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Journal articles on the topic 'Selective Hydrolysis'

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Published: 7 July 2024

Last updated: 7 July 2024

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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 (October 15, 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 phosphoramidon. Peptidyl dipeptidase A purified from pig kidney was shown to hydrolyse substance P but not neurokinin A. It is concluded that endopeptidase-24.11 has the general capacity to hydrolyse and inactivate the family of tachykinin peptides, including substance P and neurokinin A.

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 (April 15, 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 substrates was observed in the presence and absence of detergents. Selective hydrolysis of 2-arachidonoyl-GPE over 2-palmitoyl-GPE was observed when equimolar quantities of the two substrates were incubated with the enzyme. There was no preferential hydrolysis of either 2-linoleoyl- or 2-arachidonoyl-GPE when presented individually or as a mixture. Significant differences in the characteristics of 2-acyl-GPE-hydrolysing and 2-acyl-GPC-hydrolysing activities included differences in their optimum pH, the effect of Ca2+ and their acyl specificities. Taken together, these results suggest that the two activities are catalysed by different enzymes. 2-Acyl-GPE lysophospholipase activity with a preference for 2-arachidonoyl-GPE over 2-oleoyl-GPE was observed in guinea-pig brain, liver, kidney and lung microsomes. Lysophospholipase A1 activity that catalyses the hydrolysis of 1-acyl-GPE was also present in guinea-pig heart microsomes and had different characteristics from the 2-acyl-GPE-hydrolysing activity, including a preference for saturated over unsaturated substrates. The 2-acyl-GPE lysophospholipase A2 activity appeared to be distinct from Ca(2+)-independent phospholipase A2. The characteristics of the 2-acyl-GPE lysophospholipase A2 suggest it could play a role in the selective release of arachidonic and linoleic acids for further metabolism in cells.

3

Lisak Jakopović, Katarina, Seronei Chelulei Cheison, Ulrich Kulozik, and 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, no. 1 (February 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 pepsin, Acid Protease A and Protease M by randomized hydrolysis conditions. Reversed-phase high performance liquid chromatography was used to analyse residual proteins. Regarding enzyme selectivity under various milieu conditions, all three enzymes showed similarities in the reaction progress and their potential for β-Lg isolation.

4

Shipilov, A. I., L. A. Kolpashchikova, and S. M. Igumnov. "Selective Hydrolysis of Pentafluorobenzotrichloride." Russian Journal of Organic Chemistry 39, no. 7 (July 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 (March 2008): 213–17. http://dx.doi.org/10.1021/op700226s.

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6

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

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7

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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8

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

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9

Unnikrishnan, Parvathy, Binsi Puthenveetil Kizhakkethil, Jeyakumari Annamalai, Joshy Chalil George, Aliyamveetil Abubacker Zynudheen, George Ninan, and Chandragiri Nagarajarao Ravishankar. "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 (January 22, 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 formulating 13 experimental runs. The coefficient of determination (R2) ranged between 0.73 – 0.99 indicating the suitability of the fitted regression models. The optimum hydrolytic conditions to get hydrolysates having superior surface-active properties were enzyme-substrate ratio (E/S) of 0.41 % and 30 minutes hydrolysis time with a desirability of 0.611. Similarly, the optimum conditions to exhibit the highest antioxidative properties with a desirability of 0.932 were: 1.28 % E/S and 240 minutes hydrolysis time.

10

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 (August 1, 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 the first acid hydrolysis step is enhanced approximately 10-fold in the presence of the cavitand, compared with control reactions of the molecules in bulk solution. Hydrolysis under basic conditions (saponification) with the cavitand gave >90% yields of the corresponding monoesters. Under basic conditions the cavitand complex of the monoanion precipitates from solution and prevents further reaction.

11

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 (August 9, 2010): 170–78. http://dx.doi.org/10.3998/ark.5550190.0011.713.

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12

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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13

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 (June 2000): 2019–28. http://dx.doi.org/10.1080/00397910008087251.

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14

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 (December 6, 2018): 283–91. http://dx.doi.org/10.1007/s13399-018-0357-z.

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15

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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16

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 (February 1, 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.

17

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 to hydrolysis.

18

Lisak, Katarina, Jose Toro-Sierra, Ulrich Kulozik, Rajka Božanić, and 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, no. 1 (September 21, 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. While operating outside of the enzyme optimum it was observed that at pH 8·5 selective hydrolysis of β-lactoglobulin was improved because of a dimer-to-monomer transition while α-la remained relatively resistant. The best conditions for the recovery of native and pure α-la were at 25 °C, pH 8·5, 1% E/S ratio, 5% WPI (w/v) while the enzyme was inhibited using Bowman–Birk inhibitor with around 81% of original α-la in WPI was recovered with no more β-lg. Operating conditions for hydrolysis away from the chymotrypsin optimum conditions offers a great potential for selective WPI hydrolysis, and removal, of β-lg with production of whey protein concentrates containing low or no β-lg and pure native α-la. This method also offers the possibility for production of β-lg-depleted milk products for sensitive populations.

19

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 (September 15, 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 of high-density lipoprotein 3, conditions where only the LDL receptor is being monitored. Also, no reduction in uptake was observed in the presence of IgG-C7, an anti-(LDL receptor) monoclonal antibody. Both findings indicate that the selective uptake occurs through the LBS and that the LBS contributes more to the entry of CE from LDL into the cell than does the LDL receptor. The fates of CE entering the cell via the LDL receptor and the LBS were also followed. To achieve this, LDL were labelled with [3H]cholesteryl oleate and the hydrolysis of [3H]cholesteryl oleate was monitored. The results indicated that 45% of the CE were hydrolysed after a 4 h incubation period, irrespective of the site of entry. Chloroquine (100 µM) was shown to inhibit hydrolysis, indicating that lysosomal enzymes were responsible for the hydrolysis of LDL–CE, whichever pathway was used. Thus our results reveal, for the first time, that the mass of CE entering the cell via the LBS is substantial and that hydrolysis of CE is by lysosomal enzyme activity. Overall, this suggests that the LBS has significant physiological importance.

20

WATANABE, Takeshi, Yumiko ARIGA, Urara SATO, Tadayuki TORATANI, Masayuki HASHIMOTO, Naoki NIKAIDOU, Yuichiro KEZUKA, Takamasa NONAKA, and Junji SUGIYAMA. "Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin." Biochemical Journal 376, no. 1 (November 15, 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 the hydrolysing activity against crystalline β-chitin and colloidal chitin, but enhanced the activities against soluble substrates. These mutations increased the Km-value when reduced (GlcNAc)5 (where GlcNAc is N-acetylglucosamine) was used as the substrate, but decreased substrate inhibition observed with wild-type ChiA1 at higher concentrations of this substrate. In contrast with the selective effect of the other mutations, mutations of W433 and Y279 at subsite −1 decreased the hydrolysing activity drastically against all substrates and reduced the kcat-value, measured with 4-methylumbelliferyl chitotrioside to 0.022% and 0.59% respectively. From these observations, it was concluded that residues Y56 and W53 are only essential for crystalline-chitin hydrolysis. W164 and W285 are very important for crystalline-chitin hydrolysis and also participate in hydrolysis of other substrates. W433 and Y279 are both essential for catalytic reaction as predicted from the structure.

21

LIU, Jing-Yuan, He-Shui YU, Bing FENG, Li-Ping KANG, Xu PANG, Cheng-Qi XIONG, Yang ZHAO, Chun-Mei LI, Yi ZHANG, and Bai-Ping MA. "Selective hydrolysis of flavonoid glycosides by Curvularia lunata." Chinese Journal of Natural Medicines 11, no. 6 (March 24, 2014): 684–89. http://dx.doi.org/10.3724/sp.j.1009.2013.00684.

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22

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 (December 1987): 1151–69. http://dx.doi.org/10.1080/07366298708918614.

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23

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

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24

LIU, Jing-Yuan, He-Shui YU, Bing FENG, Li-Ping KANG, Xu PANG, Cheng-Qi XIONG, Yang ZHAO, Chun-Mei LI, Yi ZHANG, and Bai-Ping MA. "Selective hydrolysis of flavonoid glycosides by Curvularia lunata." Chinese Journal of Natural Medicines 11, no. 6 (November 2013): 684–89. http://dx.doi.org/10.1016/s1875-5364(13)60080-1.

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25

Barnett, James D., and Susanne Striegler. "Tuning Templated Microgel Catalysts for Selective Glycoside Hydrolysis." Topics in Catalysis 55, no. 7-10 (June 23, 2012): 460–65. http://dx.doi.org/10.1007/s11244-012-9817-z.

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26

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 (February 1997): 267–75. http://dx.doi.org/10.1016/s0167-4838(96)00172-0.

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27

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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28

Chajkowski, S. M., J. Mallela, D. E. Watson, J. Wang, C. R. McCurdy, J. M. Rimoldi, and Z. Shariat-Madar. "Highly selective hydrolysis of kinins by recombinant prolylcarboxypeptidase." Biochemical and Biophysical Research Communications 405, no. 3 (February 2011): 338–43. http://dx.doi.org/10.1016/j.bbrc.2010.12.036.

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29

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 (June 1990): 299–305. http://dx.doi.org/10.1002/jccs.199000041.

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30

BASAVAIAH, D., and S. B. RAJU. "ChemInform Abstract: Selective Enzymatic Hydrolysis of Phenolic Acetates." ChemInform 25, no. 42 (August 18, 2010): no. http://dx.doi.org/10.1002/chin.199442035.

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31

Mahalingam, Sakkarapalayam M., Bijay K. Mishra, and Hari N. Pati. "ChemInform Abstract: Selective Hydrolysis of Terminal Isopropylidene Ketals." ChemInform 41, no. 22 (June 1, 2010): no. http://dx.doi.org/10.1002/chin.201022222.

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32

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 palmitoyl chloride gave the dipalmitate/acetate. Selective cleavage of the acetate group afforded the dipalmitate of (1). Analogous chemistry with trimethyl orthoformate provided the same dipalmitate via the orthoformate, monoformate/diol, and dipalmitate/formate. A more robust synthesis of the dipalmitate was achieved by converting the hydroxyl group of the acetonide of (1) into a tert-butyldiphenylsilyl ether, followed by acetal hydrolysis, palmitoylation of the liberated hydroxyl groups, and desilylation.

33

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 (January 13, 2021): 145–55. http://dx.doi.org/10.1021/acscentsci.0c01193.

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34

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 (July 30, 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 fragments that were observed on sodium dodecyl sulfate poly(acrylamide) gel electrophoresis (SDS-PAGE), but the hydrolysis efficiency varied depending on the nature of Zr-POMs. Molecular interactions between Zr-POMs and transferrin were investigated by using a range of complementary techniques such as tryptophan fluorescence, circular dichroism (CD), 31P-NMR spectroscopy, in order to gain better understanding of different efficiency of investigated Zr-POMs. A tryptophan fluorescence quenching study revealed that the most reactive Zr-WD species show the strongest interaction toward transferrin. The CD results demonstrated that interaction of Zr-POMs and transferrin in buffer solution result in significant secondary structure changes. The speciation of Zr-POMs has been followed by 31P-NMR spectroscopy in the presence and absence of transferrin, providing insight into stability of the catalysts under reaction condition.

35

Xiao, Xiangshu, and Donglu Bai. "An Efficient and Selective Method for Hydrolysis of Acetonides." Synlett 2001, no. 04 (December 31, 2001): 0535–37. http://dx.doi.org/10.1055/s-2001-12340.

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36

Wang, Jun, Yan-Long Ma, Xiang-Yang Wu, Liang Yu, Rui Xia, Guo-Xia Sun, and Fu-An Wu. "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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37

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 (December 1993): 5899–900. http://dx.doi.org/10.1021/ic00078a002.

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38

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

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39

Fernandez-Lorente, Gloria, Jose M. Palomo, Jany Cocca, Cesar Mateo, Paola Moro, Marco Terreni, Roberto Fernandez-Lafuente, and Jose M. Guisan. "Regio-selective deprotection of peracetylated sugars via lipase hydrolysis." Tetrahedron 59, no. 30 (July 2003): 5705–11. http://dx.doi.org/10.1016/s0040-4020(03)00876-7.

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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 (October 1993): 2211–17. http://dx.doi.org/10.1016/s0957-4166(00)80071-3.

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

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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 (November 16, 2018): 1125–39. http://dx.doi.org/10.1007/s10570-018-2109-4.

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43

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

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

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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 (June 3, 2010): no. http://dx.doi.org/10.1002/chin.200036222.

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Jacques, Sylvain A., Geoffray Leriche, Michel Mosser, Marc Nothisen, Christian D. Muller, Jean-Serge Remy, and Alain Wagner. "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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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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48

Bibiłło, A., K. Ziomek, M. Figlerowicz, and R. Kierzek. "Nonenzymatic hydrolysis of oligoribonucleotides. V. The elements affecting the process of self-hydrolysis." Acta Biochimica Polonica 46, no. 1 (March 31, 1999): 145–53. http://dx.doi.org/10.18388/abp.1999_4192.

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Abstract:

Chemical instability of some of the phosphodiester bonds, often observed in large RNAs, visualizes the autocatalytic properties of this class of nucleic acids. Unexpectedly, selective hydrolysis occurs also in short oligoribonucleotides (as short as a tetramer or hexamer). Herein, we describe additional experiments which support the conclusion that the hydrolysis is not due to ribonuclease contamination but is of autocatalytic origin and is related to the sequence and structure of single-stranded oligomers. Moreover, we show that the presence in the reaction mixture of polyamines, such as spermidine, is essential for hydrolysis of oligoribonucleotides.

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Ni, Jizhi, Youhei Sohma, and Motomu Kanai. "Scandium(iii) triflate-promoted serine/threonine-selective peptide bond cleavage." Chemical Communications 53, no. 23 (2017): 3311–14. http://dx.doi.org/10.1039/c6cc10300f.

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50

Gutteridge, S., G. S. Reddy, and G. Lorimer. "The synthesis and purification of 2′-carboxy-d-arabinitol 1-phosphate, a natural inhibitor of ribulose 1,5-bisphosphate carboxylase, investigated by31P n.m.r." Biochemical Journal 260, no. 3 (June 15, 1989): 711–16. http://dx.doi.org/10.1042/bj2600711.

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Abstract:

2′-Carboxy-D-arabinitol 1-phosphate (2CA1P), a natural inhibitor of ribulose 1,5-bisphosphate carboxylase was synthesized from 2′-carboxy-D-arabinitol 1,5-bisphosphate (2CABP). The selective dephosphorylation of 2CABP with either acid phosphatase or alkaline phosphatase was investigated by using 31P n.m.r. The n.m.r. spectra of the progress of the reactions indicated that both phosphatases preferentially removed the 5-phosphate from the bisphosphate. After the consumption of all of the bisphosphate, alkaline phosphatase generated a mixture of 2′-carboxy-D-arabinitol 1- and 5-monophosphates in the ratio of about 4:1, along with Pi. The enzyme also hydrolysed the monophosphates to 2′-carboxyarabinitol, thus decreasing the yield of 2CA1P further. In contrast, acid phosphatase catalysed almost quantitative conversion of 2CABP into 2CA1P, preferring to hydrolyse only the 5-phosphate. In either case, separation of the 2CA1P from Pi or other products of enzymic hydrolysis was readily accomplished by conventional ion-exchange chromatography or h.p.l.c.