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Journal articles on the topic 'Actinidin'

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Published: 4 June 2021

Last updated: 12 February 2022

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1

Nieuwenhuizen, Niels J., Lesley L. Beuning, Paul W. Sutherland, Neelam N. Sharma, Janine M. Cooney, Lara R. F. Bieleski, Roswitha Schröder, Elspeth A. MacRae, and Ross G. Atkinson. "Identification and characterisation of acidic and novel basic forms of actinidin, the highly abundant cysteine protease from kiwifruit." Functional Plant Biology 34, no. 10 (2007): 946. http://dx.doi.org/10.1071/fp07121.

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Actinidin is a cysteine protease found in Actinidia Lindl. (kiwifruit) species that affects the nutraceutical properties, processing characteristics and allergenicity of the fruit. Given the increased consumption of kiwifruit worldwide and the release of new varieties from different Actinidia species, the expression of actinidin mRNA and protein in a range of kiwifruit tissues was examined. Ten different actinidin mRNAs were identified encoding mature proteins of similar molecular weight (~24 kDa), but with predicted pIs ranging from acidic (pI 3.9) to basic (pI 9.3). In A. deliciosa ‘Hayward’ (green-fleshed kiwifruit) and A. chinensis ‘Hort16A’ and EM4 (gold-fleshed kiwifruit), actinidin mRNAs for acidic and basic proteins were expressed at comparable levels throughout ripening. Actinidin mRNA expression was highest in fruit at harvest, expression decreased as fruit ripened and was much lower in the core compared with outer pericarp tissue. Two-dimensional gel electrophoresis, combined with western analysis and liquid chromatography mass spectrometry (LC-MS) identified low levels of a novel basic actinidin protein in ripe A. deliciosa and A. chinensis fruit. Extremely high levels of an acidic actinidin protein were detected in A. deliciosa fruit and EM4, but this acidic protein appeared to be absent in ‘Hort16A’, the most important commercial cultivar of A. chinensis. Analyses on native gels indicated that both the basic and acidic actinidin isoforms in A. deliciosa were active cysteine proteases. Immunolocalisation showed that actinidin was present in small cells, but not large cells in the outer pericarp of mature A. deliciosa fruit at harvest. Within the small cells, actinidin was localised diffusely in the vacuole, associated with the plasma membrane, and in a layer in the plastids near starch granules. The presence of multiple forms of actinidin and varying protein levels in fruit will impact on the ability to breed new kiwifruit varieties with altered actinidin levels.

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2

Ali, Maysaa Adil. "Optimizing Extraction Conditions of Actinidin from Kiwifruit (Actinidia deliciosa)." Al-Mustansiriyah Journal of Science 28, no. 3 (July 3, 2018): 61. http://dx.doi.org/10.23851/mjs.v28i3.57.

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Kiwifruit (Actinidia deliciosa) is one many fruits that is rich of enzymes like Actinidin. Actinidin is a member of cysteine protease. In this study, different parameters and conditions were tested for optimal Actinidin extraction from kiwifruit. The tested parameters are optimum buffers, pH, Molarity, time, and amounts (gm) of kiwifruit to volume (ml) of buffer ratio. The best buffer for Actinidin extraction from kiwifruit was Sodium phosphate because it gave high activity, with casein as a substrate. The next experiments used sodium phosphate as an optimal buffer for Actinidin extraction and casein as a substrate, detected the optimal Actinidin extraction conditions were carried out at pH 7.0, 0.1 M of sodium phosphate, 2.5 min of extraction time, 1:0.5 (gm of kiwifruit fruit/ v of sodium phosphate buffer) extraction percentage, and 30 min of incubation time. Also this study showed that the maximum enzyme activity for Actinidin extracted from kiwifruit was at pH 7and at 30 min of incubation with casein as substrate.

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3

Kiyat, Warsono El. "Potensi Aktinidin sebagai Pelunak Daging." JURNAL AGRI-TEK : Jurnal Penelitian Ilmu-Ilmu Eksakta 20, no. 1 (May 10, 2019): 6–11. http://dx.doi.org/10.33319/agtek.v20i1.44.

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This study aimed to discuss the activity of actinidin in meat tenderization and to understand the ability of actinidin as a substitute for other tenderizing enzymes such as papain. Actinidin could be found in kiwi fruits with a similar structure and proteolytic activity characteristics to papain. The proteolytic activity of actinidin was found to be able to substitute papain in meat tenderizing without creating an off flavor side effect. However, increasing the actinidin concentration could enhance its proteolytic activity. Besides, actinidin also has the ability to hydrolyze collagen proteins and fibrinogens perfectly compared to papain activity.

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4

Montoya, Carlos A., Shane M. Rutherfurd, Trent D. Olson, Ajitpal S. Purba, Lynley N. Drummond, Mike J. Boland, and Paul J. Moughan. "Actinidin from kiwifruit (Actinidia deliciosacv. Hayward) increases the digestion and rate of gastric emptying of meat proteins in the growing pig." British Journal of Nutrition 111, no. 6 (November 19, 2013): 957–67. http://dx.doi.org/10.1017/s0007114513003401.

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The present study aimed to investigate the effect of dietary actinidin on the kinetics of gastric digestion of beef muscle proteins and on the rate of stomach emptying in growing pigs. For this purpose, 120 pigs (mean body weight 28 (sd2·9) kg) were fed beef muscle protein-based diets containing either actinidin (fresh green kiwifruit pulp or gold kiwifruit pulp supplemented with purified actinidin) or no actinidin (fresh gold kiwifruit pulp or green kiwifruit pulp with inactivated actinidin). Additionally, fifteen pigs were fed with a protein-free diet to determine the endogenous protein flow. Pigs were euthanised at exactly 0·5, 1, 3, 5 and 7 h postprandially (n6 per time point for each kiwifruit diet andn3 for protein-free diet). Stomach chyme was collected for measuring gastric retention, actinidin activity, individual beef muscle protein digestion based on SDS–PAGE and the degree of hydrolysis based on the appearance of free amino groups. The stomach emptying of DM and N was faster when actinidin was present in the diet (P< 0·05): the half gastric emptying time of DM was 137v. 172 min ( ± 7·4 min pooled standard error) for the diets with and without actinidin, respectively. The presence of dietary actinidin in the stomach chyme increased the digestion of beef muscle protein (P< 0·05) and, more specifically, those proteins with a high molecular weight (>34 kDa;P< 0·05). In conclusion, dietary actinidin fed in the form of fresh green kiwifruit increased the rate of gastric emptying and the digestion of several beef muscle proteins.

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5

REID, James D., Syeed HUSSAIN, Suneal K. SREEDHARAN, Tamara S. F. BAILEY, Surapong PINITGLANG, Emrys W. THOMAS, Chandra S. VERMA, and Keith BROCKLEHURST. "Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations." Biochemical Journal 357, no. 2 (July 9, 2001): 343–52. http://dx.doi.org/10.1042/bj3570343.

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The possibility of a slow post-acylation conformational change during catalysis by cysteine proteinases was investigated by using a new chromogenic substrate, N-acetyl-Phe-Gly methyl thionoester, four natural variants (papain, caricain, actinidin and ficin), and stopped-flow spectral analysis to monitor the pre-steady state formation of the dithioacylenzyme intermediates and their steady state hydrolysis. The predicted reversibility of acylation was demonstrated kinetically for actinidin and ficin, but not for papain or caricain. This difference between actinidin and papain was investigated by modelling using QUANTA and CHARMM. The weaker binding of hydrophobic substrates, including the new thionoester, by actinidin than by papain may not be due to the well-known difference in their S2-subsites, whereby that of actinidin in the free enzyme is shorter due to the presence of Met211. Molecular dynamics simulation suggests that during substrate binding the sidechain of Met211 moves to allow full access of a Phe sidechain to the S2-subsite. The highly anionic surface of actinidin may contribute to the specificity difference between papain and actinidin. During subsequent molecular dynamics simulations the P1 product, methanol, diffuses rapidly (over < 8ps) out of papain and caricain but ‘lingers’ around the active centre of actinidin. Uniquely in actinidin, an Asp142–Lys145 salt bridge allows formation of a cavity which appears to constrain diffusion of the methanol away from the catalytic site. The cavity then undergoes large scale movements (over 4.8 Å) in a highly correlated manner, thus controlling the motions of the methanol molecule. The changes in this cavity that release the methanol might be those deduced kinetically.

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6

Praekelt, Uta M., Raymond A. McKee, and Harry Smith. "Molecular analysis of actinidin, the cysteine proteinase of Actinidia chinensis." Plant Molecular Biology 10, no. 3 (1988): 193–202. http://dx.doi.org/10.1007/bf00027396.

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7

Lindahl, P., M. Abrahamson, and I. Björk. "Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin." Biochemical Journal 281, no. 1 (January 1, 1992): 49–55. http://dx.doi.org/10.1042/bj2810049.

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The interaction between recombinant human cystatin C and the cysteine proteinases papain and actinidin was studied by spectroscopic, kinetic and equilibrium methods. The absorption, near-u.v.c.d. and fluorescence-emission difference spectra for the cystatin C-proteinase interactions were all found to be similar to the corresponding spectra for chicken cystatin. The kinetics of binding of cystatin C to the two enzymes were best described by a simple reversible one-step bimolecular mechanism, like the kinetics of the reaction of chicken cystatin with several cysteine proteinases. Moreover, the second-order association rate constants at 25 degrees C, pH 7.4 and I0.15, of 1.1 x 10(7) and 2.4 x 10(6) M-1.s-1 for the reactions of cystatin C with papain and actinidin respectively, were similar to the corresponding rate constants for the chicken inhibitor and close to the value expected for a diffusion-controlled rate. The dissociation equilibrium constants, approx. 11 fM and approx. 19 nM for the binding of cystatin C to papain and actinidin respectively, were also comparable with the dissociation constants for chicken cystatin. The affinity between cystatin C and several inactivated papains or actinidins decreased with increasing size of the inactivating group in a manner similar to that in earlier studies with the chicken inhibitor. Together, these results strongly indicate that the mechanisms of the reactions of cystatin C and chicken cystatin with cysteine proteinases are identical or highly similar, but differ from that of reactions between serine-proteinase inhibitors and their target enzymes. The model for the proteinase-inhibitor interaction, based on the X-ray structure of chicken cystatin, therefore should be largely applicable also to human cystatin C.

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8

Chalabi, Maryam, Fatemeh Khademi, Reza Yarani, and Ali Mostafaie. "Proteolytic Activities of Kiwifruit Actinidin (Actinidia deliciosa cv. Hayward) on Different Fibrous and Globular Proteins: A Comparative Study of Actinidin with Papain." Applied Biochemistry and Biotechnology 172, no. 8 (March 7, 2014): 4025–37. http://dx.doi.org/10.1007/s12010-014-0812-7.

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9

Pr�stamo, Guadalupe. "Actinidin in kiwifruit cultivars." Zeitschrift f�r Lebensmittel-Untersuchung und -Forschung 200, no. 1 (January 1995): 64–66. http://dx.doi.org/10.1007/bf01192910.

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10

Miyazaki-Katamura, Sayaka, Mio Yoneta-Wada, Miyuki Kozuka, Tomohisa Sakaue, Takuya Yamane, Junko Suzuki, Yoshihito Arakawa, and Iwao Ohkubo. "Purification and Biochemical Characterization of Cysteine Protease from Baby Kiwi (Actinidia arguta)." Open Biochemistry Journal 13, no. 1 (August 30, 2019): 54–63. http://dx.doi.org/10.2174/1874091x01913010054.

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Background: It has recently been reported that the fruit, stems and leaves of Actinidia arguta have various potential health effects including an antioxidant effect, anticancer effect, anti-allergic effect and α-glucosidase inhibitory effect. However, little is known about the biochemical properties of cysteine protease in the fruit juice of A. arguta. Methods: Ion exchange chromatography to purify the cysteine protease from the fruit juice of A. arguta, and some synthetic substrates to determinate the enzyme activity were used. Results: Cysteine protease was purified to homogeneity from A. arguta fruit juice by ion exchange chromatography. The molecular weight of the purified enzyme was calculated to be approximately 25,500 by SDS-PAGE in the presence of β-ME. The enzyme rapidly hydrolyzed the substrate Z-Leu-Arg-MCA and moderately hydrolyzed other substrates including Boc-Val-Leu-Lys-MCA, Z-Val-Val-Arg-MCA and Z-Phe-Arg-MCA. Kinetic parameters for these four substrates were determined. The Km, Vmax, Kcat and Kcat/Km values for Z-Leu-Arg-MCA, the most preferentially cleaved by the enzyme, were 100 μM, 63.8 μmoles/mg/min, 27.26 sec-1 and 0.2726 sec-1μM-1, respectively. Furthermore, the activity of the enzyme was strongly inhibited by inhibitors including antipain, leupeptin, E-64, E-64c, kinin-free-LMW kininogen and cystatin C. Those biochemical data indicated that the enzyme was a cysteine protease. The amino acid sequence of the first 21 residues of cysteine protease purified from Actinidia arguta was Val1-Leu-Pro-Asp-Tyr5-Val-Asp-Trp-Arg-Ser10-Ala-Gly-Ala-Val-Val15-Asp-Ile-Lys-Ser-Qln20-Gly. This sequence showed high homology to the sequences of actinidin from Acinidia deliciosa (95.0%) and actinidin from Actinidia eriantha (90%). These three cysteine proteases were thought to be common allied species. Conclusion: The biochemical properties of the enzyme purified from A. arguta fruit juice were determined. These basic data are expected to contribute to the maintenance and improvement of human health as well as to the promotion of protein digestion and absorption through its proteolytic functions.

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11

LEWIS, DEBORAH A., and B. S. LUH. "DEVELOPMENT AND DISTRIBUTION OF ACTINIDIN IN KIWIFRUIT (ACTINIDIA CHINENSIS) AND ITS PARTIAL CHARACTERIZATION." Journal of Food Biochemistry 12, no. 2 (June 1988): 109–16. http://dx.doi.org/10.1111/j.1745-4514.1988.tb00363.x.

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12

Yamanaka, Miho, Tadachika Oota, Tetsuo Fukuda, and Ichiro Nishiyama. "Varietal Difference in Actinidin Concentration and Protease Activity in Fruit Juice of Actinidia Species." NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI 51, no. 9 (2004): 491–94. http://dx.doi.org/10.3136/nskkk.51.491.

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13

Tello-Solís, Salvador R., María Elena Valle-Guadarrama, and Andrés Hernández-Arana. "Purification and circular dichroism studies of multiple forms of actinidin from Actinidia chinensis (kiwifruit)." Plant Science 106, no. 2 (April 1995): 227–32. http://dx.doi.org/10.1016/0168-9452(95)04085-9.

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14

Kowlessur, D., M. O'Driscoll, C. M. Topham, W. Templeton, E. W. Thomas, and K. Brocklehurst. "The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain." Biochemical Journal 259, no. 2 (April 15, 1989): 443–52. http://dx.doi.org/10.1042/bj2590443.

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1. The pH-dependence of the second-order rate constant (k) for the reaction of actinidin (EC 3.4.22.14) with 2-(N'-acetyl-L-phenylalanylamino)ethyl 2'-pyridyl disulphide was determined and the contributions to k of various hydronic states were evaluated. 2. The data were used to assess the consequences for transition-state geometry of providing P2/S2 hydrophobic contacts in addition to hydrogen-bonding opportunities in the S1-S2 intersubsite region. 3. The P2/S2 contacts (a) substantially improve enzyme-ligand binding, (b) greatly enhance the contribution to reactivity of the hydronic state bounded by pKa 3 (the pKa characteristic of the formation of catalytic-site-S-/-ImH+ state) and pKa 5 (a relatively minor contributor in reactions that lack the P2/S2 contacts), such that the major rate optimum occurs at pH 4 instead of at pH 2.8-2.9, and (c) reveal the kinetic influence of a pKa approx. 6.3 not hitherto observed in reactions of actinidin. 4. Possibilities for the interplay of electrostatic effects and binding interactions in both actinidin and papain (EC 3.4.22.2) are discussed.

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15

HUSSAIN, Syeed, Surapong PINITGLANG, Tamara S. F. BAILEY, James D. REID, Michael A. NOBLE, Marina RESMINI, Emrys W. THOMAS, Richard B. GREAVES, Chandra S. VERMA, and Keith BROCKLEHURST. "Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion." Biochemical Journal 372, no. 3 (June 15, 2003): 735–46. http://dx.doi.org/10.1042/bj20030177.

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The acylation and deacylation stages of the hydrolysis of N-acetyl-Phe-Gly methyl thionoester catalysed by papain and actinidin were investigated by stopped-flow spectral analysis. Differences in the forms of pH-dependence of the steady-state and pre-steady-state kinetic parameters support the hypothesis that, whereas for papain, in accord with the traditional view, the rate-determining step is the base-catalysed reaction of the acyl-enzyme intermediate with water, for actinidin it is a post-acylation conformational change required to permit release of the alcohol product and its replacement in the catalytic site by the key water molecule. Possible assignments of the kinetically influential pKa values, guided by the results of modelling, including electrostatic-potential calculations, and of the mechanistic roles of the ionizing groups, are discussed. It is concluded that Asp161 is the source of a key electrostatic modulator (pKa 5.0±0.1) in actinidin, analogous to Asp158 in papain, whose influence is not detected kinetically; it is always in the ‘on’ state because of its low pKa value (2.8±0.06).

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16

Nishiyama, Ichiro, Tetsuo Fukuda, and Tadachika Oota. "Varietal Differences in Actinidin Concentration and Protease Activity in the Fruit Juice of Actinidia arguta and Actinidia rufa." Engei Gakkai zasshi 73, no. 2 (2004): 157–62. http://dx.doi.org/10.2503/jjshs.73.157.

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17

Pickersgill, R. W., P. W. Goodenough, I. G. Sumner, and M. E. Collins. "The electrostatic fields in the active-site clefts of actinidin and papain." Biochemical Journal 254, no. 1 (August 15, 1988): 235–38. http://dx.doi.org/10.1042/bj2540235.

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The active sites of actinidin (EC 3.4.22.14) and papain (EC 3.4.22.2) display different reactivity characteristics to probes targeted at the active-site cysteine residue despite the close structural similarity of their active sites. The calculated electrostatic fields in the active-site clefts of actinidin and papain differ significantly and may explain the reactivity characteristics of these enzymes. Calculation of electrostatic potential also focuses attention on the electrostatic properties that govern formation of the active-site thiolate-imidazolium ion-pair. These calculations will guide the modification of the pH-activity profile of the cysteine proteinases by site-directed mutagenesis.

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18

Martin, Harry, Sarah B. Cordiner, and Tony K. McGhie. "Kiwifruit actinidin digests salivary amylase but not gastric lipase." Food & Function 8, no. 9 (2017): 3339–45. http://dx.doi.org/10.1039/c7fo00914c.

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19

Rødbotten, R., I. Magliano, V. Høst, and E. Veiseth-Kent. "Proteolytic Effects of Marinades Containing Actinidin." Meat and Muscle Biology 1, no. 3 (January 1, 2017): 150. http://dx.doi.org/10.22175/rmc2017.143.

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20

Patel, M., I. S. Kayani, G. W. Mellor, S. Sreedharan, W. Templeton, E. W. Thomas, M. Thomas, and K. Brocklehurst. "Variation in the P2-S2 stereochemical selectivity towards the enantiomeric N-acetylphenylalanylglycine 4-nitroanilides among the cysteine proteinases papain, ficin and actinidin." Biochemical Journal 281, no. 2 (January 15, 1992): 553–59. http://dx.doi.org/10.1042/bj2810553.

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1. Values of the kinetic specificity constant, kcat./Km, for the hydrolysis of N-acetyl-L-phenylalanylglycine 4-nitroanilide (I) and of its D-enantiomer (II) catalysed by ficin (EC 3.4.22.3) and by actinidin (EC 3.4.22.14) at pH 6.0, I 0.1 mol/l, 8.3% (v/v) NN-dimethylformamide and 25 degrees C were determined by using initial-rate data with [S] much less than Km and weighted nonlinear regression analysis as: for ficin, (kcat./Km)L = 271 +/- 6 M-1.s-1, (kcat./Km)D = 2.9 +/- 0.1 M-1.s-1, and for actinidin (kcat./Km)L = 13.3 +/- 0.7 M-1.s-1, (kcat/Km)D = 0.34 +/- 0.01 M-1.s-1.2. These data and analogous values for the corresponding reactions catalysed by papain (EC 3.4.22.2), (kcat./Km)L = 2064 +/- 31 M-1.s-1, (kcat./Km)D = 5.5 +/- 0.1 M-1.s-1, demonstrate marked variation in stereochemical selectivity for substrates (I) and (II) among the three cysteine proteinases with the following values for the index of stereochemical selectivity Iss = (kcat./Km)L/(kcat./Km)D: for papain, 375; for ficin 93; for actinidin 39. 3. Model building suggests ways in which, for the papain-catalysed reactions, binding interactions involving the extended acyl groups of the substrates may need to change as the reaction proceeds from adsorptive complex (ES) to tetrahedral intermediate (THI) before its rate-determining, general acid-catalysed collapse to acylenzyme intermediate. In particular, satisfactory alignment in the catalytic site at the THI stage of the acylation process appears to demand rotation of the substrate moiety about its long axis. 4. The different consequences of this rotation for the L- and D-enantiomers suggest that for closely related systems the greater the extent of this rotational adjustment the greater would be the value of Iss.5. For the actinidin-substrate combinations, model building suggests that even at the ES complex stage of catalysis it is not possible to approach optimized P2-S2 contacts and the three hydrogen-bonding interactions deduced for papain-ligand complexes in the absence of significant movement of protein conformation. Possible binding modes in which some of the interactions deduced for papain are relaxed are discussed. Consideration of postulated binding modes in the various transition states is shown to account for the order of reactivity reflected in values kcat./Km for the four reactions involving papain (Pap) and actinidin (Act) with the L- and D-enantiomeric substrates: Pap-L much greater than Act-L greater than Pap-D much greater than Act-D.(ABSTRACT TRUNCATED AT 400 WORDS)

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21

Podivinsky, E., Kim C. Snowden, J. Keeling, E. Lin, and R. C. Gardner. "EXPRESSION OF ACTINIDIN, A KIWIFRUIT CYSTEINE PROTEASE." Acta Horticulturae, no. 297 (April 1992): 140. http://dx.doi.org/10.17660/actahortic.1992.297.16.

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22

Snowden, K. C., and R. C. Gardner. "Nucleotide sequence of an actinidin genomic clone." Nucleic Acids Research 18, no. 22 (1990): 6684. http://dx.doi.org/10.1093/nar/18.22.6684.

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23

REID, James D., Syeed HUSSAIN, Tamara S. F. BAILEY, Sanjiv SONKARIA, Suneal K. SREEDHARAN, Emrys W. THOMAS, Marina RESMINI, and Keith BROCKLEHURST. "Isomerization of the uncomplexed actinidin molecule: kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation." Biochemical Journal 378, no. 2 (March 1, 2004): 699–703. http://dx.doi.org/10.1042/bj20031318.

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The effects of increasing the content of the aprotic dipolar organic co-solvent acetonitrile on the observed first-order rate constant (kobs) of the pre-steady state acylation phases of the hydrolysis of N-acetyl-Phe-Gly methyl thionester catalysed by the cysteine proteinase variants actinidin and papain in sodium acetate buffer, pH 5.3, were investigated by stopped-flow spectral analysis. With low acetonitrile content, plots of kobs against [S]0 for the actinidin reaction are linear with an ordinate intercept of magnitude consistent with a five-step mechanism involving a post-acylation conformational change. Increasing the acetonitrile content results in marked deviations of the plots from linearity with a rate minimum around [S]0=150 µM. The unusual negative dependence of kobs on [S]0 in the range 25–150 µM is characteristic of a rate-determining isomerization of the free enzyme before substrate binding, additional to the five-step mechanism. There was no evidence for this phenomenon nor for the post-acylation conformational change in the analogous reaction with papain. For this enzyme, however, acetonitrile acts as an inhibitor with approximately uncompetitive characteristics. Possible mechanistic consequences of the differential solvent-perturbed kinetics are indicated. The free enzyme isomerization of actinidin may provide an explanation for the marked difference in sensitivity between this enzyme and papain of binding site–catalytic site signalling in reactions of substrate-derived 2-pyridyl disulphide reactivity probes.

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24

Yuwono, T. "The Presence of Actinidin (Cysteine Protease) and Recombinant Plasmids Carrying the Actinidin Gene Influence the Growth of Saccharomyces Cerevisiae." World Journal of Microbiology and Biotechnology 20, no. 5 (July 2004): 441–47. http://dx.doi.org/10.1023/b:wibi.0000040373.44508.cf.

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25

Kamiyoshihara, Y., D. Kamei, S. Mizuno, K. Watanabe, and A. Tateishi. "Validation of promoter functionality in the upstream region of actinidin-coding gene in kiwifruit (Actinidia chinensis ‘Kohi’)." Acta Horticulturae, no. 1297 (November 2020): 675–80. http://dx.doi.org/10.17660/actahortic.2020.1297.89.

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26

Maddumage, Ratnasiri, Niels J. Nieuwenhuizen, Sean M. Bulley, Janine M. Cooney, Sol A. Green, and Ross G. Atkinson. "Diversity and Relative Levels of Actinidin, Kiwellin, and Thaumatin-Like Allergens in 15 Varieties of Kiwifruit (Actinidia)." Journal of Agricultural and Food Chemistry 61, no. 3 (January 14, 2013): 728–39. http://dx.doi.org/10.1021/jf304289f.

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27

Nam, Seung-Hee. "Changes in the physicochemical quality, functional properties, and actinidin content of kiwifruit (Actinidia chinensis) during postharvest storage." Korean Journal of Food Preservation 23, no. 3 (June 2016): 291–300. http://dx.doi.org/10.11002/kjfp.2016.23.3.291.

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28

Gul, Sheraz, Geoffrey W. Mellor, Emrys W. Thomas, and Keith Brocklehurst. "Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features." Biochemical Journal 396, no. 1 (April 26, 2006): 17–21. http://dx.doi.org/10.1042/bj20051501.

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The temperature-dependences of the second-order rate constants (k) of the reactions of the catalytic site thiol groups of two cysteine peptidases papain (EC 3.4.22.2) and actinidin (EC 3.4.22.14) with a series of seven 2-pyridyl disulphide reactivity probes (R-S-S-2-Py, in which R provides variation in recognition features) were determined at pH 6.7 at temperatures in the range 4–30 °C by stopped-flow methodology and were used to calculate values of ΔS‡, ΔH‡ and ΔG‡. The marked changes in ΔS‡ from negative to positive in the papain reactions consequent on provision of increase in the opportunities for key non-covalent recognition interactions may implicate microsite desolvation in binding site–catalytic site signalling to provide a catalytically relevant transition state. The substantially different behaviour of actinidin including apparent masking of changes in ΔH‡ by an endothermic conformational change suggests a difference in mechanism involving kinetically significant conformational change.

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29

Ballyev, S. B., A. S. Parsanov, E. F. Voznesensky, and F. S. Sharifullin. "The use of actinidin when soaking camel skin." Izvestiya vysshikh uchebnykh zavedenii. Tekhnologiya legkoi promyshlennosti 48, no. 2 (2020): 21–24. http://dx.doi.org/10.46418/0021-3489_2020_48_2_3.

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30

Chen, Yan, Qian Zhang, Xiao Yan Lin, and Xi Yan Liao. "Valuation and Characterization of Actinidin Treatment to Pork." Advanced Materials Research 554-556 (July 2012): 1258–61. http://dx.doi.org/10.4028/www.scientific.net/amr.554-556.1258.

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The paper studied the effect of kiwifruit protease on tenderization of pork and related characterization has been made, the result indicates that pork marinate with kiwifruit protease may lead the degradation of collagen protein and the change of the myofibril fragmentation index (MFI), particle size, viscosity, Warner-Bratzler shear force, area force versus time (Area F-T) as well as microstructure characteristics. Because of the inconvenience of characterization of MFI and soluble collagen, viscosity, particle size analysis, shear force and area F-T can fast and accurate characteristic the changes of tenderizer of pork after marination with kiwifruit protease.

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31

Varughese, Kottayil I., Ying Su, Dean Cromwell, Sadiq Hasnain, and Nguyen Huu Xuong. "Crystal structure of an actinidin-E-64 complex." Biochemistry 31, no. 22 (June 1992): 5172–76. http://dx.doi.org/10.1021/bi00137a012.

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32

Podivinsky, Ellen, Richard L. S. Forster, and Richard C. Gardner. "Nucleotide sequence of actinidin, a kiwi fruit protease." Nucleic Acids Research 17, no. 20 (1989): 8363. http://dx.doi.org/10.1093/nar/17.20.8363.

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33

SAMEJIMA, Kunihiko, Il-Shin CHOE, Makoto ISHIOROSHI, and Tadaaki HAYAKAWA. "Hydrolysis of Muscle Proteins by Actinidin (Kiwifruits Protease)." NIPPON SHOKUHIN KOGYO GAKKAISHI 38, no. 9 (1991): 817–21. http://dx.doi.org/10.3136/nskkk1962.38.817.

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34

Topham, C. M., E. Salih, C. Frazao, D. Kowlessur, J. P. Overington, M. Thomas, S. M. Brocklehurst, M. Patel, E. W. Thomas, and K. Brocklehurst. "Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase Ω. Three-dimensional structure of papaya proteinase Ω deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis." Biochemical Journal 280, no. 1 (November 15, 1991): 79–92. http://dx.doi.org/10.1042/bj2800079.

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1. A model of the three-dimensional structure of papaya proteinase omega, the most basic cysteine proteinase component of the latex of papaya (Carica papaya), was built from its amino acid sequence and the two currently known high-resolution crystal structures of the homologous enzymes papain (EC 3.4.22.2) and actinidin (EC 3.4.22.14). The method used a knowledge-based approach incorporated in the COMPOSER suite of programs and refinement by using the interactive graphics program FRODO on an Evans and Sutherland PS 390 and by energy minimization using the GROMOS program library. 2. Functional similarities and differences between the three cysteine proteinases revealed by analysis of pH-dependent kinetics of the acylation process of the catalytic act and of the reactions of the enzyme catalytic sites with substrate-derived 2-pyridyl disulphides as two-hydronic-state reactivity probes are reported and discussed in terms of the knowledge-based model. 3. To facilitate analysis of complex pH-dependent kinetic data, a multitasking application program (SKETCHER) for parameter estimation by interactive manipulation of calculated curves and a simple method of writing down pH-dependent kinetic equations for reactions involving any number of reactive hydronic states by using information matrices were developed. 4. Papaya proteinase omega differs from the other two enzymes in the ionization characteristics of the common (Cys)-SH/(His)-Im+H catalytic-site system and of the other acid/base groups that modulate thiol reactivity towards substrate-derived inhibitors and the acylation process of the catalytic act. The most marked difference in the Cys/His system is that the pKa for the loss of the ion-pair state to form -S-/-Im is 8.1-8.3 for papaya proteinase omega, whereas it is 9.5 for both actinidin and papain. Papaya proteinase omega is similar to actinidin in that it lacks the second catalytically influential group with pKa approx. 4 present in papain and possesses a catalytically influential group with pKa 5.5-6.0. 5. Papaya proteinase omega occupies an intermediate position between actinidin and papain in the sensitivity with which hydrophobic interaction in the S2 subsite is transmitted to produce changes in transition-state geometry in the catalytic site, a fact that may be linked with differences in specificity in P2-S2 interaction exhibited by the three enzymes.(ABSTRACT TRUNCATED AT 400 WORDS)

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Thomas, M. P., C. Verma, S. M. Boyd, and K. Brocklehurst. "The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin." Biochemical Journal 306, no. 1 (February 15, 1995): 39–46. http://dx.doi.org/10.1042/bj3060039.

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1. The selectivity observed when the potentially general technique for the isolation of fully active forms of cysteine proteinases, covalent chromatography by thiol-disulphide interchange, is applied to chymopapain M and to actinidin was investigated by a combination of experimentation and computer modelling. Neither of these enzymes is able to react with the original Sepharose-GSH-2-dipyridyl disulphide gel, but fully active forms of both enzymes are obtained by using Sepharose-2-hydroxypropyl-2′-dipyridyl disulphide gel, which is both electrically neutral and sterically less demanding than the GSH gel. Electrostatic potential calculations, minimization and molecular-dynamics simulations provide explanations for the unusual, but different, specificities exhibited by actinidin and chymopapain M in the interactions of their active centres with ligands. 2. The unique behaviour of chymopapain M in exerting an almost absolute specificity for substrates with glycine at the P1 position and in resisting inhibition by cystatin was examined by the computer-modelling techniques. A new, modelled, structure of the complete chicken egg-white cystatin molecule based on the crystal structure of a short form of cystatin was deduced as a necessary prerequisite. The results suggest that electrostatic repulsion prevents reaction of actinidin with the GSH gel, whereas a steric ‘cap’ resulting from a unique arginine-65-glutamic acid-23 interaction in chymopapain M prevents reaction of the gel with this enzyme and accounts for the lack of its inhibition by cystatin and its specificity in catalysis. 3. Use of chymopapain M as a structural variant of papain demonstrates the validity of the predictions of Lowe and Yuthavong [Biochem. J. (1971) 124, 107-115] relating to the structural requirements and binding characteristics of the S1 subsite of papain.

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Björk, I., I. Brieditis, and M. Abrahamson. "Probing the functional role of the N-terminal region of cystatins by equilibrium and kinetic studies of the binding of Gly-11 variants of recombinant human cystatin C to target proteinases." Biochemical Journal 306, no. 2 (March 1, 1995): 513–18. http://dx.doi.org/10.1042/bj3060513.

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The interaction between cystatin C variants, in which the evolutionarily conserved Gly-11 residue was substituted by Ala, Glu or Trp, and the cysteine proteinases, papain, ficin, actinidin and cathepsin B, was characterized. The substitutions reduced the affinity of binding in a manner consistent with the Gly residue of the wild-type inhibitor, allowing the N-terminal region to adopt a conformation that was optimal for interaction with target proteinases. Replacement of Gly-11 by Ala resulted in only a 5- to 100-fold reduction in binding affinity. Comparison with the affinities of wild-type cystatin C lacking the N-terminal region indicated that even this small structural change affects the conformation of this region sufficiently to largely abolish its interaction with the weakly binding proteinases, actinidin and cathepsin B. However, the substitution allows interactions of appreciable strength between the N-terminal region and the tightly binding enzymes, papain or ficin. Replacement of Gly-11 with the larger Glu and Trp residues substantially decreased the affinity of binding to all enzymes, from 10(3)- to 10(5)-fold. These substitutions further affect the conformation of the N-terminal region, so that interactions of this region with papain and ficin are also essentially eliminated. The decreased affinities of the three cystatin C variants for papain, ficin and actinidin were due exclusively to increased dissociation rate constants. In contrast, the decreased affinity between cathepsin B and the Ala-11 variant, the only one for which rate constants could be determined with this enzyme, was due almost entirely to a decreased association rate constant. This behaviour is analogous to that observed for forms of cystatin C lacking the N-terminal region and supports the conclusion that the mode of interaction of this region with target proteinases varies with the enzyme as a result of structural differences in the active-site region of the latter.

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37

Brocklehurst, K., S. M. Brocklehurst, D. Kowlessur, M. O'Driscoll, G. Patel, E. Salih, W. Templeton, E. Thomas, C. M. Topham, and F. Willenbrock. "Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics." Biochemical Journal 256, no. 2 (December 1, 1988): 543–58. http://dx.doi.org/10.1042/bj2560543.

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1. The influence on the reactivities of the catalytic sites of papain (EC 3.4.22.2) and actinidin (3.4.22.14) of providing for interactions involving the S1-S2 intersubsite regions of the enzymes was evaluated by using as a series of thiol-specific two-hydronic-state reactivity probes: n-propyl 2-pyridyl disulphide (I) (a ‘featureless’ probe), 2-(acetamido)ethyl 2′-pyridyl disulphide (II) (containing a P1-P2 amide bond), 2-(acetoxy)ethyl 2′-pyridyl disulphide (III) [the ester analogue of probe (II)] and 2-carboxyethyl 2′-pyridyl disulphide N-methylamide (IV) [the retroamide analogue of probe (II)]. Syntheses of compounds (I), (III) and (IV) are reported. 2. The reactivities of the two enzymes towards the four reactivity probes (I)-(IV) and also that of papain towards 2-(N'-acetyl-L-phenylalanylamino)ethyl 2′-pyridyl disulphide (VII) (containing both a P1-P2 amide bond and an L-phenylalanyl side chain as an occupant for the S2 subsite), in up to four hydronic (previously called protonic) states, were evaluated by analysis of pH-dependent stopped-flow kinetic data (for the release of pyridine-2-thione) by using an eight-parameter rate equation [described in the Appendix: Brocklehurst & Brocklehurst (1988) Biochem. J. 256, 556-558] to provide pH-independent rate constants and macroscopic pKa values. The analysis reveals the various ways in which the two enzymes respond very differently to the binding of ligands in the S1-S2 intersubsite regions despite the virtually superimposable crystal structures in these regions of the molecules. 3. Particularly striking differences between the behaviour of papain and that of actinidin are that (a) only papain responds to the presence of a P1-P2 amide bond in the probe such that a rate maximum at pH 6-7 is produced in the pH-k profile in place of the rate minimum, (b) only in the papain reactions does the pKa value of the alkaline limb of the pH-k profile change from 9.5 to approx. 8.2 [the value characteristic of a pH-(kcat./Km) profile] when the probe contains a P1-P2 amide bond, (c) only papain reactivity is affected by two positively co-operative hydronic dissociations with pKI congruent to pKII congruent to 4 and (d) modulation of the reactivity of the common -S(-)-ImH+ catalytic-site ion-pair (Cys-25/His-159 in papain and Cys-25/His-162 in actinidin) by hydronic dissociation with pKa approx. 5 is more marked and occurs more generally in reactions of actinidin than is the case for papain reactions.(ABSTRACT TRUNCATED AT 400 WORDS)

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38

Zhu, Xiaojie, Lovedeep Kaur, and Mike Boland. "Thermal inactivation of actinidin as affected by meat matrix." Meat Science 145 (November 2018): 238–44. http://dx.doi.org/10.1016/j.meatsci.2018.06.027.

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39

Vázquez-Lara, Lourdes, Salvador R. Tello-Solís, Lorena Gómez-Ruiz, Mariano García-Garibay, and Gabriela M. Rodríguez-Serrano. "Degradation of α-Lactalbumin and β-Lactoglobulin by Actinidin." Food Biotechnology 17, no. 2 (January 7, 2003): 117–28. http://dx.doi.org/10.1081/fbt-120023075.

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40

Kaneda, M., Y. Tomita, and N. Tominaga. "Photochemical oxidation of actinidin, a thiol protease fromActinidia chinensis." Experientia 43, no. 3 (March 1987): 318–19. http://dx.doi.org/10.1007/bf01945567.

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41

Grozdanović, Milica M., Branko J. Drakulić, and Marija Gavrović-Jankulović. "Conformational mobility of active and E-64-inhibited actinidin." Biochimica et Biophysica Acta (BBA) - General Subjects 1830, no. 10 (October 2013): 4790–99. http://dx.doi.org/10.1016/j.bbagen.2013.06.015.

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42

Lees, Konarska, Tarr, Polkinghorne, and McGilchrist. "Influence of Kiwifruit Extract Infusion on Consumer Sensory Outcomes of Striploin (M. longissimus lumborum) and Outside Flat (M. biceps femoris) from Beef Carcasses." Foods 8, no. 8 (August 8, 2019): 332. http://dx.doi.org/10.3390/foods8080332.

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Actinidin is a cysteine protease enzyme which occurs in kiwifruit and has been associated with improved tenderness in red meat. This study evaluated the impact of actinidin, derived from kiwifruit, on consumer sensory outcomes for striploin (M. longissimus lumborum) and outside flat (M. biceps femoris). Striploins and outside flats were collected from 87 grass-fed steers. Carcasses were graded to the Meat Standards Australia (MSA) protocols. Striploins and outside flats were then dissected in half and allocated to one of the following two treatments: (1) not infused (control) and (2) infused with a kiwifruit extract (enhanced), and then prepared as grill and roast samples. Grill and roast samples were then aged for 10 or 28 days. Consumer evaluations for tenderness, juiciness, flavor, and overall liking were conducted using untrained consumer sensory panels consisting of 2080 individual consumers, in accordance with the MSA protocols. These scores were then used to calculate an overall eating quality (MQ4) score. Consumer sensory scores for tenderness, juiciness, flavor, overall liking, and MQ4 score were analyzed using a linear mixed-effects model. Kiwifruit extract improved consumer scores for tenderness, juiciness, flavor, overall liking, and MQ4 scores for striploins and outside flat (p < 0.05). These results suggest that kiwifruit extract provides an opportunity to improve eating experiences for consumers.

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43

Rutherfurd, Shane M., Carlos A. Montoya, Maggie L. Zou, Paul J. Moughan, Lynley N. Drummond, and Mike J. Boland. "Effect of actinidin from kiwifruit (Actinidia deliciosa cv. Hayward) on the digestion of food proteins determined in the growing rat." Food Chemistry 129, no. 4 (December 2011): 1681–89. http://dx.doi.org/10.1016/j.foodchem.2011.06.031.

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44

Cavic, Milena, Milica M. Grozdanovic, Aleksandar Bajic, Radmila Jankovic, Pavle R. Andjus, and Marija Gavrovic-Jankulovic. "The effect of kiwifruit (Actinidia deliciosa) cysteine protease actinidin on the occludin tight junction network in T84 intestinal epithelial cells." Food and Chemical Toxicology 72 (October 2014): 61–68. http://dx.doi.org/10.1016/j.fct.2014.07.012.

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45

Pastorello, Elide A., Amedeo Conti, Valerio Pravettoni, Laura Farioli, Federica Rivolta, Raffaella Ansaloni, Marco Ispano, Cristoforo Incorvaia, Maria Gabriella Giuffrida, and Claudio Ortolani. "Identification of actinidin as the major allergen of kiwi fruit." Journal of Allergy and Clinical Immunology 101, no. 4 (April 1998): 531–37. http://dx.doi.org/10.1016/s0091-6749(98)70360-4.

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46

Alexandrakis, Z., G. Katsaros, Ph Stavros, G. Nounesis, and P. Taoukis. "Inactivation Kinetics and Structural Changes of High Pressure Treated Actinidin." International Journal of Agricultural Science and Technology 5, no. 1 (2017): 18–29. http://dx.doi.org/10.12783/ijast.2017.0501.02.

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47

Boyes, Stewart, Peter Strübi, and Hinga Marsh. "Actinidin Levels in Fruit ofActinidiaSpecies and SomeActinidia argutaRootstock–Scion Combinations." LWT - Food Science and Technology 30, no. 4 (June 1997): 379–89. http://dx.doi.org/10.1006/fstl.1996.0193.

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48

REID, JAMES D., SUNEAL SREEDHARAN, AMBROSE COLE, SCOTT MASKELL, ANJUMON BOKTH, EMRYS W. THOMAS, and KEITH BROCKLEHURST. "Detection of a free enzyme isomerisation in actinidin catalysed hydrolysis." Biochemical Society Transactions 26, no. 2 (May 1, 1998): S173. http://dx.doi.org/10.1042/bst026s173.

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49

Keeling, Jeannette, Peter Mexwell, and Richard C. Gardner. "Nucleotide sequence of the promoter region from kiwifruit actinidin genes." Plant Molecular Biology 15, no. 5 (November 1990): 787–88. http://dx.doi.org/10.1007/bf00016129.

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Neria-Rios, Maricela, Jaqueline Padilla-Zuniga, Enrique Garcia-Hernandez, Salvador Tello-Solis, and Rafael Zubillaga. "Binding Energetics Of The Inhibitor Cystatin To The Cysteine Proteinase Actinidin." Protein & Peptide Letters 10, no. 2 (April 1, 2003): 139–45. http://dx.doi.org/10.2174/0929866033479121.

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