Preventive Nutrition and Food Science

The Korean Society of Food Science and Nutrition (한국식품영양과학회)
권호 표지
DOI QR코드

DOI QR Code

Optimization of Alcalase for Krill Byproduct Hydrolysis and Antioxidative Activities by Response Surface Methodology

  • Kim, Kyoung-Myo (Department of Practical Korea Culinary, Sorabol College) ;
  • Lee, Da-Sun (Department of Food Science & Technology, Pukyong National University) ;
  • Nam, Min-Hee (Department of Food Science & Technology, Pukyong National University) ;
  • Yoo, Hong-Seok (Department of Food Science & Technology, Pukyong National University) ;
  • Kim, Seon-Bong (Department of Food Science & Technology, Pukyong National University) ;
  • Chun, Byung-Soo (Department of Food Science & Technology, Pukyong National University) ;
  • Lee, Yang-Bong (Department of Food Science & Technology, Pukyong National University)
  • Received : 2010.10.26
  • Accepted : 2010.12.12
  • Published : 2010.12.31
Download PDF
⟨ Previous Next ⟩

Abstract

Krill byproduct was hydrolyzed with Alcalase 2.4L to produce functional ingredients for high antioxidative activities against 1,1-dimethyl-2-picryl-hydrazyl (DPPH) radical and Fe. The objective of this study was to investigate the optimum condition for degree of hydrolysis and antioxidative activity of enzymatic hydrolysate produced with the commercial Alcalase using response surface methodology (RSM) with a central composite rotatable design (CCRD). The ranges of independent variables were pH 7.6~10.4 for initial pH and $50.9{\sim}79.1^{\circ}C$ for hydrolysis temperature and their dependent variables were degree of hydrolysis, Brix, amount of phenolic compounds, DPPH-scavenging activity and Fe-chelating activity. RSM with CCRD was well designed to investigate the optimum condition for functional ingredients with high antioxidative activities using Alcalase 2.4L because of their high $R^2$ values of the range of 0.93~0.99 except the $R^2$ value of 0.50 for the amount of total phenolic compounds. The optimum hydrolysis conditions were pH 9.5 and $62^{\circ}C$ for degree of hydrolysis (DH) and pH 9.1 and $64^{\circ}C$ for DPPH-scavenging activity by response surface methodology. The yield of DH and DPPH-scavenging activity were $14.1{\pm}0.5%$ and $10.5{\pm}0.2%$, respectively. It is advantageous to determine the optimum hydrolysis conditions of krill and its by-products for the creation of different kinds of food products, as well as to increase the usage of marine protein sources.

Keywords

References

  1. Robin MR. 1988. Euphausia super－A critical review of estimates of annual production. Comp Biochem Physiol 90B: 499-505.
  2. Suh HL. 1988. Review on the reproduction feeding and longevity of the antarctic krill, Euphausia super. Bull Korean Fish Soc 21: 303-310.
  3. Guerard F, Guimas L, Binet A. 2002. Production of tuna waste hydrolysates by a commercial neutral protease preparation. J Mol Catal B Enzym 19-20: 489-498. https://doi.org/10.1016/S1381-1177(02)00203-5
  4. Kim E, Cha Y. 1996. Development of functional seasoning agents from skipjack preparation by-product with commercial proteases: I. Processing of hydrolysate from skipjack processing by-products with protease treatment. J Korean Soc Food Sci Nutr 25: 608-616.
  5. Benjakul S, Morrissey MT. 1997. Protein hydrolysates form Pacific whiting solid wastes. J Agric Food Chem 45: 3423-3430. https://doi.org/10.1021/jf970294g
  6. Guerard F, Sumaya-Martinez MT, Laroque D, Chabeaud A, Dufosse L. 2007. Optimization of free radical scavenging activity by response surface methodology in the hydrolysis of shrimp processing discards. Process Biochem 42: 1486-1491. https://doi.org/10.1016/j.procbio.2007.07.016
  7. Gildberg A, Stenberg E. 2001. A new process for advanced utilisation of shrimp waste. Process Biochem 36: 809-812. https://doi.org/10.1016/S0032-9592(00)00278-8
  8. Haslaniza H, Maskat MY, Wan Aida WM, Mamot S. 2010. The effect of enzyme concentration, temperature and incubation time on nitrogen content and degree of hydrolysis of protein precipitate from cockle (Anadara granosa) meat wash water. Int Food Res J 17: 147-152.
  9. Whang HJ, Han WS, Yoon KR. 2001. Quantitative analysis of total phenolic content in apple. Korean J Anal Sci Technol 14: 377-383.
  10. Slizyte R, Mozuraityte R, Martonez-Alvarez O, Falch E, Fouchereau-Peron M, Rustad T. 2009. Functional, bioactive and antioxidative properties of hydrolysates obtained from cod (Gadusmorhua) backbones. Process Biochem 44: 668-677. https://doi.org/10.1016/j.procbio.2009.02.010
  11. Raghavan S, Kristinsson HG. 2008. Antioxidative efficacy of alkali-treated tilapia protein hydrolysates: A comparative study of five enzymes. J Agric Food Chem 56: 1434-1441. https://doi.org/10.1021/jf0733160
  12. Jang HJ, Kim MC, Jung EJ, Shin EC, Lee SH, Lee SJ, Kim SB, Lee YB. 2005. Optimization and flavor quality of enzymatic hydrolysate from dark muscle of skipjack. J Korean Soc Food Sci Nutr 10: 11-16. https://doi.org/10.3746/jfn.2005.10.1.011
  13. Novozymes A/S. 2010. Alcalase Food Grade. Product Sheet. Novo Industries A/S. Bagsvaerd, Denmark.
  14. Lee YB, Raghavan S, Nam MH, Choi MA, Hettiarachchy NS, Kristinsson HG, Marshall MR. 2009. Optimization of enzymatic hydrolysis with Cryotin F on antioxidative activities for shrimp hydrolysate using response surface methodology. J Food Sci Nutr 14: 323-328. https://doi.org/10.3746/jfn.2009.14.4.323
  15. Xia SH, Wang Z, Xu SY. 2007. Characteristics of Bellamya purificata snail foot protein and enzymatic hydrolysates. Food Chem 101: 1188-1196. https://doi.org/10.1016/j.foodchem.2006.03.031
  16. Holanda HD, Netto FM. 2006. Recovery of components from shrimp (Xiphopenaeus kroyeri) processing waste by enzymatic hydrolysis. J Food Sci 71: C298-C303. https://doi.org/10.1111/j.1750-3841.2006.00040.x
  17. Guerard F, Dufossea L, La Broisea DD, Bineta A. 2001. Enzymatic hydrolysis of proteins from yellowfin tuna (Thunnus albacares) wastes using Alcalase. J Mol Catal B Enzym 11: 1051-1059. https://doi.org/10.1016/S1381-1177(00)00031-X