Study on muscle protein hydrolysis by Alcalase and optimization pickled process of Gaogou bundle hoof
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Hoof
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The optimization of hydrolysis conditions in terms of pH, temperature, enzymesubstrate
(ES) ratio and hydrolysis time for the production of threadfin bream
(Nemipterus japonicus) hydrolysate was studied. Alcalase showed a higher
percent nitrogen recovery (% NR) than Flavourzyme: Protamex mixture. By
using Alcalase, the optimum hydrolysis conditions were pH 8.5, 60°C, ES2%
and 120 min hydrolysis time. At least twenty percent degree of hydrolysis (% DH) and 70% NR was achieved. The yield of spray-dried hydrolysate
hydrolysed under these conditions was 4%. The hydrolysate was white in
color, highly soluble over a wide pH range, high in protein and essential amino
acids but low in fat. The hydrolysate also exhibited an improvement in foam
ability in comparison to the threadfin bream muscle but the foam was unstable.
Hydrolysis with Alcalase also produced hydrolysate with poor emulsifying
properties. The major free amino acids in the hydrolysate were glutamic acid,aspartic acid, lysine, leucine and arginine in which glutamic acid was the
dominant amino acid. Bitter amino acids methionine, valine, isoleucine,
phenylalanine, leucine, arginine and tyrosine comprised of 42.34% of the total
free amino acids. The inosine 5'-monophosphate (IMP) content was higher in
the hydrolysate than that in the muscle. SDS-PAGE showed the presence of
twenty peptide bands in the muscle having molecular weight between 7.2 to
87.6 kD and thirteen in the hydrolysate with molecular weight between 7.2 to
64 kD. For Sephadex G-75 fractions (FR), no peptide bands were seen in FR
I, III, IV, VI, VII and VIII. FR II and V showed the presence of respectively five
and seven peptide bands with molecular weight between 11.4 to 54 kD and
10.5 to 51.3 kD. Histamine content in the muscle was found to be 14.45 mgkg
1 but no histamine was detected in the hydrolysate. Sensory evaluation of the
hydrolysate indicated that it was fishy in flavor and constitutes three basic
tastes namely bitter, umami and salty with umami and bitterness as the
dominating tastes.
Isoleucine
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Umami
Enzymatic Hydrolysis
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Enzymatic Hydrolysis
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In this research, difference soybean peptides were prepared by hydrolyzing soybean protein isolate with alcalase, pepsin, trypsinase,p apaina ndn eutrase respectively,a ndt hed ifference oft heira ngiotensinc onverting enzyme (ACE)i nhibiting activities was studied. Comparison experiments on peptides increments, relationship between degree of hydrolysis (DH) and ACE inhibitoryr ate, relation betweenu ltrafiltrateo fp eptidesa ndA CEi nhibitoryr atea nde lectrophoretics eparation werec onducted. The result showed that the peptides increments by alcalase hydrolysis were the largest, and the sequent order in turn was pepsin papainneutrase, but trypsinase was abnormal. The degree of hydrolysis (DH) increased with prolongation of time. The biggest Dh of alcalase was 21%, and the sequent order in turn was pepsinpapainneutrase, but trypsinase was only 9%. ACE inhibitory rate of alcalase, pepsin, papain, neutrase and trypsinase hydrolysates at the biggest DH, were 44.9%, 43.5%, 23.1%, 23.5% and 15.7% respectively. Peptides with above 1000 daltons molecular weight have the strongest inhibitory effects on ACE. Small molecular peptides by alcalase and pepsin amounted for 71.3% and 69.4% of all the peptides respectively, and the ACE inhibitory rate of the small molecular peptides by alcalase, pepsin, papain, neutrase and trypsinase were 64.57%, 78.49%, 47.3%, 45.7% and 29.6% respectively. So it can be concluded that papain was optimum for ACE inhibiting peptide preparation among 5kinds of protease, and the sequent order in ture: alcalasepapainneutrasetrypsinase.
Pepsin
Enzymatic Hydrolysis
Proteolytic enzymes
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Enzymatic Hydrolysis
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The amino acid contents of the enzymatic hydrolysates of the fish scale collagen treated by papain, alcalase, flavorzyme and trypsin were measured. The result showed that the peptide yields of the different enzymatic hydrolysates were different. The peptide yields of the products treated by papain and alcalase were higher. The low hydrolysis rate of hydroxyproline in fish scale collagen was observed. About 99.3% of hydroxyproline in the enzymatic hydrolysate treated by papain existed in the peptides.
Hydroxyproline
Enzymatic Hydrolysis
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Antigenicity
Pepsin
Enzymatic Hydrolysis
Hydrostatic pressure
Proteolysis
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Hydrolyzed collagen (HC) from defatted Asian sea bass skin was prepared by different enzymatic hydrolysis processes. For one-enzyme hydrolysis, papain (0.3 unit per g dry matter, DM) at 40 °C for 90 min or Alcalase (0.2 or 0.3 unit per g DM) at 50 °C for 90 min were used. The two-enzyme hydrolysis was accomplished with papain at 0.3 unit per g DM (P0.3), followed by Alcalase hydrolysis at 0.2 or 0.3 units per g DM (A0.2 or A0.3, respectively). HC prepared using the P0.3 + A0.3 process showed higher peptide yield, recovery and imino acid content in addition to stronger ABTS, DPPH radical scavenging activities and ferric reducing antioxidant power than other hydrolysis processes. HC obtained from the P0.3 + A0.3 process (at 125-500 μg mL
ABTS
Enzymatic Hydrolysis
Human skin
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ABSTRACT: The effects of different proteolytic treatments on the physiochemical and bitterness properties of pea protein hydrolysates were investigated. A commercial pea protein isolate was digested using each of 5 different proteases to produce protein hydrolysates with varying properties. After 4 h of enzyme digestion, samples were clarified by centrifugation followed by desalting of the supernatant with a 1000 Da membrane; the retentates were then freeze‐dried. Alcalase and Flavourzyme™ produced protein hydrolysates with significantly higher ( P < 0.05) degree of hydrolysis when compared to the other proteases. Flavourzyme, papain, and alcalase produced hydrolysates that contained the highest levels of aromatic amino acids, while trypsin hydrolysate had the highest levels of lysine and arginine. Papain hydrolysate contained high molecular weight peptides (10 to 178 kDa) while hydrolysates from the other 4 proteases contained predominantly low molecular weight peptides (≤ 23 kDa). DPPH (1,1‐diphenyl‐2‐picrylhydrazyl) free radical scavenging activity of the Flavourzyme hydrolysate was significantly ( P < 0.05) the highest while alcalase and trypsin hydrolysates were the lowest. Inhibition of angiotensin converting enzyme (ACE) activity was significantly higher ( P < 0.05) for papain hydrolysate while Flavourzyme hydrolysate had the least inhibitory activity. Sensory analysis showed that the alcalase hydrolysate was the most bitter while papain and α‐chymotrypsin hydrolysates were the least. Among the 5 enzymes used in this study, papain and α‐chymotrypsin appear to be the most desirable for producing high quality pea protein hydrolysates because of the low bitterness scores combined with a high level of angiotensin converting enzyme inhibition and moderate free radical scavenging activity.
Pea protein
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Residue (chemistry)
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