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Journal articles on the topic 'Selective Hydrolysis'

Author: Grafiati

Published: 7 July 2024

Last updated: 31 July 2025

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1

Hooper, N. M., A. J. Kenny, and A. J. Turner. "The metabolism of neuropeptides. Neurokinin A (substance K) is a substrate for endopeptidase-24.11 but not for peptidyl dipeptidase A (angiotensin-converting enzyme)." Biochemical Journal 231, no. 2 (1985): 357–61. http://dx.doi.org/10.1042/bj2310357.

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Both endopeptidase-24.11 and peptidyl dipeptidase A have previously been shown to hydrolyse the neuropeptide substance P. The structurally related peptide neurokinin A is also shown to be hydrolysed by pig kidney endopeptidase-24.11. The identified products indicated hydrolysis at two sites, Ser5-Phe6 and Gly8-Leu9, consistent with the known specificity of the enzyme. The pattern of hydrolysis of neurokinin A by synaptic membranes prepared from pig striatum was similar to that observed with purified endopeptidase-24.11, and hydrolysis was substantially abolished by the selective inhibitor phos

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2

Badiani, K., and G. Arthur. "2-acyl-sn-glycero-3-phosphoethanolamine lysophospholipase A2 activity in guinea-pig heart microsomes." Biochemical Journal 275, no. 2 (1991): 393–98. http://dx.doi.org/10.1042/bj2750393.

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We have recently described a lysophospholipase A2 activity in guinea-pig heart microsomes that hydrolyses 2-acyl-sn-glycero-3-phosphocholine (2-acyl-GPC). The presence of a similar activity that hydrolyses 2-acyl-sn-glycero-3-phosphoethanolamine (2-acyl-GPE) was not known. In this study, a lysophospholipase A2 activity in guinea-pig heart microsomes that hydrolyses 2-acyl-GPE has been characterized. The enzyme did not require Ca2+ for activity and exhibited a high specificity for 2-arachidonoyl-GPE and 2-linoleoyl-GPE over 2-oleoyl-GPE and 2-palmitoyl-GPE. The specificity for these unsaturated

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3

Lisak Jakopović, Katarina, Seronei Chelulei Cheison, Ulrich Kulozik та Rajka Božanić. "Comparison of selective hydrolysis of α-lactalbumin by acid Protease A and Protease M as alternative to pepsin: potential for β-lactoglobulin purification in whey proteins". Journal of Dairy Research 86, № 1 (2019): 114–19. http://dx.doi.org/10.1017/s0022029919000086.

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AbstractThe experiments reported in this research paper examine the potential of digestion using acidic enzymes Protease A and Protease M to selectively hydrolyse α-lactalbumin (α-La) whilst leaving β-lactoglobulin (β-Lg) relatively intact. Both enzymes were compared with pepsin hydrolysis since its selectivity to different whey proteins is known. Analysis of the hydrolysis environment showed that the pH and temperature play a significant role in determining the best conditions for achievement of hydrolysis, irrespective of which enzyme was used. Whey protein isolate (WPI) was hydrolysed using

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4

Shipilov, A. I., L. A. Kolpashchikova, and S. M. Igumnov. "Selective Hydrolysis of Pentafluorobenzotrichloride." Russian Journal of Organic Chemistry 39, no. 7 (2003): 975–78. http://dx.doi.org/10.1023/b:rujo.0000003188.49417.22.

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5

Chan, Lai Chun, Brian G. Cox, and Rhona S. Sinclair. "Selective Hydrolysis of Methanesulfonate Esters." Organic Process Research & Development 12, no. 2 (2008): 213–17. http://dx.doi.org/10.1021/op700226s.

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6

Bui, Tien Tan, and Yan Zhao. "Molecularly Imprinted Nanozymes for Selective Hydrolysis of Aromatic Carbonates Under Mild Conditions." Nanomaterials 15, no. 3 (2025): 169. https://doi.org/10.3390/nano15030169.

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Aliphatic polycarbonate (PC) can be readily hydrolyzed by lipase, but bisphenol A-derived PC (i.e., BPA-PC) lacks enzyme catalysts for their efficient hydrolysis due to the high hydrophobicity and rigidity of its polymer backbone. This study aims to develop an artificial nanozyme for the selective hydrolysis of small-molecule aromatic carbonates as model substrates for BPA-PC. The catalyst is prepared through molecular imprinting of cross-linkable micelles in a one-pot reaction using a thiourea template and a zinc-containing functional monomer. The resulting water-soluble nanoparticle resemble

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7

Unnikrishnan, Parvathy, Binsi Puthenveetil Kizhakkethil, Jeyakumari Annamalai, et al. "Selective Extraction of Surface-active and Antioxidant Hydrolysates from Yellowfin Tuna Red Meat Protein using Papain by Response Surface Methodology." Indian Journal of Nutrition and Dietetics 56, no. 1 (2019): 10. http://dx.doi.org/10.21048//ijnd.2019.56.1.22125.

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The present study was focused on the selective extraction of surface-active and antioxidant hydrolysates from yellowfin tuna (Thunnus albacares) red meat based on separate hydrolytic conditions using papain. The effect of key processing variables viz., enzymesubstrate ratio (0.25-1.5 %) and hydrolysis time (30-240 min) under optimized temperature and pH, on the protein recovery, surface-active and antioxidative properties, was determined using Response Surface Methodology (RSM) with a central composite design. Single and combined effects of the variables on the responses were studied by formul

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8

Basavaiah, D., and S. Bhaskar Raju. "Selective Enzymatic Hydrolysis of Phenolic Acetates." Synthetic Communications 24, no. 4 (1994): 467–73. http://dx.doi.org/10.1080/00397919408011496.

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9

Blay, Gonzalo, M. Luz Cardona, M. Begoña Garcia, and José R. Pedro. "A Selective Hydrolysis of Aryl Acetates." Synthesis 1989, no. 06 (1989): 438–39. http://dx.doi.org/10.1055/s-1989-27277.

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10

Litt, M. H., and C. S. Lin. "Selective hydrolysis of oxazoline block copolymers." Journal of Polymer Science Part A: Polymer Chemistry 30, no. 5 (1992): 779–86. http://dx.doi.org/10.1002/pola.1992.080300507.

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11

Shi, Qixun, Matthew P. Mower, Donna G. Blackmond, and Julius Rebek. "Water-soluble cavitands promote hydrolyses of long-chain diesters." Proceedings of the National Academy of Sciences 113, no. 33 (2016): 9199–203. http://dx.doi.org/10.1073/pnas.1610006113.

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Water-soluble, deep cavitands serve as chaperones of long-chain diesters for their selective hydrolysis in aqueous solution. The cavitands bind the diesters in rapidly exchanging, folded J-shape conformations that bury the hydrocarbon chain and expose each ester group in turn to the aqueous medium. The acid hydrolyses in the presence of the cavitand result in enhanced yields of monoacid monoester products. Product distributions indicate a two- to fourfold relative decrease in the hydrolysis rate constant of the second ester caused by the confined space in the cavitand. The rate constant for th

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12

Jones, J. Bryan, R. Scott Hinks, and Philip G. Hultin. "Enzymes in organic synthesis. 33. Stereoselective pig liver esterase-catalyzed hydrolyses of meso cyclopentyl-, tetrahydrofuranyl-, and tetrahydrothiophenyl-1,3-diesters." Canadian Journal of Chemistry 63, no. 2 (1985): 452–56. http://dx.doi.org/10.1139/v85-074.

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Preparative-scale pig liver esterase-catalyzed hydrolyses of five-membered ring meso-1,3-diesters are enantiotopically selective. While pro-S enantiotopic selectivity is exhibited in each case, the absolute configuration sense of the hydrolysis in the cyclopentyl series is opposite to that of both the tetrahydrofuranyl and tetrahydrothiophenyl diesters. The enantiomeric excess levels induced are in the 34–46% range.

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13

Mironowicz, Agnieszka, Bogdan Jarosz, and Antoni Siewiński. "The ability of fruit and vegetable enzyme system to hydrolyse ester bonds." Acta Societatis Botanicorum Poloniae 64, no. 3 (2014): 281–85. http://dx.doi.org/10.5586/asbp.1995.037.

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The pulp of potato tubers (<i>Solanum tuberosum</i>), topinambur (<i>Helianthus tuberosus</i>) and apples (<i>Malus silvestris</i>) can hydrolyse totally, or almost totally, ester bonds in phenyl, α- and β-naphthyl, benzyl and cinnamyl acetates. In methyl 4-acetoxy-3-metoxybenzoate and methyl 2,5-diacetoxybenzoate as well as testosterone propionate and 16,17-acetonide of 21-acetoxy-6-fluoro-16α,17β,21-trihydroxy-4-pregnen-3,20-dione, the hydrolysis is selective towards the substrate and the bioreagent. In contrast, ethyl benzoate and cinnamate are resistant

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14

Kim, Ja Hyung, Hyun Jung Kim, Chang Wan Bae, Jun Won Park, Joung Hae Lee, and Jong Seung Kim. "Hg2+-induced hydrolysis-based selective fluorescent chemodosimeter." Arkivoc 2010, no. 7 (2010): 170–78. http://dx.doi.org/10.3998/ark.5550190.0011.713.

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15

FUNADA, Tadashi, Jiro HIRANO, Ron HASHIZUME, and Yukihisa TANAKA. "Selective Hydrolysis of Fish Oil by Bioreactors." Journal of Japan Oil Chemists' Society 41, no. 6 (1992): 495–500. http://dx.doi.org/10.5650/jos1956.41.495.

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16

Cioletti, Alessandra Gomes, Ricardo José Alves, José Dias de Souza Filho, Josiano Gomes Chaves, and Maria Auxiliadora Fontes Prado. "Mild Selective Hydrolysis of Acetals in Carbohydrates." Synthetic Communications 30, no. 11 (2000): 2019–28. http://dx.doi.org/10.1080/00397910008087251.

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17

Rusanen, Annu, Katja Lappalainen, Johanna Kärkkäinen, Tero Tuuttila, Marja Mikola, and Ulla Lassi. "Selective hemicellulose hydrolysis of Scots pine sawdust." Biomass Conversion and Biorefinery 9, no. 2 (2018): 283–91. http://dx.doi.org/10.1007/s13399-018-0357-z.

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18

Ji, N., J. Xu, Y. Wang, M. Guo, and X. Xu. "Selective protein hydrolysis catalyzed by LaCoO3 nanoparticles." Materials Today Chemistry 34 (December 2023): 101823. http://dx.doi.org/10.1016/j.mtchem.2023.101823.

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19

Lisak, Katarina, Jose Toro-Sierra, Ulrich Kulozik, Rajka Božanić та Seronei Chelulei Cheison. "Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification". Journal of Dairy Research 80, № 1 (2012): 14–20. http://dx.doi.org/10.1017/s0022029912000416.

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The present study examines the resistance of the α-lactalbumin to α-chymotrypsin (EC 3.4.21.1) digestion under various experimental conditions. Whey protein isolate (WPI) was hydrolysed using randomised hydrolysis conditions (5 and 10% of WPI; pH 7·0, 7·8 and 8·5; temperature 25, 37 and 50 °C; enzyme-to-substrate ratio, E/S, of 0·1%, 0·5 and 1%). Reversed-phase high performance liquid chromatography (RP-HPLC) was used to analyse residual proteins. Heat, pH adjustment and two inhibitors (Bowman–Birk inhibitor and trypsin inhibitor from chicken egg white) were used to stop the enzyme reaction. W

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20

BRISSETTE, Louise, Marie-Claude CHAREST, and Louise FALSTRAULT. "Selective uptake of cholesteryl esters of low-density lipoproteins is mediated by the lipoprotein-binding site in HepG2 cells and is followed by the hydrolysis of cholesteryl esters." Biochemical Journal 318, no. 3 (1996): 841–47. http://dx.doi.org/10.1042/bj3180841.

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The study described in this paper shows that 125I-labelled low-density lipoproteins (LDL) interact with high- and low-affinity binding sites on human hepatoma (HepG2) cells. The former site is the LDL receptor and the latter is the lipoprotein-binding site (LBS). The association of 125I-labelled LDL and [3H]cholesteryl ethers–LDL with HepG2 cells revealed a 4-fold selective uptake of cholesteryl esters (CE) in a 4 h incubation period, which correlated with the depletion of CE mass in LDL. This selective uptake was not observed when the cells were incubated in the presence of a 100-fold excess

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21

WATANABE, Takeshi, Yumiko ARIGA, Urara SATO, et al. "Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin." Biochemical Journal 376, no. 1 (2003): 237–44. http://dx.doi.org/10.1042/bj20030419.

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Bacillus circulans chitinase A1 (ChiA1) has a deep substrate-binding cleft on top of its (β/α)8-barrel catalytic domain and an interaction between the aromatic residues in this cleft and bound oligosaccharide has been suggested. To study the roles of these aromatic residues, especially in crystalline-chitin hydrolysis, site-directed mutagenesis of these residues was carried out. Y56A and W53A mutations at subsites −5 and −3, respectively, selectively decreased the hydrolysing activity against highly crystalline β-chitin. W164A and W285A mutations at subsites +1 and +2, respectively, decreased

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22

Lyu, Hongyu, Shuai Chen, Rong Zhang, Chunliang Zhang, Ruiruo Jiang, and Wen Yang. "Enhanced hydrolysis of spiramycin in aqueous solution using SiO₂/SO₃H." Journal of Physics: Conference Series 2842, no. 1 (2024): 012018. http://dx.doi.org/10.1088/1742-6596/2842/1/012018.

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Abstract Sulfonated silicon dioxide (SiO2/SO3H) solid acids were synthesized and they were characterized and used for spiramycin hydrolysis pretreatment of antibiotic wastewater. Results show that the spiramycin removal effect rankings are as follows: SiO2/SO3H > SiO2 (pH = 3 or so) > control group. A first-order model was used to reflect the hydrolytic kinetics. The hydrolysis rate of the SiO2/SO3H solid acid calcined at 600°C is the highest, up to 3.59×10−2 (k). The performance of SiO2/SO3H is in positive correlation with the total acidity, which was determined by using the n-butylamin

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23

LIU, Jing-Yuan, He-Shui YU, Bing FENG, et al. "Selective hydrolysis of flavonoid glycosides by Curvularia lunata." Chinese Journal of Natural Medicines 11, no. 6 (2014): 684–89. http://dx.doi.org/10.3724/sp.j.1009.2013.00684.

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24

Olivera Pastor, P., E. Rodríguez-Castellón, and A. Rodrífguez. "HYDROLYSIS AND SELECTIVE SORPTION OF LANTHANIDES IN VERMICULITE." Solvent Extraction and Ion Exchange 5, no. 6 (1987): 1151–69. http://dx.doi.org/10.1080/07366298708918614.

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25

Basu, Manas K., Dipak C. Sarkar, and Brindaban C. Ranu. "A mild and Selective Method of Ester Hydrolysis." Synthetic Communications 19, no. 3-4 (1989): 627–31. http://dx.doi.org/10.1080/00397918908050708.

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26

LIU, Jing-Yuan, He-Shui YU, Bing FENG, et al. "Selective hydrolysis of flavonoid glycosides by Curvularia lunata." Chinese Journal of Natural Medicines 11, no. 6 (2013): 684–89. http://dx.doi.org/10.1016/s1875-5364(13)60080-1.

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27

Barnett, James D., and Susanne Striegler. "Tuning Templated Microgel Catalysts for Selective Glycoside Hydrolysis." Topics in Catalysis 55, no. 7-10 (2012): 460–65. http://dx.doi.org/10.1007/s11244-012-9817-z.

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28

Falcone, Joseph M., and Harold C. Box. "Selective hydrolysis of damaged DNA by nuclease P1." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1337, no. 2 (1997): 267–75. http://dx.doi.org/10.1016/s0167-4838(96)00172-0.

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29

Goto, Muneharu, Masahiro Goto, and Fumiyuki Nakashio. "Selective Hydrolysis of Triglycerides with Surfactant-coated Lipase." KAGAKU KOGAKU RONBUNSHU 19, no. 3 (1993): 424–30. http://dx.doi.org/10.1252/kakoronbunshu.19.424.

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30

Chajkowski, S. M., J. Mallela, D. E. Watson, et al. "Highly selective hydrolysis of kinins by recombinant prolylcarboxypeptidase." Biochemical and Biophysical Research Communications 405, no. 3 (2011): 338–43. http://dx.doi.org/10.1016/j.bbrc.2010.12.036.

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31

Chen, Shui-Tein, Chung-Ho Chang, Johnson Lin, and Kung-Tsung Wang. "Selective Alkaline Protease Catalyzed Hydrolysis of Peptide Esters." Journal of the Chinese Chemical Society 37, no. 3 (1990): 299–305. http://dx.doi.org/10.1002/jccs.199000041.

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32

BASAVAIAH, D., and S. B. RAJU. "ChemInform Abstract: Selective Enzymatic Hydrolysis of Phenolic Acetates." ChemInform 25, no. 42 (2010): no. http://dx.doi.org/10.1002/chin.199442035.

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33

Mahalingam, Sakkarapalayam M., Bijay K. Mishra, and Hari N. Pati. "ChemInform Abstract: Selective Hydrolysis of Terminal Isopropylidene Ketals." ChemInform 41, no. 22 (2010): no. http://dx.doi.org/10.1002/chin.201022222.

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34

Jacques, Sylvain A., Geoffray Leriche, Michel Mosser, et al. "From solution to in-cell study of the chemical reactivity of acid sensitive functional groups: a rational approach towards improved cleavable linkers for biospecific endosomal release." Organic & Biomolecular Chemistry 14, no. 21 (2016): 4794–803. http://dx.doi.org/10.1039/c6ob00846a.

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35

Adhikari, R., C. L. Francis, G. W. Simpson, and Q. Yang. "Selective Protection Strategies in the Synthesis of TRIS-Fatty Ester Derivatives." Australian Journal of Chemistry 55, no. 10 (2002): 629. http://dx.doi.org/10.1071/ch02124.

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A methodology for the selective synthesis of lipophilic acyl derivatives of the glycinamido triol (1) with either one, two, or three fatty ester groups has been established. Peracylation of (1), with palmitoyl chloride gave the triacylated derivative. Conversion of (1) into the acetonide, followed by acylation with either palmitoyl chloride or lauroyl chloride, and acetal hydrolysis provided the monoacylated derivatives. Treatment of (1) with trimethyl orthoacetate gave the orthoacetate derivative. Mild hydrolysis provided the monoacetate/diol. Acylation of the two hydroxyl groups with palmito

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36

Ash, Jeffrey, Hai Huang, Paula Cordero, and Jun Yong Kang. "Selective hydrolysis of phosphorus(v) compounds to form organophosphorus monoacids." Organic & Biomolecular Chemistry 19, no. 27 (2021): 6007–14. http://dx.doi.org/10.1039/d1ob00881a.

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37

Park, Sun Young, Woori Kim, Sun-Hee Park, et al. "An endoplasmic reticulum-selective ratiometric fluorescent probe for imaging a copper pool." Chemical Communications 53, no. 32 (2017): 4457–60. http://dx.doi.org/10.1039/c7cc01430a.

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38

Imiołek, Mateusz, Patrick G. Isenegger, Wai-Lung Ng, Aziz Khan, Véronique Gouverneur, and Benjamin G. Davis. "Residue-Selective Protein C-Formylation via Sequential Difluoroalkylation-Hydrolysis." ACS Central Science 7, no. 1 (2021): 145–55. http://dx.doi.org/10.1021/acscentsci.0c01193.

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39

Van Rompuy, Laura S., Nada D. Savić, Alvaro Rodriguez, and Tatjana N. Parac-Vogt. "Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates." Molecules 25, no. 15 (2020): 3472. http://dx.doi.org/10.3390/molecules25153472.

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The hydrolysis of the iron-binding blood plasma glycoprotein transferrin (Tf) has been examined at pH = 7.4 in the presence of a series of Zr-substituted polyoxometalates (Zr-POMs) including Keggin (Et2NH2)10[Zr(PW11O39)2]∙7H2O (Zr-K 1:2), (Et2NH2)8[{α-PW11O39Zr-(μ-OH) (H2O)}2]∙7H2O (Zr-K 2:2), Wells-Dawson K15H[Zr(α2-P2W17O61)2]·25H2O (Zr-WD 1:2), Na14[Zr4(α-P2W16O59)2(μ3-O)2(μ-OH)2(H2O)4]·57H2O (Zr-WD 4:2) and Lindqvist (Me4N)2[ZrW5O18(H2O)3] (Zr-L 1:1), (nBu4N)6[(ZrW5O18(μ–OH))2]∙2H2O (Zr-L 2:2)) type POMs. Incubation of transferrin with Zr-POMs resulted in formation of 13 polypeptide fragm

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40

Xiao, Xiangshu, and Donglu Bai. "An Efficient and Selective Method for Hydrolysis of Acetonides." Synlett 2001, no. 04 (2001): 0535–37. http://dx.doi.org/10.1055/s-2001-12340.

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41

Wang, Jun, Yan-Long Ma, Xiang-Yang Wu, et al. "Selective hydrolysis by commercially available hesperidinase for isoquercitrin production." Journal of Molecular Catalysis B: Enzymatic 81 (September 2012): 37–42. http://dx.doi.org/10.1016/j.molcatb.2012.05.005.

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42

Hayashi, Nobuhiro, Naoya Takeda, Tetsuro Shiiba, Morio Yashiro, Kimitsuna Watanabe, and Makoto Komiyama. "Site-selective hydrolysis of tRNA by lanthanide metal complexes." Inorganic Chemistry 32, no. 26 (1993): 5899–900. http://dx.doi.org/10.1021/ic00078a002.

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43

Dinh, Phi M., Jonathan MJ Williams, and William Harris. "Selective racemisation of esters: Relevance to enzymatic hydrolysis reactions." Tetrahedron Letters 40, no. 4 (1999): 749–52. http://dx.doi.org/10.1016/s0040-4039(98)02362-4.

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44

Fernandez-Lorente, Gloria, Jose M. Palomo, Jany Cocca, et al. "Regio-selective deprotection of peracetylated sugars via lipase hydrolysis." Tetrahedron 59, no. 30 (2003): 5705–11. http://dx.doi.org/10.1016/s0040-4020(03)00876-7.

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45

Poppe, László, Lajos Novák, Mária Kajtár-Peredy, and Csaba Szántay. "Lipase-catalyzed enantiomer selective hydrolysis of 1,2-diol diacetates." Tetrahedron: Asymmetry 4, no. 10 (1993): 2211–17. http://dx.doi.org/10.1016/s0957-4166(00)80071-3.

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46

Chmielowiec, Urszula, Hanna Kruszewska, and Jacek Cybulski. "Selective hydrolysis of nucleotides to nucleosides and free bases." Il Farmaco 54, no. 9 (1999): 611–14. http://dx.doi.org/10.1016/s0014-827x(99)00071-3.

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47

Penín, L., S. Peleteiro, V. Santos, J. L. Alonso, and J. C. Parajó. "Selective fractionation and enzymatic hydrolysis of Eucalyptus nitens wood." Cellulose 26, no. 2 (2018): 1125–39. http://dx.doi.org/10.1007/s10570-018-2109-4.

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48

Briggs, John R., Arnold M. Harrison, and John H. Robson. "Selective ethylene oxide hydrolysis catalysed by oxo-molybdenum species." Polyhedron 5, no. 1-2 (1986): 281–87. http://dx.doi.org/10.1016/s0277-5387(00)84923-2.

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49

Baillargeon, Mary Welch, and Philip E. Sonnet. "Selective lipid hydrolysis byGeotrichum candidum NRRL Y-553 lipase." Biotechnology Letters 13, no. 12 (1991): 871–74. http://dx.doi.org/10.1007/bf01022089.

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50

Gomes Cioletti, Alessandra, Ricardo Jose Alves, Jose Dias de Souza Filho, Josiano Gomes Chaves, and Maria Auxiliadora Fontes Prado. "ChemInform Abstract: Mild Selective Hydrolysis of Acetals in Carbohydrates." ChemInform 31, no. 36 (2010): no. http://dx.doi.org/10.1002/chin.200036222.

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