Preparation by enzymolysis and bioactivity of iron complex of fish protein hydrolysate (Fe-FPH) from low value fish

Shanggui Deng; Jiancong Huo; Chao Xie

doi:10.1007/s00343-008-0300-4

Your Location：

Home >

Browse articles >

Preparation by enzymolysis and bioactivity of iron complex of fish protein hydrolysate (Fe-FPH) from low value fish

OriginalPaper | Updated：2023-05-16

- Preparation by enzymolysis and bioactivity of iron complex of fish protein hydrolysate (Fe-FPH) from low value fish
- Preparation by enzymolysis and bioactivity of iron complex of fish protein hydrolysate (Fe-FPH) from low value fish
- 海洋湖沼学报（英文） 2008年26卷第3期页码：300-306
- Affiliations：
  
  College of Food and Pharmacology Zhejiang Ocean University
- Author bio：
- Funds：
  
  Supported by National Natural Science Foundation of China (No.30371123) and Science and Technology Department of Zhejiang Province (No. 2007C12013).
- DOI：10.1007/s00343-008-0300-4
  中图分类号：
- 网络首发：2008-08-20，
  
  纸质出版：2008
- Accepted：
Scan QR Code
Preparation by enzymolysis and bioactivity of iron complex of fish protein hydrolysate (Fe-FPH) from low value fish[J]. 海洋湖沼学报（英文）, 2008,26(3):300-306.

Deng, S., Huo, J. & Xie, C. Preparation by enzymolysis and bioactivity of iron complex of fish protein hydrolysate (Fe-FPH) from low value fish., Chin. J. Ocean. Limnol. 26, 300–306 (2008). https://doi.org/10.1007/s00343-008-0300-4
Preparation by enzymolysis and bioactivity of iron complex of fish protein hydrolysate (Fe-FPH) from low value fish[J]. 海洋湖沼学报（英文）, 2008,26(3):300-306. DOI： 10.1007/s00343-008-0300-4.

Deng, S., Huo, J. & Xie, C. Preparation by enzymolysis and bioactivity of iron complex of fish protein hydrolysate (Fe-FPH) from low value fish., Chin. J. Ocean. Limnol. 26, 300–306 (2008). https://doi.org/10.1007/s00343-008-0300-4 DOI：

摘要

Abstract

Preparation of Fe2+ chelate of fish protein hydrolysate (Fe-FPH) obtained from low value fish proteins was introduced and its bioactivity was studied by compound enzymolysis. The optimum conditions for hydrolysate chelating Fe2+ are DH (degree of hydrolysis) at 5%

pH 7.0

20°C and 15 min chelating time for FM (material not being defatted). Four types of Fe-FPH including CA (deposit after chelating)

CB (deposit in 50% of absolute ethanol solution)

CC (suspended deposit in 80% of absolute ethanol solution)

and CD (bottom deposit in 80% of absolute ethanol solution) were fractionated with absolute ethanol from FM. Structural analysis through infra-red spectrum revealed that Fe2+ was combined strongly with amino-group and carboxyl-group in each chelate and each Fe2+ could form two five-member ring structures. All of the four chelates were shown more significant antioxidative activity and can be used as natural hydrophobic and hydrophilic antioxidant. Among all the chelates

the CB possesses the most effective antioxidative activity at 92% as high as that of a-tocopherol. Among all Fe-FPHs

only CD showed the most effective antibacterial activity against Escherichia coli

Staphylococcus aureus

Salmonella typhi

and Bacillus subtilis and can be used as natural antibacterial. It provides a more effective way for utilization of low value fish proteins and key information of Fe-FPH as additive in food industry.

关键词

Keywords

references

Baek, H. H. and K. R. Cadwallader, 1995. Enzymic hydrolysis of crayfish processing by-products. J. Food Sci. 60: 929–934.

Deng, S. G., Z. Y. Peng, F. Chen, P. Yang and T. Wang, 2004a. Amino acids composition and anti-anaemia action of hydrolyzed offal protein from Harengula zunasi Bleeker. Food Chemistry 87(1): 97–102.

Deng, S. G, Z. Y. Peng, F. Chen, Z. J. Chang and P. Yang, 2004b. Hydrolysis dynamics model of protein from Harengula zunasi by compound enzymes. J. Zhanjiang Ocean University 24(4): 28–32. (in Chinese)

Freeman, H. C. and P. L. Hoogland, 1956. Processing of cod and haddock viscera: 1. Laboratory experiments. J. Fish Res. Board Can. 13: 86–877.

Hale, M. B., 1969. Relative activities of commercial-available enzymes in the hydrolysis of fish protein. Food Technol. 23: 107–110.

Hale, M. B., 1974. Using enzymes to make fish protein concentrates. Mar Fish Rev. 36: 15–19.

He, N., C. L. Wang, X. B. Gu, F. P. Lu and L. X. Du, 1999. Study on the optimization of the activity of lactobacillin with well test. J. Tianjin Institute of Light Industry 2: 17–20.

Hevia, P., J. Whitaker and H. S. Olott, 1976. Solubilization of a fish protein concentrate with proteolytic enzymes. J. Agric. Food Chem. 24: 383–390.

Hordur, G. K. and A. R. Barbara, 2000. Kinetics of the hydrolysis of Atlantic salmon (Salmo salar) muscle proteins by alkaline proteases and a visceral serine protease mixture. Process Biochemistry 36: 131–139.

Jeon, Y. J., H. G. Byun and S. K. Kim, 1999. Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes. Process Biochemistry 35: 471–478.

Kim, S. K., Y. J. Jeon, H. G. Byun, Y. T. Kim and C. K. Lee, 1997. Enzymatic recovery of cod frame protein by crude proteinase derived from tuna pyloric caeca. Fish Sci. 63: 421–427.

Kristinsson, H. G. and B. A. Rasco, 2000a. Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. J. Agric. Food Chem. 48: 657–666.

Kristinsson, H. G. and B. A. Rasco, 2000b. Kinetics of the hydrolysis of Atlantic salmon (Salmo salar) muscle proteins by alkaline proteases and a visceral serine protease mixture. Proc. Biochem. 36: 131–139.

Kristinsson, H. G. and B. A. Rasco, 2000c. Fish protein hydrolysates: production, biochemical, and functional properties. CRC Crit Rev Food Sci. Nutr. 40: 43–81.

Liaset, B., E. Lied and M. Espe, 2000. Enzymatic hydrolysis of by-products from the fish-filleting industry; chemical characterisation and nutritional evaluation. J. Sci. Food Agric. 80: 581–589.

McBride J. R., D. R. Idler and R. A. MacLeod, 1961. The liquefaction of British Columbia herring by ensilage, proteolytic enzymes and acid hydrolysis. J. Fish. Res. Board Can. 18: 93–112.

Mohr, V., 1977. Fish protein concentrate production by enzymic hydrolysis. In: Adler-Nissen J, (eds). Biochemical Aspects of New Protein Food. New York: Pergamon. p. 53–62.

Ohkawa, H., N. Ohishi and K. Yagi, 1979. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 95: 351–358.

Osawa, T and M. Namiki, 1981. A novel type of antioxidant isolated from leaf wax of eucalyptus leaves. Agric. Biol. Chem. 45: 735–773.

Quaglia, G. B. and E. Orban, 1987a. Influence of the degree of hydrolysis on the solubility of the protein hydrolsyates from sardine (Sardina pilchardus). J. Sci. Food Agric. 38: 271–276.

Quaglia, G. B. and E. Orban, 1987b. Enzymic solubilisation of proteins of sardine (Sardina pilchardus) by commercial proteases. J. Sci. Food Agric. 38: 263–269.

Sen, D. P., N. V. Sripathy, N. L. Lahiry et al, 1962. Fish hydrolysates I: Rate of hydrolysis of fish flesh with papain. Food Technol. 16(5): 138–140.

Tarr, H. L. A., 1948. Possibilities in developing fisheries by-products. Food Techol. 2: 268–277.

Uchida, K. and S. Kawakishi, 1992. Sequence-dependent reactivity of histidine-containing peptides with copper(II): ascorbate. J. Agric. Food Chem. 40: 13–16.

Zhao, H. G., and M. R. Huang, 1987. Aquatic Product Inspection. 1st edn. Tianjin Science and Technology Press, Tianjin. p. 165–166.

浏览量

Downloads

CSCD

文章被引用时，请邮件提醒。

Submit

工具集

关联资源

Structural characterization of sulfated galactofucan from Undaria pinnatifida and its effect on type 2 diabetic mice

Phylogenetic diversity and bioactivity of culturable deepsea-derived fungi from Okinawa Trough

Extracts of the seaweed Bifurcaria bifurcata display antifungal activity against human dermatophyte fungi

Structural analysis and anti-complement activity of polysaccharides extracted from Grateloupia livida (Harv.) Yamada

Determinants of structure in aquatic non-pelagic protozoan communities