Environmental Science and Pollution Research

, Volume 25, Issue 12, pp 11987–11998 | Cite as

Recovery and characterization of proteins from pangas (Pangasius pangasius) processing waste obtained through pH shift processing

  • Vijay Kumar Reddy Surasani
  • Tanaji Kudre
  • Rajashekhar V. Ballari
Research Article


Study was conducted to recover proteins from pangas (Pangasius pangasius) processing waste (fillet frames) using pH shift method and to characterize the recovered isolates. pH 2.0 from acidic range and pH 13.0 from alkaline range were found to have maximum protein recovery (p < 0.05). During the recovery process, acidic pH (pH 2.0) was found to have minimal effect on proteins resulting in more stable isolates and strong protein gels. Alkaline pH (pH 13.0) caused protein denaturation resulting in less stable proteins and poor gel network. Both acidic and alkaline-aided processing caused significant (p < 0.05) reductions in total lipid, myoglobin, and pigment content thus by resulting in whiter protein isolates and gels. The content of total essential amino acids increased during pH shift processing, indicating the enrichment of essential amino acids. No microbial counts were detected in any of the isolates prepared using acid and alkaline extraction methods. pH shift processing was found to be promising in the utilization of fish processing waste for the recovery of functional proteins from pangas processing waste thus by reducing the supply demand gap as well pollution problems.


Pangas Fillet frame Protein Acidic Alkaline Isolate 



Authors wish to express their sincere thanks to the Dean, College of Fisheries, GADVASU and University Authorities, GADVASU for their constant support during the work period. Authors also wish to express their thanks to Ms. Manvinder Kaur for her technical help during the preparation of manuscript.


  1. AOAC (2000) Association of official analytical chemists, 16th edn. Washington, DCGoogle Scholar
  2. Azadian M, Moosavi-Nasab M, Abedi E (2012) Comparison of functional properties and SDS-PAGE patterns between fish protein isolate and surimi produced from silver carp. Eur Food Res Technol 235(1):83–90. CrossRefGoogle Scholar
  3. Batista I (1999) Recovery of proteins from fish waste products by alkaline extraction. Eur Food Res Technol 210(2):84–89. CrossRefGoogle Scholar
  4. Batista I, Pires C, Nelhas R (2007) Extraction of sardine proteins by acidic and alkaline solubilisation. Food Sci Technol Int 13(3):189–194. CrossRefGoogle Scholar
  5. Bidlingmeyer BA, Cohen SA, Tarvin TL (1984) Rapid analysis of amino acids using precolumn derivatisation. J Chromatogr 336(1):93–104. CrossRefGoogle Scholar
  6. Chaijan M, Undeland I (2015) Development of a new method for determination of total haem protein in fish muscle. Food Chem 173:1133–1141. CrossRefGoogle Scholar
  7. Chaijan M, Benjakul S, Visessanguan W, Faustman C (2006) Physicochemical properties, gel forming ability and myoglobin content of sardine (Sardinnella gibbosa) and mackerel (Rastrelliger kanagurta) surimi produced by conventional method and alkaline solubilization process. Eur Food Res Technol 222(1-2):58–63. CrossRefGoogle Scholar
  8. Chen YC, Tou JC, Jaczynski J (2007) Protein recovery from rainbow trout (Oncorhynchus mykiss) processing byproducts via isoelectric solubilization/precipitation and its gelation properties as affected by functional additives. J Agric Food Chem 55(22):9079–9088. CrossRefGoogle Scholar
  9. Cortes-Ruis J, Pachero-Aguilar R, Garcia-Sanchez G, Lugo-Sanches ME (2001) Functional characterization of a protein concentrate from bristly sardine made under acidic conditions. J Aquat Food Prod Technol 10(4):5–23. CrossRefGoogle Scholar
  10. Fatin NS, Huda N, David W (2015) Physicochemical properties of Japanese scad (Decapterus Maruadsi) surimi prepared using the acid and alkaline solubilization methods. Int J Sci Eng Res 6(4):141–147Google Scholar
  11. Feng YM, Hultin HO (2001) Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength. J Agric Food Chem 49(8):3927–3935. CrossRefGoogle Scholar
  12. Freitas IR, Gauterio GV, Rios DG, Prentice C (2011) Functionality of protein isolates from argentine anchovy (Engraulis anchoita) residue using pH shift processing. J Food Sci Eng 1:374–378Google Scholar
  13. Freitas IR, Cortez-Wega WR, Prentice C (2015) Evaluation of properties of protein recovered from fish muscle by acid solubilization process. Int Food Res J 22(3):1067–1073Google Scholar
  14. Gehring CK, Gigliotti JC, Moritz JS, Tou JC, Jaczynski J (2010) Functional and nutritional characteristics of proteins and lipids recovered by isoelectric processing of fish by-products and low-value fish: a review. Food Chem 124:422–431CrossRefGoogle Scholar
  15. Haard NF (1992) Control of chemical composition and food quality attributes of cultured fish. Food Res Int 25(4):289–307. CrossRefGoogle Scholar
  16. Hamm R (1994) The influence of pH on the protein net charge in the myofibrillar system. Reciprocal Meat Conf Proc 47:5–9Google Scholar
  17. Harlow E, Lane D (1988) Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, New YorkGoogle Scholar
  18. Huang L, Chen Y, Morrissey MT (1997) Coagulation of fish proteins from frozen fish mince wash water by ohmic heating. J Food Process Eng 20(4):285–300. CrossRefGoogle Scholar
  19. Hultin HO, Kelleher SD (1999) Process for isolating a protein composition from a muscle source and protein composition. US Patent 6,005,073Google Scholar
  20. Hultin HO, Kelleher SD, Feng YM, Kristinsson HG, Richards MP, Undenand IA (2000) High efficiency alkaline protein extraction. US Patent 6,136,959Google Scholar
  21. Huss HH (1983) Fresk Fisk. K valitet Og Holdbarhed. [Fresh fish. Quality and quality changes]. Ministry of Fisheries, Technological laboratory, LyngbyGoogle Scholar
  22. Jafarpour SA, Shabanpour B, Filabadi SS (2013) Biochemical properties of fish protein isolate (FPI) from silver carp (Hypophthalmychthis molitrix) by application of acid-alkali process compared to traditional prepared surimi. Ecopersia 1(3):315–327Google Scholar
  23. Jay JM (1986) Modern food microbiology. Van Nostrand Reinhold Company, New YorkGoogle Scholar
  24. Jongjareonrak A, Rawdkuen S, Chaijan M, Benjakul S, Osako K, Tanaka M (2010) Chemical compositions and characterization of skin gelatin from farmed giant catfish (Pangasianodon gigas). LWT Food Sci Technol 43(1):161–165. CrossRefGoogle Scholar
  25. Kelleher SD, Hultin HO (2000) Functional chicken muscle protein isolates prepared using low ionic strength, acid solubilisation/precipitation. Reciprocal Meat Conf Proc 3:76–81Google Scholar
  26. Kinsella JE (1976) Functional properties of proteins in foods, a survey. CRC Crit Rev Food Sci Nutr 7(3):219–280. CrossRefGoogle Scholar
  27. Kristinsson H, Demir N (2003) Functional fish protein ingredients from fish species of warm and temperate waters: comparison of acid- and alkali-aided processing vs. conventional surimi processing. In: Betchel PJ (ed) Advances in seafood byproducts 2002 Conference Proceedings, Alaska Sea Grant College Program University of Alaska, pp. 277–295Google Scholar
  28. Kristinsson H, Ingadottir B (2006) Recovery and properties of muscle proteins extracted from tilapia (Oreochromis niloticus) light muscle by pH shift processing. J Food Sci 1(3):E132–E141CrossRefGoogle Scholar
  29. Kristinsson HG, Liang Y (2006) Effect of pH-shift processing and surimi processing on Atlantic croaker (Micropogonias undulates) muscle proteins. J Food Sci 71(5):C304–C312. CrossRefGoogle Scholar
  30. Kristinsson H, Theodore AE, Demir N, Ingadottir B (2005) A comparative study between acid- and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle. J Food Sci 70(4):C298–C306CrossRefGoogle Scholar
  31. Kudo G, Okada M, Miyauchi D (1973) Gel-forming capacity of washed and unwashed flesh of some Pacific coast species of fish. Mar Fish Rev 32:10–15Google Scholar
  32. Laemmli UK (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227(5259):680–685. CrossRefGoogle Scholar
  33. Lubana GK, Kaur B, Surasani VKR (2016) Quality changes in fresh rohu (Labeo rohita) cutlets added with fibers from ragi, oat and jowar. Nutr Food Sci 46(4):571–582. CrossRefGoogle Scholar
  34. Marmon SK, Undeland I (2010) Protein isolation from gutted herring (Clupea harengus) using pH-shift processes. J Agric Food Chem 58(19):10480–10486. CrossRefGoogle Scholar
  35. Mutilangi WAM, Panyam D, Kilara A (1996) Functional properties of properties of hydrolysates from proteolysis of heat-denatured whey protein isolate. J Food Sci 61(2):270–274. CrossRefGoogle Scholar
  36. Niki H, Kato T, Deya E, Igarashi S (1985) Recovery of protein from effluent of fish meat in producing surimi and utilization of recovered protein. Nippon Suisan Gakkaishi 51(6):959–964. CrossRefGoogle Scholar
  37. Nolsøe H, Undeland I (2009) The acid and alkaline solubilization process for the isolation of muscle proteins: state of art. Food Bioprocess Technol 2(1):1–27. CrossRefGoogle Scholar
  38. Nolsøe H, Marmon SK, Undeland I (2011) Application of filtration to recover solubilized proteins during ph-shift processing of blue whiting (Micromesistius poutassou); effects on protein yield and qualities of protein isolates. Open Food Sci J 5(1):1–9. CrossRefGoogle Scholar
  39. Panpipat W, Chaijan M (2016) Biochemical and physicochemical characteristics of protein isolates from bigeye snapper (Priacanthus Tayenus) head by-product using pH shift method. Turkish. J Fish Aquat Sci 16:41–50Google Scholar
  40. Rawdkuen S, Sai-Ut S, Khamsorn S, Chaijan M, Benjakul S (2009) Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process. Food Chem 112(1):112–119. CrossRefGoogle Scholar
  41. Reddy SVK (2016) Effect of formulation and processing methods on the quality and acceptability of cutlets made from minced meat of pangas (Pangasius pangasius). SAARC J Agric 14(1):25–36. CrossRefGoogle Scholar
  42. Robinson HW, Hogden CG (1940) The biuret reaction in the determination of serum proteins. J Biol Chem 135:707–725Google Scholar
  43. Sathe SK, Deshpande SS, Salunkhe DK (1982) Functional properties of lupin seed (Supinus mutabilis) proteins and protein concentrates. J Food Sci 7:191–197Google Scholar
  44. Shabanpour B, Etemadian Y, Taghipour B (2015) Physicochemical and rheological parameters changes for determining the quality of surimi and kamaboko produced by conventional, acid and alkaline solubilization process methods from common kilka (Clupeonella cultriventris caspia). Iran J Fish Sci 14(4):826–845Google Scholar
  45. Surasani VKR (2017) Influence of rohu (Labeo rohita) deboning by-product on composition, physical properties and sensorial acceptability of rohu cutlets. Nutr Food Sci 47(3):398–408. CrossRefGoogle Scholar
  46. Surasani VKR, Tyagi A, Kudre T (2017) Recovery of proteins from rohu processing waste using ph shift method: characterization of isolates. J Aquat Food Prod Technol 26(3):356–365. CrossRefGoogle Scholar
  47. Szczesniak AS (2002) Texture is a sensory property. Food Qual Prefer 13(4):215–225. CrossRefGoogle Scholar
  48. Tian Y, Wang W, Yuan C, Zhang L, Liu J, Liu J (2016) Nutritional and digestive properties of protein isolates extracted from the muscle of the common carp using pH shift processing. J Food Process Preserv 41(1):e12847. CrossRefGoogle Scholar
  49. Undeland I, Kelleher SD, Hultin HO (2002) Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process. J Agric Food Chem 50(25):7371–7379. CrossRefGoogle Scholar
  50. WHO/FAO/UNU (2007) Protein and amino requirements in human nutrition. Report of a Joint WHO/FAO/UNU Expert Consultation, WHO Technical Report Series 935, World Health Organization, GenevaGoogle Scholar

Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of Harvest and Post-harvest Technology, College of FisheriesGADVASULudhianaIndia
  2. 2.CSIR-Central Food Technological Research InstituteMysoreIndia

Personalised recommendations