Skip to main content
SpringerLink
Log in

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

  • Original Article
  • Published:
Journal of Food Science and Technology Aims and scope Submit manuscript

Abstract

This study was conducted to evaluate the kinetic characteristics of proteolytic activity of proteases on Channa striatus protein fractions. Degree of hydrolysis (DH), amino acid composition and kinetic parameters of sarcoplasmic and myofibrillar proteins were investigated when incubated with proteinase K and thermolysin, separately. After 30 min incubation with proteases, a decrease in DH of sarcoplasmic protein was observed whereas, hydrolysis of myofibrillar protein with proteases took 2 h with an increase in DH. The major amino acids were glutamic acid (16.6%) in thermolysin- myofibrillar hydrolysate followed by aspartic acid (11.1%) in sarcoplasmic protein fraction with no enzyme treatment and lysine (10%) in thermolysin-myofibrillar hydrolysate. The apparent Michaelis constant of proteinase K was lower than thermolysin for both sarcoplasmic and myofibrillar proteins. However, rate of turnover and enzyme efficiency suggested that sarcoplasmic and myofibrillar proteins are suitable substrates for proteinase K and thermolysin hydrolytic reaction, respectively.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3

Similar content being viewed by others

References

  • Alaiz M, Navarro JL, Girón J, Vioque E (1992) Amino acid analysis by high-performance liquid chromatography after derivatization with diethyl ethoxymethylenemalonate. J Chromatogr 591:181–186

    Article  CAS  Google Scholar 

  • Arihara K (2006) Functional properties of bioactive peptides derived from meat proteins. In: Advanced technologies for meat processing. CRC Press, Boca Raton, 245–274

  • Biesalski HK (2005) Meat as a component of a healthy diet—are there any risks or benefits if meat is avoided in the diet? Meat Sci 70:509–524

    Article  Google Scholar 

  • Bisswanger H (2004) Enzyme reaction. In: Practical enzymology. Wiley, Germany, 7–164

  • Chelh I, Gatellier P, Santé-Lhoutellier V (2007) Characterization of fluorescent Schiff bases formed during oxidation of pig myofibrils. Meat Sci 76:210–215

    Article  CAS  Google Scholar 

  • Church FC, Swaisgood HE, Porter DH, Catignani GL (1983) Spectrophotometric assay using O-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J Dairy Sci 66:1219–1227

    Article  CAS  Google Scholar 

  • Eisenthal R, Danson MJ, Hough DW (2007) Catalytic efficiency and kcat/Km: a useful comparator. Trends Biotechnol 25:247–249

    Article  CAS  Google Scholar 

  • Ghassem M, Khoo TC, Feni HS, Babji AS, Tengku Rozaina TM (2009) Proximate composition, fatty acid and amino acid profiles of selected Malaysian freshwater fish. Malay Fish J 8:7–16

    Google Scholar 

  • Hay JD, Currie RW, Wolf FH, Sanders ESB (1973) The effect of post mortem aging on chicken muscle fibrils. J Food Sci 38:981–990

    Article  Google Scholar 

  • Kim SK, Lee HC, Byun HG, Jeon YJ (1996) Isolation and characterization of antioxidative peptides from enzymatic hydrolysates of yellowfin sole skin gelation. J Korean Fish Soc 29:246–255

    CAS  Google Scholar 

  • Kraus E, Femfert U (1976) Proteinase K from the mold Tritirachium album Limber. Specificity and mode of action. Hoppe Seylers Z Physiol Chem 357:937–947

    Article  CAS  Google Scholar 

  • Kristinsson HG, Rasco BA (2000) Fish protein hydrolysates: production, biochemical and functional properties. Crit Rev Food Sci 32:1–39

    Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275

    CAS  Google Scholar 

  • Mackie IM (1982) Fish protein hydrolysates. Process biochem 17:26–31

    CAS  Google Scholar 

  • Mat Jais AM (2007) Pharmacognosy and pharmacology of Haruan (Channa striatus), a medicinal fish with wound healing properties. Bol Latinoam Caribe Plant Med Aromat 6:52–60

    Google Scholar 

  • Ming H, Feng H, Xinglian X, Guanghong Z (2009) Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging. Food Chem 115:181–186

    Article  Google Scholar 

  • Morzel M, Gatellier PH, Sayd T, Renerre M, Laville E (2006) Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins. Meat Sci 73:536–543

    Article  CAS  Google Scholar 

  • Murray BA, FitzGerald RJ (2007) Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Curr Pharm Des 13(8):773–791

    Article  CAS  Google Scholar 

  • Nagai T, Suzuki N, Nagashima T (2006) Antioxidative activities and angiotensin I-converting enzyme inhibitory activities of enzymatic hydrolysates from commercially available Kamaboko species. J Food Sci Technol 12:335–346

    CAS  Google Scholar 

  • Nakagawa T, Watabe S, Hashimoto K (1988) Identification of three major components in fish sarcoplasmic proteins. Nippon Suisan Gakk 54(6):999–1004

    Article  CAS  Google Scholar 

  • Nazeer RA, Divya Prabha KR, Sampath Kumar NS, Jai Ganesh R (2011) Isolation of antioxidant peptides from clam, Meretrix casta (Chemnitz). J Food Sci Technol. doi:10.1007/s13197-011-0395-z

  • Qian S, Huixing S, Yongkang L (2011) Antioxidant activity of hydrolysates and peptide fractions derived from porcine haemoglobin. J Food Sci Technol 48(1):53–60

    Article  Google Scholar 

  • Sairam S, Krishna AGG, Urooj A (2010) Physico-chemical characteristics of defatted rice bran and its utilization in a bakery product. J Food Sci Technol 48(4):478–483

    Article  Google Scholar 

  • Salami M, Yousefi R, Ehsani MR, Dalgalarrondo MI, Chobert JM, Haertlé T, Razavi SH, Saboury AA, Niasari-Naslaji A, Moosavi-Movahedi AA (2008) Kinetic characterization of hydrolysis of camel and bovine milk proteins by pancreatic enzymes. Int Dairy J 18:1097–1102

    Article  CAS  Google Scholar 

  • Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368–379

    Article  CAS  Google Scholar 

  • Shargel L, Wu-Pong S, Yu ABC (2005) Applied Biopharmaceutics and Pharmacokinetics, 5th edn. Appleton & Lange Reviews/McGraw-Hill, New York

    Google Scholar 

  • Skaara T, Regenstein JM (1990) The structure and properties of myofibrillar proteins in beef, poultry, and fish. J Muscle Foods 1:269–291

    Article  Google Scholar 

  • Taylor WJ, Diers-Caviness MH (2003) A textbook of the clinical application of therapeutic drug monitoring. Abbott Laboratories Ltd, Diagnostic Division, Irving

    Google Scholar 

  • Thiansilakul Y, Benjakul S, Shahidi F (2007) Compositions, functional properties and antioxidative activity of protein hydrolysates prepared from round scad (Decapterus maruadsi). Food Chem 103:1385–1394

    Article  CAS  Google Scholar 

  • Wayne SI, Fruton JS (1983) Thermolysin-catalyzed peptide bond synthesis. Proc Natl Acad Sci 80:3241–3244

    Article  CAS  Google Scholar 

  • Zuraini A, Somchit MN, Solihah MH, Goh YM, Arifah AK, Zakaria MS, Somchit N, Rajion MA, Zakaria ZA, Mat Jais AM (2006) Fatty acid and amino acid composition of three local Malaysian Channa spp fish. Food Chem 97:674–678

    Article  CAS  Google Scholar 

Download references

Acknowledgment

The authors would like to thank the Fisheries Research Institute, Batu Maung, Penang, for the grant STGL-009-2008.

Author information

Authors and Affiliations

  1. School of Chemical Sciences and Food Technology, Universiti Kebangsaan Malaysia, 43600, Bangi, Selangor, Malaysia

    Masomeh Ghassem, See Siau Fern, Mamot Said & Abdul Salam Babji

  2. School of biosciences and biotechnology, Universiti Kebangsaan Malaysia, 43600, Bangi, Selangor, Malaysia

    Zainon Mohd Ali

  3. Fishery Research Institute, 11960, Batu Muang, Penang, Malaysia

    Saadiah Ibrahim

Authors
  1. Masomeh Ghassem
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. See Siau Fern
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Mamot Said
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Zainon Mohd Ali
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Saadiah Ibrahim
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Abdul Salam Babji
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Masomeh Ghassem.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ghassem, M., Fern, S.S., Said, M. et al. Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates. J Food Sci Technol 51, 467–475 (2014). https://doi.org/10.1007/s13197-011-0526-6

Download citation

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s13197-011-0526-6

Keywords

Search

Navigation