Korean J Nutr.  2012 Oct;45(5):429-436. 10.4163/kjn.2012.45.5.429.

Characteristics of protein from red crab (Chionoecetes japonicus) shell by commercial proteases

Affiliations
  • 1Center of Smart Foods and Drugs and Food Science Institute, Inje University, Gimhae 621-749, Korea. fdsnsong@inje.ac.kr
  • 2Clinical Research Institute CRL. Kyung Hee Universuty Hospital, Seoul 134-727, Korea.
  • 3School of Culinary Art & Baking Technology, Dong-Ju College, Busan 604-080, Korea.
  • 4Division of Marine Environment & Bioscience, Korea Maritime University, Busan 606-791, Korea.

Abstract

This study was performed to examine the characteristics of protein of red crab (Chionoecetes japonicus) shell powder hydrolyzed by commercial proteases. Red crab shell was digested by commercial proteases, such as Protamex (P), Neutrase (N), Flavourzyme (F), Alcalase (A), Protease M (PM) and Protease A (PA). Protein yield analyzed by Biuret assay, absorbance at 280 nm and brix revealed that PA was the enzyme having the highest proteolytic activity. SDS PAGE showed that molecular weight of proteins produced by protease treatments was various and below 150 kDa. Combinational treatment of proteases (PA + P, PA + PM, PA + F, PA + A) was tried whether these increase protein hydrolysis from red crab shell powder compared to a PA single treatment. Soluble protein content was similar, but amino acid concentration by combinational treatments was higher than PA single treatment [PA + P 247.4 mg/g > PA + F (206.4 mg/g) > PA + A (133.4 mg/g) > PA + PM (59.1 mg/g) > PA (54.9 mg/g)]. Amino acid composition by combinational treatments was slightly different. Most abundant essential amino acids were phenylalanine, glycine, alanine, and leucine, whereas tyrosine and cystine were not detected.

Keyword

red crab (Chionoecetes japonicus) shell; protease; amino acid composition; MW

MeSH Terms

Alanine
Amino Acids, Essential
Biuret
Cystine
Electrophoresis, Polyacrylamide Gel
Endopeptidases
Glycine
Hydrolysis
Leucine
Metalloendopeptidases
Molecular Weight
Peptide Hydrolases
Phenylalanine
Proteins
Subtilisins
Tyrosine
Alanine
Amino Acids, Essential
Biuret
Cystine
Endopeptidases
Glycine
Leucine
Metalloendopeptidases
Peptide Hydrolases
Phenylalanine
Proteins
Subtilisins
Tyrosine

Figure

  • Fig. 1 Protein contents of red crab shell hydrolyzed with commercial proteases by Biuret and A280. Data represent the means ± SD, each values being the mean of triplicate assays. Values sharing same superscript are not significantly different by one-way ANOVA followed by Duncan's multiple range at p < 0.05. A: Alcalase, PM: Protease M, N: Neutrase PA: Protease A, P: Protamex, F: Flavourzyme.

  • Fig. 2 °Brix of red crab shell hydrolyzates by commercial proteases. Refer to Fig. 1.

  • Fig. 3 SDS-PAGE patterns of red crab shell hydrolysates by commercial proteases. M: molecular marker. Refer to Fig. 1.

  • Fig. 4 Effects of incubation time and concentration of protease A on the hydrolysis of red crab shell. Panel A: Soluble protein concentrations by Biuret assay. Panel B: Soluble protein concentrations by 280 nm assay. Refer to Fig. 1.

  • Fig. 5 Protein contents of red crab shell hydrolysates by commercial proteases. PA: Protease A, PA + P: Protease A + Protamex, PA + PM: Protease A + Protease M, PA + F: Protease A + Flavourzyme, PA + F: Protease A + Alcalase. Refer to Fig. 1.


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