Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 29

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Inhibition of post-mortem fish muscle softening and degradation using legume seed proteinase inhibitors

Singh, Jaspreet, Singh, Balwinder·2020·Journal of Food Science and Technology
DOI 10.1007/s13197-019-04044-6
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1007/s13197-019-04044-6

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 1 references

Research works printed but not linked: 71

  1. Ahmed Z, Donkor O, Street WA, Vasiljevic T (2015) Calpains-and cathepsins-induced myofibrillar changes in post-mortem fish: impact on structural softening and release of bioactive peptides. Trends Food Sci Technol 45(1):130–146 · DOI
  2. Alderton AL, Means WJ, Kalchayanand N, McCormick RJ, Miller KW (2004) Bovine metalloprotease characterization and in vitro connective tissue degradation. J Animal Sci 82(5):1475–1481 · DOI
  3. Ando M, Toyohara H, Sakaguchi M (1992) Post-mortem tenderization of rainbow trout muscle caused by the disintegration of collagen fibers in the pericellular connective tissue. Nippon Suisan Gakk 58(3):567–570 · DOI
  4. Béné C, Barange M, Subasinghe R, Pinstrup-Andersen P, Merino G, Hemre GI, Williams M (2015) Feeding 9 billion by 2050—putting fish back on the menu. Food Secur 7(2):261–274 · DOI
  5. Benhabiles MS, Abdi N, Drouiche N, Lounici H, Pauss A, Goosen MFA, Mameri N (2012) Fish protein hydrolysate production from sardine solid waste by crude pepsin enzymatic hydrolysis in a bioreactor coupled to an ultrafiltration unit. Mat Sci Eng C 32(4):922–928 · DOI
  6. Benjakul S, Karoon S, Suwanno A (1999) Inhibitory effects of legume seed extracts on fish proteinases. J Sci Food Agric 79(13):1875–1881 · DOI
  7. Benjakul S, Visessanguan W, Thummaratwasik P (2000) Inhibition of gel weakening of threadfin bream surimi using Thai legume seed proteinase inhibitors. J Food Biochem 24(5):363–380 · DOI
  8. Boye SW, Lanier TC (1988) Effects of heat-stable alkaline protease activity of Atlantic menhaden (Brevoorti tyrannus) on surimi gels. J Food Sci 53(5):1340–1342 · DOI
  9. Cao MJ, Hara K, Osatomi K, Tachibana K, Izumi T, Ishihara T (1999) Myofibril-Bound Serine Proteinase (MBP) and its degradation of myofibrillar proteins. J Food Sci 64(4):644–647 · DOI
  10. Chéret R, Delbarre-Ladrat C, de Lamballerie-Anton M, Verrez-Bagnis V (2007) Calpain and cathepsin activities in post mortem fish and meat muscles. Food Chem 101(4):1474–1479 · DOI
  11. D’Alessandro A, Zolla L (2013) Meat science: from proteomics to integrated omics towards system biology. J Proteomics 78:558–577 · DOI
  12. Delbarre-Ladrat C, Verrez-Bagnis V, Noël J, Fleurence J (2004) Relative contribution of calpain and cathepsins to protein degradation in muscle of sea bass (Dicentrarchus labrax L.). Food Chem 88(3):389–395 · DOI
  13. Delbarre-Ladrat C, Chéret R, Taylor R, Verrez-Bagnis V (2006) Trends in postmortem aging in fish: understanding of proteolysis and disorganization of the myofibrillar structure. Crit Rev Food Sci Nutr 46(5):409–421 · DOI
  14. Elliott PR, Pei XY, Dafforn TR, Lomas DA (2000) Topography of a 2.0 Å structure of α 1-antitrypsin reveals targets for rational drug design to prevent conformational disease. Protein Sci 9(7):1274–1281 · DOI
  15. Fowler MR, Park JW (2015) Salmon blood plasma: effective inhibitor of protease-laden Pacific whiting surimi and salmon mince. Food Chem 176:448–454 · DOI
  16. García-Carreño FL, Navarrete del Toro MA, Díaz-López M, Hernandez-Cortes MP, Ezquerra JM (1996) Proteinase inhibition of fish muscle enzymes using legume seed extracts. J Food Prot 59(3):312–318 · DOI
  17. Geesink GH, Kuchay S, Chishti AH, Koohmaraie M (2006) μ-Calpain is essential for postmortem proteolysis of muscle proteins. J Anim Sci 84(10):2834–2840 · DOI
  18. Ghaly AE, Dave D, Budge S, Brooks MS (2010) Fish spoilage mechanisms and preservation techniques: review. Am J Appl Sci 7:846–864 · DOI
  19. Ho ML, Chen GH, Jiang ST (2000) Effects of mackerel cathepsins L, L-like and calpain on the degradation of mackerel surimi. Fish Sci 66(3):558–568 · DOI
  20. Hopkins DL, Thompson JM (2002) The degradation of myofibrillar proteins in beef and lamb using denaturing electrophoresis-an overview. J Muscle Foods 13(2):81–102 · DOI
  21. Hossain MI, Itoh Y, Morioka K, Obatake A (2001) Inhibiting effect of polymerization and degradation of myosin heavy chain during preheating at 30 °C and 50 °C on the gel-forming ability of Walleye pollack surimi. Fisheries Sci 67(4):718–725 · DOI
  22. Hu Y, Morioka K, Itoh Y (2010) Participation of cysteine protease cathepsin L in the gel disintegration of red bulleye (Priacanthus macracanthus) surimi gel paste. J Sci Food Agric 90:370–375 · DOI
  23. Hu Y, Yu H, Dong K, Yang S, Ye X, Chen S (2014) Analysis of the tenderisation of jumbo squid (Dosidicus gigas) meat by ultrasonic treatment using response surface methodology. Food Chem 160:219–225 · DOI
  24. Huang M, Huang F, Xu X, Zhou G (2009) Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging. Food Chem 115(1):181–186 · DOI
  25. Ishida N, Yamashita M, Koizumi N, Terayama M, Ineno T, Minami T (2003) Inhibition of post-mortem muscle softening following in situ perfusion of protease inhibitors in tilapia. Fisheries Sci 69(3):632–638 · DOI
  26. Kemp CM, Sensky PL, Bardsley RG, Buttery PJ, Parr T (2010) Tenderness—an enzymatic view. Meat Sci 84(2):248–256 · DOI
  27. Klomklao S, Benjakul S (2015) Effect of trypsin inhibitor in adzuki bean (Vigna angularis) on proteolysis and gel properties of threadfin bream (Nemipterus bleekeri). LWT - Food Sci Technol 63(2):906–911 · DOI
  28. Koohmaraie M, Geesink GH (2006) Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci 74(1):34–43 · DOI
  29. Kristoffersen S, Tobiassen T, Esaiassen M, Olsson GB, Godvik LA, Seppola MA, Olsen RL (2006) Effects of pre-rigour filleting on quality aspects of Atlantic cod (Gadus morhua L.). Aquac Res 37(15):1556–1564 · DOI
  30. Kudre T, Benjakul S, Kishimura H (2013) Effects of protein isolates from black bean and mungbean on proteolysis and gel properties of surimi from sardine (Sardinella albella). LWT - Food Sci Technol 50:511–518 · DOI
  31. Kunimoto M, Hamada-Sato N, Kato N (2016) Main protein components in frozen surimi contributed to heat-induced gel formation. Int Food Res J 23(5):1939–1948
  32. Lafarga T, Hayes M (2014) Bioactive peptides from meat muscle and by-products: generation, functionality and application as functional ingredients. Meat Sci 98(2):227–239 · DOI
  33. Law RH, Zhang Q, McGowan S, Buckle AM, Silverman GA, Wong W, Rosado CJ, Langendorf CG, Pike RN, Bird PI, Whisstock JC (2006) An overview of the serpin superfamily. Genome Biol 7(5):216 · DOI
  34. Lonergan EH, Zhang W, Lonergan SM (2010) Biochemistry of postmortem muscle—lessons on mechanisms of meat tenderization. Meat Sci 86(1):184–195 · DOI
  35. López FM, Dıaz IM, López MD, López FA (1999) Inhibition of digestive proteases by vegetable meals in three fish species; seabream (Sparus aurata), tilapia (Oreochromis niloticus) and African sole (Solea senegalensis). Comp Biochem Physiol B: Biochem Mol Biol 122(3):327–332 · DOI
  36. Luo Y, Kuwahara R, Kaneniwa M, Murata Y, Yokoyama M (2004) Effect of soy protein isolate on gel properties of Alaska pollock and common carp surimi at different setting conditions. J Sci Food Agric 84(7):663–671 · DOI
  37. Martín-Cabrejas MA, Aguilera Y, Pedrosa MM, Cuadrado C, Hernández T, Díaz S, Esteban RM (2009) The impact of dehydration process on antinutrients and protein digestibility of some legume flours. Food Chem 114(3):1063–1068 · DOI
  38. Mazorra-Manzano MA, Ramírez-Suárez JC, Moreno-Hernández JM, Pacheco-Aguilar R (2018) Seafood proteins. In: Yada RY (ed) Proteins in food processing. Woodhead Publishing, Cambridge, pp 445–475 · DOI
  39. Ohkubo M, Miyagawa K, Osatomi K, Hara K, Nozaki Y, Ishihara T (2004) Purification and characterization of myofibril-bound serine protease from lizard fish (Saurida undosquamis) muscle. Comp Biochem Physiol B: Biochem Mol Biol 137(1):139–150 · DOI
  40. Olson ST, Gettins PG (2011) Regulation of proteases by protein inhibitors of the serpin superfamily. Prog Mol Biol Transl Sci 99:185–240 · DOI
  41. Ouali A, Herrera-Mendez CH, Coulis G, Becila S, Boudjellal A, Aubry L, Sentandreu MA (2006) Revisiting the conversion of muscle into meat and the underlying mechanisms. Meat Sci 74(1):44–58 · DOI
  42. Ouali A, Gagaoua M, Boudida Y, Becila S, Boudjellal A, Herrera-Mendez CH, Sentandreu MA (2013) Biomarkers of meat tenderness: present knowledge and perspectives in regards to our current understanding of the mechanisms involved. Meat Sci 95(4):854–870 · DOI
  43. Oujifard A, Benjakul S, Ahmad M, Seyfabadi J (2012) Effect of bambara groundnut protein isolate on autolysis and gel properties of surimi from threadfin bream (Nemipterus bleekeri). LWT - Food Sci Technol 47:261–266 · DOI
  44. Pereira PMDCC, Vicente AFDRB (2013) Meat nutritional composition and nutritive role in the human diet. Meat Sci 93(3):586–592 · DOI
  45. Prato E, Biandolino F (2015) The contribution of fish to the Mediterranean diet. In: Preedy VR, Watson RR (eds) The Mediterranean diet. Academic Press, Cambridge, pp 165–174 · DOI
  46. Prato E, Biandolino F, Parlapiano I, Giandomenico S, Denti G, Calò M, Spada L, Di Leo A (2019) Proximate, fatty acids and metals in edible marine bivalves from Italian market: beneficial and risk for consumers health. Sci Total Environ 648:153–163 · DOI
  47. Pushparajan N, Varadharajan D, Soundarapandian P (2013) Microbial studies of prepared curries stored in tin free steel cans. J Food Process Technol 4(6):1000238
  48. Ramírez JA, García-Carreño EL, Morales OG, Sanchez A (2002) Inhibition of Modori-associated proteinases by legume seed extracts in surimi production. J Food Sci 67(2):578–581 · DOI
  49. Schechter NM, Plotnick MI (2004) Measurement of the kinetic parameters mediating protease–serpin inhibition. Methods 32(2):159–168 · DOI
  50. Sentandreu MA, Coulis G, Ouali A (2002) Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends Food Sci Technol 13(12):400–421 · DOI
  51. Silverman GA, Bird PI, Carrell RW, Coughlin PB, Gettins PG, Irving JI, Lomas DA, Luke CJ, Moyer RW, Pemberton PA, Remold-O’Donnell E, Salvesen GS, Travis J, Whisstock JC (2001) The serpins are an expanding superfamily of structurally similar but funtionally diverse proteins: evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J Biol Chem 276(36):33293–33296 · DOI
  52. Singh A, Benjakul S (2018) Proteolysis and its control using protease inhibitors in fish and fish products: a review. Compr Rev Food Sci Food Saf 17:496–509 · DOI · Paper page
  53. Singh B, Singh JP, Shevkani K, Singh N, Kaur A (2017a) Bioactive constituents in pulses and their health benefits. J Food Sci Technol 54(4):858–870 · DOI
  54. Singh B, Singh JP, Kaur A, Singh N (2017b) Phenolic composition and antioxidant potential of grain legume seeds: a review. Food Res Int 101:1–16 · DOI
  55. Singh B, Singh JP, Singh N, Kaur A (2017c) Saponins in pulses and their health promoting activities: a review. Food Chem 233:540–549 · DOI
  56. Sriket C (2014) Proteases in fish and shellfish: role on muscle softening and prevention. Int Food Res J 21:433–445
  57. Sriket C, Benjakul S, Visessanguan W, Kishimura H (2011a) Collagenolytic serine protease in fresh water prawn (Macrobrachium rosenbergii): characteristics and its impact on muscle during iced storage. Food Chem 124(1):29–35 · DOI
  58. Sriket C, Benjakul S, Visessanguan W, Hara K (2011b) Effect of legume seed extracts on the inhibition of proteolytic activity and muscle degradation of fresh water prawn (Macrobrachium rosenbergii). Food Chem 129(3):1093–1099 · DOI
  59. Stoknes I, Rustad T (1995) Proteolytic activity in muscle from Atlantic salmon (Salmo salar). J Food Sci 60(4):711–714 · DOI
  60. Suarez MD, Abad M, Ruiz-Cara T, Estrada JD, García-Gallego M (2005) Changes in muscle collagen content during post mortem storage of farmed sea bream (Sparus aurata): influence on textural properties. Aquac Int 13(4):315–325 · DOI
  61. Sulikowski T, Bauer BA, Patston PA (2002) α1-Proteinase inhibitor mutants with specificity for plasma kallikrein and C1 s but not C1. Protein Sci 11(9):2230–2236 · DOI
  62. Suwansakornkul P, Itoh Y, Hara S, Obatake A (1993) Identification of proteolytic activities of gel-degradation factors in three lizard fish species. Nippon Suisan Gakk 59(6):1039–1045 · DOI
  63. Taylor R, Fjaera S, Skjervold P (2002) Salmon fillet texture is determined by myofiber–myofiber and myofiber–myocommata attachment. J Food Sci 67(6):2067–2071 · DOI
  64. Tsuchiya H, Seki N (1991) Action of calpain on α-actinin within and isolated from carp myofibrils. Nippon Suisan Gakk 57(6):1133–1139 · DOI
  65. Wu JL, Lu BJ, Du MH, Liu GM, Hara KJ, Su WJ, Cao MJ (2008) Purification and characterization of gelatinase-like proteinases from the dark muscle of common carp (Cyprinus carpio). J Agric Food Chem 56(6):2216–2222 · DOI
  66. Wu GP, Chen SH, Liu GM, Yoshida A, Zhang LJ, Su WJ, Cao MJ (2010) Purification and characterization of a collagenolytic serine proteinase from the skeletal muscle of red sea bream (Pagrus major). Comp Biochem Physiol B: Biochem Mol Biol 155(3):281–287
  67. Xiong GY, Zhang LL, Zhang W, Wu J (2012) Influence of ultrasound and proteolytic enzyme inhibitors on muscle degradation, tenderness and cooking loss of hens during aging. Czech J Food Sci 30(3):195–205 · DOI
  68. Yamashita M, Konagaya S (1991) Hydrolytic action of salmon cathepsins B and L to muscle structural proteins in respect of muscle softening. Nippon Suisan Gakk 57(10):1917–1922 · DOI
  69. Yongsawatdigul J, Park JW, Virulhakul P, Viratchakul S (2000) Proteolytic degradation of tropical tilapia surimi. J Food Sci 65(1):129–133 · DOI
  70. Yu D, Wu L, Regenstein JM, Jiang Q, Yang F, Xu Y, Xia W (2019) Recent advances in quality retention of non-frozen fish and fishery products: a review. Crit Rev Food Sci Nutr. https://doi.org/10.1080/10408398.2019.1596067 · DOI
  71. Zamora F, Aubry L, Sayd T, Lepetit J, Lebert A, Sentandreu MA, Ouali A (2005) Serine peptidase inhibitors, the best predictor of beef ageing amongst a large set of quantitative variables. Meat Sci 71(4):730–742 · DOI

Cited by

Metadata

Authors
Singh, J., & Singh, B.
ORCID
Singh, Balwinder
Venue
Journal of Food Science and Technology
Publisher
Springer Science and Business Media LLC
Published
2019-08-24
Volume
57
Issue
1
Pages
1-11
ISSN
  • 0022-1155
  • 0975-8402
DOI
10.1007/s13197-019-04044-6
Cited by
29
References
1
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.