Chemical and Biochemical Hydrolysis of Persian Sturgeon (Acipenser persicus) Visceral Protein

Ovissipour, Mahmoudreza; Safari, Reza; Motamedzadegan, Ali; Shábanpour, Bahareh

doi:10.1007/s11947-009-0284-x

Cited by 61 publications

(65 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In contrast, the investigators [32, 39, 40] had reported a decrease in the DH with prolonged incubation periods. Guerard et al [39] proposed the reduced DH observed with a prolonged incubation period might be caused by limited enzyme activity by the formation of reaction products at a high DH, the decreased concentration of peptide bonds available for hydrolysis, enzyme inhibition, and enzyme deactivation.…”

Section: Resultsmentioning

confidence: 92%

Optimisation of the Enzymatic Hydrolysis of Blood Cells with a Neutral Protease

Zheng

Chen

Shan

et al. 2013

BioMed Research International

View full text Add to dashboard Cite

For utilizing the blood cells (BCs) effectively, enzymatic hydrolysis was applied to produce the enzymatically hydrolyzed blood cells (EHBCs) by using a neutral protease as a catalyst. The results of the single-factor experiments showed optimal substrate concentration, enzyme to substrate ratio (E/S), pH, temperature, and incubation period were 1.00%, 0.10, 7.00, 50.00°C, and 12.00 h, respectively. The optimized hydrolysis conditions from response surface methodology (RSM) were pH 6.50, E/S 0.11, temperature 45.00°C, and incubation period 12.00 h. Under these conditions (substrate concentration 1.00%), the degree of hydrolysis (DH) was 35.06%. The free amino acids (FAAs) content of the EHBCs (35.24%) was 40.46 times higher than BCs while the total amino acids (TAAs) content was lower than BCs. The scores of lysine (human 0.87; pig 0.97), valine (human 1.42; pig 1.38), leucine (human 1.50; pig 1.90), tyrosine (human 0.84; pig 1.09), and histidine (human 2.17; pig 2.50) indicated that the EHBCs basically fulfilled the adult human and pig nutritional requirements. The calculated protein efficiency ratios (C-PERs) of the EHBCs were 3.94, 6.19, 21.73, and 2.04. In summary, the EHBCs were produced successfully with optimized conditions and could be a novel protein source for humans and pigs.

show abstract

Section: Resultsmentioning

confidence: 92%

Optimisation of the Enzymatic Hydrolysis of Blood Cells with a Neutral Protease

Zheng

Chen

Shan

et al. 2013

BioMed Research International

View full text Add to dashboard Cite

show abstract

“…Generally, Alcalase® 2.4-L-assisted reactions have been repeatedly favored for fish hydrolysis, due to the high degree of hydrolysis that can be achieved in a relatively short time under moderate pH conditions, compared with the neutral or acidic enzymes (Kristinsson and Rasco 2000a, b;Hoyle and Merritt 1994;Shahidi et al 1995;Benjakul and Morrissey 1997;Aspmo et al 2005;Ovissipour et al 2009b).…”

Section: Introductionmentioning

confidence: 99%

Optimization of Enzymatic Hydrolysis of Visceral Waste Proteins of Yellowfin Tuna (Thunnus albacares)

Ovissipour

Kenari

Motamedzadegan

et al. 2010

Food Bioprocess Technol

Self Cite

View full text Add to dashboard Cite

Fish protein hydrolysate was produced from the viscera of yellowfin tuna (Thunnus albacares). Hydrolysis conditions (enzyme activity, temperature, and time) were optimized using response surface methodology. A factorial design was applied to minimize enzyme utilization and modeling of degree of hydrolysis (r 2 =0.94). Lack-of-fit test revealed a non-significant value for the model, indicating that the regression equation was adequate for predicting the degree of hydrolysis under any combination of the variables (P<0.05). The optimum conditions to reach the highest degree of hydrolysis were: 60.4°C, 90.25 min, and a protease (Alcalase 2.4 L) activity of 70.22 AU/kg protein.The spray-dried tuna visceral protein hydrolysates had relatively high protein (72.34%) and low lipid (1.43%) content. The chemical score of the hydrolysate indicated that it fulfils adult human nutritional requirements except for methionine. Lysine and methionine were the first and the second limiting amino acids in that order. Phenylalanine was the predominant amino acid in the hydrolysates with respect to common carp requirement. In addition, the protein efficiency ratio of tuna visceral hydrolysate was 2.85-5.35.

show abstract

“…A number of peptides with significant biological activities have been identified in the enzymatic hydrolysis various marine tissue proteins, for example, antihypertensive activity peptides (Byun and Kim 2001;Qian et al 2007;Lee et al 2010;Tsai et al 2008;Zhao et al 2009;Lee and Song 2009;Sheih et al 2009), antioxidant peptides (Ovissipour et al 2009;Jung et al 2005b;Kim et al 2007a;Je et al 2008;Slizyte et al 2009;Cho et al 2008;Qian et al 2008), anticoagulant peptides (Jo et al 2008;Jung and Kim 2009;Jung et al 2002), antimicrobial peptides (Liu et al 2008;Battison et al 2008;Li et al 2008), angiotensin I converting enzyme (ACE)-inhibitory peptides (Kong et al 2009;He et al 2006;Cheung and Li-Chan 2010;), and mineral carrier peptides (Jung et al 2006;Jung and Kim 2007).…”

Section: Introductionmentioning

confidence: 99%

Separation of Iron-Binding Peptides from Shrimp Processing By-products Hydrolysates

Huang

Ren

Jiang

2010

Food Bioprocess Technol

View full text Add to dashboard Cite

Separation of iron-binding peptides derived from shrimp processing by-products (SPB) by Alacase hydrolysis was investigated. The highest iron-binding capacity of the hydrolysate (17.5 μmol/g of protein) was obtained with Alacase at a degree of hydrolysis of 8%. The molecular weight (MW) distribution on gel permeation chromatography (GPC) showed that it was ranging from 1 to 6 kDa. By separating with ion-exchange chromatography on SPSepharose Fast Flow and gel filtration on Sephadex G-25, one fraction with highest iron-binding capacity of 8,800μmol/g of protein was purified, and the purification fold of 502 was obtained. When the highest iron-binding capacity fraction was applied on RP-HPLC column, there were four main peaks. By comparing with the infrared spectra of the iron-binding peptides and iron-peptides complex, it was suggested that the principal site of iron-binding corresponded primarily to the carboxylate groups and to a lesser extent to the peptide bonds.

show abstract

Chemical and Biochemical Hydrolysis of Persian Sturgeon (Acipenser persicus) Visceral Protein

Cited by 61 publications

References 17 publications

Optimisation of the Enzymatic Hydrolysis of Blood Cells with a Neutral Protease

Optimisation of the Enzymatic Hydrolysis of Blood Cells with a Neutral Protease

Optimization of Enzymatic Hydrolysis of Visceral Waste Proteins of Yellowfin Tuna (Thunnus albacares)

Separation of Iron-Binding Peptides from Shrimp Processing By-products Hydrolysates

Contact Info

Product

Resources

About