology. contributor: fullname: Abada – volume: 24 start-page: 2101797 year: 2022 ident: b0020 article-title: Immobilization of antioxidant enzyme catalase on porous hybrid Microparticles of vaterite with mucin publication-title: Adv. Eng. Mater. contributor: fullname: Balabushevich – volume: 20 start-page: 80 year: 2005 end-page: 84 ident: b0070 article-title: Effect of ethanol on liver antioxidant defense systems: adose dependent study publication-title: Indian J. Clin. Biochem. contributor: fullname: Vasudevan – volume: 7 start-page: 20170030 year: 2017 ident: b0135 article-title: Factors affecting the physical stability (aggregation) of peptide therapeutics publication-title: Interface Focus contributor: fullname: Zapadka – volume: 78 start-page: 2625 year: 2010 end-page: 2637 ident: b0195 article-title: Role of partial protein unfolding in alcohol-induced protein aggregation. proteins: structure, function publication-title: Bioinformatics contributor: fullname: Singh – volume: 38 start-page: 551 year: 2019 end-page: 564 ident: b0170 publication-title: Investigation on Secondary Structure Alterations of Protein Drugs as an Indicator of Their Biological Activity upon Thermal Exposure. contributor: fullname: Kesharwani – volume: 34 start-page: 135 year: 2011 ident: b0030 article-title: The risks associated with alcohol use and alcoholism publication-title: Alcohol Research Health contributor: fullname: Rehm – volume: 78 start-page: 2625 year: 2010 end-page: 2637 ident: b0240 publication-title: Role of Partial Protein Unfolding in Alcohol-Induced Protein Aggregation. contributor: fullname: Singh – volume: 134 year: 2023 ident: b0050 article-title: Effect of ethanol on gelation and microstructure of whey protein gels in the presence of NaCl publication-title: Food Hydrocoll. contributor: fullname: Moschakis – volume: 2 start-page: 1139 year: 2021 end-page: 1176 ident: b0120 article-title: Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials publication-title: Materials Advances contributor: fullname: Rajan – volume: 3 year: 2013 ident: b0090 article-title: Osmolyte induced stabilization of protein molecules: a brief review. journal of proteins publication-title: Proteomics contributor: fullname: Chattopadhyay – volume: 111 year: 2021 ident: b0045 article-title: Ethanol induced changes in structural, morphological, and functional properties of whey proteins isolates: influence of ethanol concentration publication-title: Food Hydrocoll. contributor: fullname: Feng – volume: 109 start-page: 1108 year: 2018 end-page: 1114 ident: b0220 article-title: Structural perturbation by arsenic triggers the aggregation of hen egg white lysozyme by promoting oligomers formation publication-title: Int. J. Biol. Macromol. contributor: fullname: Varma – volume: 29 start-page: 223 year: 2011 end-page: 237 ident: b0015 article-title: Application of immobilized enzyme technologies for the textile industry: a review publication-title: Biocatalysis Biotransformation contributor: fullname: Soares – volume: 15 start-page: 341 year: 2001 end-page: 354 ident: b0175 article-title: Secondary structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization publication-title: Food Hydrocoll. contributor: fullname: Farrell – volume: 16 start-page: 192 year: 2018 end-page: 199 ident: b0005 article-title: Catalase enzyme: application in bioremediation and food industry publication-title: Biocatalysis Agricultural Biotechnology contributor: fullname: Kaushal – start-page: 229 year: 2012 end-page: 244 ident: b0180 article-title: Fourier transform infrared spectroscopy of intrinsically disordered proteins: measurement procedures and data analyses publication-title: Intrinsically Disordered Protein Analysis: Volume 1, Methods Experimental Tools contributor: fullname: Doglia – volume: 103 start-page: 13997 year: 2006 end-page: 14002 ident: b0250 article-title: A molecular mechanism for osmolyte-induced protein stability publication-title: Proc. Natl. Acad. Sci. contributor: fullname: Rose – volume: 119 start-page: 9905 year: 2015 end-page: 9919 ident: b0235 article-title: Picosecond solvation and rotational dynamics: an attempt to reinvestigate the mystery of alcohol–water binary mixtures publication-title: J. Phys. Chem. B contributor: fullname: Banik – volume: 290 start-page: 554 issue: 3 year: 2023 ident: 10.1016/j.molliq.2024.124506_b0215 article-title: A guide to studying protein aggregation publication-title: FEBS J. doi: 10.1111/febs.16312 contributor: fullname: Housmans – volume: 120 start-page: 11159 issue: 43 year: 2016 ident: 10.1016/j.molliq.2024.124506_b0270 article-title: General mechanism of osmolytes’ influence on protein stability irrespective of the type of osmolyte cosolvent publication-title: J. Phys. Chem. B doi: 10.1021/acs.jpcb.6b10119 contributor: fullname: Panuszko – volume: 182 start-page: 921 year: 2021 ident: 10.1016/j.molliq.2024.124506_b0115 article-title: Trimethylamine N-oxide alters structure-function integrity of β-casein: structural disorder co-regulates the aggregation propensity and chaperone activity publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2021.04.060 contributor: fullname: Bhat – volume: 103 start-page: 13997 issue: 38 year: 2006 ident: 10.1016/j.molliq.2024.124506_b0250 article-title: A molecular mechanism for osmolyte-induced protein stability publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.0606236103 contributor: fullname: Street – volume: 59 issue: 2 year: 2012 ident: 10.1016/j.molliq.2024.124506_b0205 article-title: Denaturation and aggregation of lysozyme in water-ethanol solution publication-title: Acta Biochim. Pol. doi: 10.18388/abp.2012_2158 contributor: fullname: Szymańska – volume: 232 start-page: 425 year: 2017 ident: 10.1016/j.molliq.2024.124506_b0055 article-title: Effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra publication-title: Food Chem. doi: 10.1016/j.foodchem.2017.04.022 contributor: fullname: Nikolaidis – volume: 17 start-page: 1542 issue: 12 year: 2010 ident: 10.1016/j.molliq.2024.124506_b0105 article-title: Counter effect of sucrose on ethanol-induced aggregation of protein publication-title: Protein Peptide Letters doi: 10.2174/0929866511009011542 contributor: fullname: Kant Yadav – volume: 21 start-page: 1097 issue: 6 year: 2003 ident: 10.1016/j.molliq.2024.124506_b0040 article-title: Do the ethanol metabolizing enzymes modify the relationship between alcohol consumption and blood pressure? publication-title: J. Hypertens. doi: 10.1097/00004872-200306000-00009 contributor: fullname: Saito – volume: 44 start-page: 8948 issue: 25 year: 2005 ident: 10.1016/j.molliq.2024.124506_b0200 article-title: Ethanol-perturbed amyloidogenic self-assembly of insulin: looking for origins of amyloid strains publication-title: Biochemistry doi: 10.1021/bi050281t contributor: fullname: Dzwolak – volume: 24 start-page: 2101797 issue: 9 year: 2022 ident: 10.1016/j.molliq.2024.124506_b0020 article-title: Immobilization of antioxidant enzyme catalase on porous hybrid Microparticles of vaterite with mucin publication-title: Adv. Eng. Mater. doi: 10.1002/adem.202101797 contributor: fullname: Balabushevich – volume: 109 start-page: 1108 year: 2018 ident: 10.1016/j.molliq.2024.124506_b0220 article-title: Structural perturbation by arsenic triggers the aggregation of hen egg white lysozyme by promoting oligomers formation publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2017.11.096 contributor: fullname: Varma – volume: 2 start-page: 1139 issue: 4 year: 2021 ident: 10.1016/j.molliq.2024.124506_b0120 article-title: Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials publication-title: Materials Advances doi: 10.1039/D0MA00760A contributor: fullname: Rajan – volume: 128 start-page: 35 year: 2013 ident: 10.1016/j.molliq.2024.124506_b0140 article-title: Binding of chrysoidine to catalase: spectroscopy, isothermal titration calorimetry and molecular docking studies publication-title: Journal of Photochemistry Photobiology b: Biology doi: 10.1016/j.jphotobiol.2013.08.006 contributor: fullname: Yang – volume: 29 start-page: 223 issue: 6 year: 2011 ident: 10.1016/j.molliq.2024.124506_b0015 article-title: Application of immobilized enzyme technologies for the textile industry: a review publication-title: Biocatalysis Biotransformation doi: 10.3109/10242422.2011.635301 contributor: fullname: Soares – volume: 15 start-page: 341 issue: 4–6 year: 2001 ident: 10.1016/j.molliq.2024.124506_b0175 article-title: Secondary structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization publication-title: Food Hydrocoll. doi: 10.1016/S0268-005X(01)00080-7 contributor: fullname: Farrell – volume: 49 start-page: 635 issue: 7 year: 1999 ident: 10.1016/j.molliq.2024.124506_b0225 article-title: Molecular simulation of the effects of alcohols on peptide structure publication-title: Biopolymers: Original Research on Biomolecules doi: 10.1002/(SICI)1097-0282(199906)49:7<635::AID-BIP8>3.0.CO;2-8 contributor: fullname: Dwyer – volume: 1870 issue: 11–12 year: 2022 ident: 10.1016/j.molliq.2024.124506_b0100 article-title: Polyol and sugar osmolytes stabilize the molten globule state of α-lactalbumin and inhibit amyloid fibril formation publication-title: Biochimica Et Biophysica Acta -Proteins contributor: fullname: Ahmad – volume: 8 start-page: 1 year: 2007 ident: 10.1016/j.molliq.2024.124506_b0110 article-title: AGGRESCAN: a server for the prediction and evaluation of“ hot spots” of aggregation in polypeptides publication-title: BMC Bioinf. doi: 10.1186/1471-2105-8-65 contributor: fullname: Conchillo-Solé – volume: 14 start-page: 1283 issue: 10 year: 1996 ident: 10.1016/j.molliq.2024.124506_b0125 article-title: Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition publication-title: Nat. Biotechnol. doi: 10.1038/nbt1096-1283 contributor: fullname: Speed – volume: 59 start-page: 1531 issue: 12 year: 2022 ident: 10.1016/j.molliq.2024.124506_b0035 article-title: Liver enzymes, alcohol consumption and the risk of diabetes: the Suita study publication-title: Acta Diabetol. doi: 10.1007/s00592-022-01949-1 contributor: fullname: Li – volume: 87 start-page: 106 issue: 2 year: 2001 ident: 10.1016/j.molliq.2024.124506_b0085 article-title: Cell and molecular biology of organic osmolyte accumulation in hypertonic renal cells publication-title: Nephron doi: 10.1159/000045897 contributor: fullname: Handler – volume: 5 start-page: 1386 year: 2022 ident: 10.1016/j.molliq.2024.124506_b0275 article-title: Structural changes and exposed amino acids of ethanol-modified whey proteins isolates promote its antioxidant potential publication-title: Current Research in Food Science doi: 10.1016/j.crfs.2022.08.012 contributor: fullname: Feng – volume: 88 start-page: 1322 issue: 2 year: 2005 ident: 10.1016/j.molliq.2024.124506_b0130 article-title: Protein structural perturbation and aggregation on homogeneous surfaces publication-title: Biophys. J. doi: 10.1529/biophysj.104.051797 contributor: fullname: Sethuraman – volume: Elsevier start-page: 61 year: 2019 ident: 10.1016/j.molliq.2024.124506_b0010 article-title: Application of microbial enzymes in the dairy industry publication-title: Enzymes in Food Biotechnology. doi: 10.1016/B978-0-12-813280-7.00005-0 contributor: fullname: Abada – start-page: 1 year: 2016 ident: 10.1016/j.molliq.2024.124506_b0095 article-title: Osmolyte accumulation and implications in plant abiotic stress tolerance contributor: fullname: Suprasanna – volume: 18 start-page: 13 issue: Suppl1 year: 2019 ident: 10.1016/j.molliq.2024.124506_b0265 article-title: Osmolyte-induced folding and stability of proteins: concepts and characterization publication-title: Iranian Journal of Pharmaceutical Research contributor: fullname: Mojtabavi – volume: 7 start-page: 44556 issue: 49 year: 2022 ident: 10.1016/j.molliq.2024.124506_b0190 article-title: Effects of external perturbations on protein systems: a microscopic view publication-title: ACS Omega doi: 10.1021/acsomega.2c06199 contributor: fullname: Dutta – volume: 22 start-page: 525 year: 2019 ident: 10.1016/j.molliq.2024.124506_b0065 article-title: Therapeutic applications of ethanol: a review publication-title: J. Pharm. Pharm. Sci. doi: 10.18433/jpps30572 contributor: fullname: Le Dare – volume: 78 start-page: 2625 issue: 12 year: 2010 ident: 10.1016/j.molliq.2024.124506_b0195 article-title: Role of partial protein unfolding in alcohol-induced protein aggregation. proteins: structure, function publication-title: Bioinformatics contributor: fullname: Singh – volume: 16 start-page: 1913306 issue: 8 year: 2021 ident: 10.1016/j.molliq.2024.124506_b0075 article-title: Understanding the roles of osmolytes for acclimatizing plants to changing environment: a review of potential mechanism publication-title: Plant Signaling Behavior doi: 10.1080/15592324.2021.1913306 contributor: fullname: Ghosh – volume: 134 year: 2023 ident: 10.1016/j.molliq.2024.124506_b0050 article-title: Effect of ethanol on gelation and microstructure of whey protein gels in the presence of NaCl publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2022.107985 contributor: fullname: Andreadis – volume: 20 start-page: 80 year: 2005 ident: 10.1016/j.molliq.2024.124506_b0070 article-title: Effect of ethanol on liver antioxidant defense systems: adose dependent study publication-title: Indian J. Clin. Biochem. doi: 10.1007/BF02893047 contributor: fullname: Das – volume: 34 start-page: 135 issue: 2 year: 2011 ident: 10.1016/j.molliq.2024.124506_b0030 article-title: The risks associated with alcohol use and alcoholism publication-title: Alcohol Research Health contributor: fullname: Rehm – volume: 11 start-page: 2409 issue: 11 year: 2023 ident: 10.1016/j.molliq.2024.124506_b0025 article-title: Understanding the activity of glucose oxidase after exposure to organic solvents publication-title: J. Mater. Chem. B doi: 10.1039/D2TB02605H contributor: fullname: Dudkaitė – volume: 9 start-page: 5639 issue: 10 year: 2023 ident: 10.1016/j.molliq.2024.124506_b0080 article-title: Osmolytes as cryoprotectants under salt stress publication-title: ACS Biomaterials Science Engineering doi: 10.1021/acsbiomaterials.3c00763 contributor: fullname: Sarkar – volume: 454 start-page: 170 issue: 2 year: 2006 ident: 10.1016/j.molliq.2024.124506_b0245 article-title: Fluoroalcohols induced unfolding of succinylated con a: native like β-structure in partially folded intermediate and α-helix in molten globule like state publication-title: Arch. Biochem. doi: 10.1016/j.abb.2006.08.014 contributor: fullname: Fatima – volume: 3 issue: 2 year: 2013 ident: 10.1016/j.molliq.2024.124506_b0090 article-title: Osmolyte induced stabilization of protein molecules: a brief review. journal of proteins publication-title: Proteomics contributor: fullname: Sharma – volume: 40 start-page: 3525 issue: 12 year: 2001 ident: 10.1016/j.molliq.2024.124506_b0185 article-title: Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates publication-title: Biochemistry doi: 10.1021/bi001782b contributor: fullname: Khurana – volume: 38 start-page: 551 year: 2019 ident: 10.1016/j.molliq.2024.124506_b0170 publication-title: Investigation on Secondary Structure Alterations of Protein Drugs as an Indicator of Their Biological Activity upon Thermal Exposure. contributor: fullname: Zeeshan – volume: 1112 start-page: 62 year: 2020 ident: 10.1016/j.molliq.2024.124506_b0150 article-title: FTIR spectroscopy as an analytical tool to compare glycosylation in therapeutic monoclonal antibodies publication-title: Anal. Chim. Acta doi: 10.1016/j.aca.2020.03.038 contributor: fullname: Derenne – volume: 55 start-page: 3794 issue: 27 year: 2016 ident: 10.1016/j.molliq.2024.124506_b0155 article-title: Determination of protein secondary structure from infrared spectra using partial least-squares regression publication-title: Biochemistry doi: 10.1021/acs.biochem.6b00403 contributor: fullname: Wilcox – start-page: 121 year: 1984 ident: 10.1016/j.molliq.2024.124506_b0280 article-title: Catalase in vitro doi: 10.1016/S0076-6879(84)05016-3 contributor: fullname: Aebi – volume: 16 start-page: 192 year: 2018 ident: 10.1016/j.molliq.2024.124506_b0005 article-title: Catalase enzyme: application in bioremediation and food industry publication-title: Biocatalysis Agricultural Biotechnology doi: 10.1016/j.bcab.2018.07.035 contributor: fullname: Kaushal – volume: 56 start-page: 8680 issue: 18 year: 2008 ident: 10.1016/j.molliq.2024.124506_b0230 article-title: Ethanol effect on the structure of β-lactoglobulin b and its ligand binding publication-title: Journal of Agricultural Food Chemistry doi: 10.1021/jf801383m contributor: fullname: Mousavi – volume: 18 start-page: e00258 year: 2018 ident: 10.1016/j.molliq.2024.124506_b0165 article-title: Immobilization of catalase onto chitosan and chitosan–bentonite complex: a comparative study publication-title: Biotechnol. Rep, doi: 10.1016/j.btre.2018.e00258 contributor: fullname: Kaushal – volume: 7 start-page: 20170030 issue: 6 year: 2017 ident: 10.1016/j.molliq.2024.124506_b0135 article-title: Factors affecting the physical stability (aggregation) of peptide therapeutics publication-title: Interface Focus doi: 10.1098/rsfs.2017.0030 contributor: fullname: Zapadka – volume: 119 start-page: 9905 issue: 30 year: 2015 ident: 10.1016/j.molliq.2024.124506_b0235 article-title: Picosecond solvation and rotational dynamics: an attempt to reinvestigate the mystery of alcohol–water binary mixtures publication-title: J. Phys. Chem. B doi: 10.1021/acs.jpcb.5b04931 contributor: fullname: Banik – volume: 10 start-page: 3503 issue: 1 year: 2020 ident: 10.1016/j.molliq.2024.124506_b0260 article-title: Taurine induces an ordered but functionally inactive conformation in intrinsically disordered casein proteins publication-title: Sci. Rep. doi: 10.1038/s41598-020-60430-7 contributor: fullname: Bhat – volume: 20 start-page: 14672 issue: 40 year: 2014 ident: 10.1016/j.molliq.2024.124506_b0060 article-title: Ethanol and liver: recent insights into the mechanisms of ethanol-induced fatty liver publication-title: World J Gastroenterol: WJG doi: 10.3748/wjg.v20.i40.14672 contributor: fullname: Liu – start-page: 229 year: 2012 ident: 10.1016/j.molliq.2024.124506_b0180 article-title: Fourier transform infrared spectroscopy of intrinsically disordered proteins: measurement procedures and data analyses publication-title: Intrinsically Disordered Protein Analysis: Volume 1, Methods Experimental Tools doi: 10.1007/978-1-61779-927-3_16 contributor: fullname: Natalello – volume: 209 start-page: 198 year: 2022 ident: 10.1016/j.molliq.2024.124506_b0255 article-title: Effect of polyol osmolytes on the structure-function integrity and aggregation propensity of catalase: a comprehensive study based on spectroscopic and molecular dynamic simulation measurements publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2022.04.013 contributor: fullname: Ali – volume: 111 year: 2021 ident: 10.1016/j.molliq.2024.124506_b0045 article-title: Ethanol induced changes in structural, morphological, and functional properties of whey proteins isolates: influence of ethanol concentration publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2020.106379 contributor: fullname: Feng – volume: 50 start-page: 613 year: 2021 ident: 10.1016/j.molliq.2024.124506_b0145 article-title: Evaluation of protein secondary structure from FTIR spectra improved after partial deuteration publication-title: Eur. Biophys. J. doi: 10.1007/s00249-021-01502-y contributor: fullname: De Meutter – volume: 78 start-page: 2625 issue: 12 year: 2010 ident: 10.1016/j.molliq.2024.124506_b0240 publication-title: Role of Partial Protein Unfolding in Alcohol-Induced Protein Aggregation. contributor: fullname: Singh – volume: 278 start-page: 10842 issue: 12 year: 2003 ident: 10.1016/j.molliq.2024.124506_b0210 article-title: Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M212540200 contributor: fullname: Kim – volume: 127 start-page: 100 issue: 1 year: 2005 ident: 10.1016/j.molliq.2024.124506_b0160 article-title: A quantitative reconstruction of the amide I contour in the IR spectra of globular proteins: from structure to spectrum publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0400685 contributor: fullname: Brauner |
SSID | ssj0005580 |
Score | 2.4239879 |
Snippet | •Ethanol induces aggregation with altered structure-function integrity of catalase.•Among osmolytes only sucrose, trehalose and betaine counteracted the... |
SourceID | crossref elsevier |
SourceType | Aggregation Database Publisher |
StartPage | 124506 |
SubjectTerms | Betaine Organic solvent Protein unfolding Solvent polarity Trehalose |
Title | Osmolyte-specific counteraction of ethanol-induced aggregation and structure-function distortion of catalase |
URI | https://dx.doi.org/10.1016/j.molliq.2024.124506 |
Volume | 400 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV09T8MwED2VVggWBAVE-agysLptEjsJY1VRFZDKAJW6RbZjV0WQlrYMLPx27pxEgIQYGGPJSXR27u7F794BXFqEGVqLkEW9UDLOpWGJFglLrLRxhgE4sk7tcxyNJvx2KqY1GFS1MESrLH1_4dOdty5HuqU1u8v5vPtABPqYDgo46VkG6IcbGI44r0Ojf3M3Gn8xPYRroOYkvmlCVUHnaF4vpH39ikAx4B2MdYJaH_0Wob5FneE-7JXpotcv3ugAaiZvws6g6tLWhG1H4dTrQ3i-X-NT3jeGUfUkMYA81wjCrIraBW9hPUM_yhfPDIE4LmnmyRnC7ZlbHE_mmVeoyb6tDKN454YzpyNS3cD97cHAdwST4fXjYMTKXgpMI2jYsLgnfYvQgWeYASgVG5upwCprglAL7idXVuHHzXUoMymI3c8THfUs5mOxQRSlwmOo54vcnICHmEZaobQOpOCGR7gLgjDSXPlcEuJqAavsly4LyYy04pI9pYW9U7J3Wti7BXFl5PTH0qfo1f-cefrvmWewS1d0LOSLc6ijdc0FZhcb1YatzoffLvfQJzTO0Uk |
link.rule.ids | 315,786,790,4521,24144,27955,27956,45618,45712 |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV07T8MwELYqECoLggKiPD2wuo_ETsKIKqoCpQy0UjfLduyqqKSlLQMLv507J5GKhBhYnTiJ7py7--zv7gi5dgAzjBEhi1qhYpwryxIjEpY45eIUHHDkfLXPQdQb8YexGFdIp8yFQVplYftzm-6tdTHSLKTZXEynzRck0Md4UMCxnmUAdngbowHkdTW-NngewrdP8wW-8fYyf86TvN6w8vU7wMSAN8DTCWx89Jt_2vA53X2yVwSL9Db_ngNSsVmNVDtlj7Ya2fEETrM6JLPnFbzlc20Z5k4i_4f6NhB2mWcu0LmjFrfJ5zMGMBwUmlI1AbA98aqhKktpXkv2Y2kZejs_nPoqIuUD_F4PuL0jMureDTs9VnRSYAYgw5rFLdV2ABx4Cv5f69i6VAdOOxuERvB2cuM0_NrchCpVArn9PDFRy0E0FlvAUDo8JlvZPLMnhAKiUU5oYwIluOURrIEgjAzXba4Qb9UJK-UnF3nBDFkyyV5lLm-J8pa5vOskLoUsfyhegk3_c-bpv2dekWpv-NSX_fvB4xnZxSt4QNQW52QLJG0vIM5Y60u_jr4BEMbSHg |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Osmolyte-specific+counteraction+of+ethanol-induced+aggregation+and+structure-function+distortion+of+catalase&rft.jtitle=Journal+of+molecular+liquids&rft.au=Manzoor%2C+Usma&rft.au=Bashir+Hajam%2C+Ishfaq&rft.au=Ali+Dar%2C+Tanveer&rft.date=2024-04-15&rft.pub=Elsevier+B.V&rft.issn=0167-7322&rft.eissn=1873-3166&rft.volume=400&rft_id=info:doi/10.1016%2Fj.molliq.2024.124506&rft.externalDocID=S0167732224005622 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0167-7322&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0167-7322&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0167-7322&client=summon |