Optimization of the Enzymatic Hydrolysis of Tilapia Frames

2012 ◽  
Vol 554-556 ◽  
pp. 1387-1394
Author(s):  
He Jian Xiong ◽  
Longfei Cao ◽  
Huajun You ◽  
Qingpi Yan ◽  
Ying Ma
Keyword(s):  
Amino Acids ◽  
Enzymatic Hydrolysis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Protein Supplementation ◽  
Degree Of Hydrolysis ◽  
Enzyme Substrate ◽  
Initial Ph ◽  
Substrate Ratio ◽  
Hydrolysis Of

Tilapia frames were subjected to enzymatic hydrolysis using Flavouzryme and Papain with a ratio of 2:1. The relationship of temperature (40 to 60°C), enzyme: substrate ratio (0.5% to 4.5%), initial pH (6.0 to 8.0) and hydrolysis time (1h to 9h) to the degree of hydrolysis were determined. The enzymatic hydrolysis was optimized for maximum degree of hydrolysis using surface response methodology. The optimum conditions for enzymatic hydrolysis of tilapia frames were temperature 53°C, enzyme : substrate ratio of 3.5%, initial pH 7.2, and reaction time 7h. Under these conditions a degree of hydrolysis of 40.01% were obtained. The yield of free amino acids in the hydrolysate was 46.61mg/g tilapia frames. The flavor amino acids and essential amino acids occupied up to 31.8% and 49.0% of the total free amino acids respectively. The hydrolysate of waste tilapia frames showed good potential for applications such as protein supplementation in food system.

scholarly journals Isolation of Free Amino Acids via Enzymatic Hydrolysis of Tobacco-Derived F1 Protein

2018 ◽  
Vol 28 (4) ◽  
pp. 179-190
Author(s):  
Mehdi Ashraf-Khorassani ◽  
William M. Coleman ◽  
Michael F. Dube ◽  
Larry T. Taylor
Keyword(s):  
Amino Acids ◽  
Enzymatic Hydrolysis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Protein Concentration ◽  
Enzyme Concentration ◽  
Enzymatic Conversion ◽  
Reaction Conditions ◽  
Analytical Methodology ◽  
Hydrolysis Of

SummaryFree amino acids have been isolated via optimized enzymatic hydrolysis of F1 tobacco protein using two cationic resins (Amberlite IR120 and Dowex MAC-2). Optimized enzymatic conversions of the protein as a result of systematic variations in conditions (e.g., time, temperature, pH, enzyme type, enzyme concentration, anaerobic/aerobic environments, and protein concentration) employing commercially available enzymes, were consistently higher than 50% with qualitative amino acid arrays that were consistent with the known composition of tobacco F1 protein. Amberlite IR120 was shown to have a much higher efficiency and capacity for isolation of amino acids from standard solutions and from hydrolysate when compared with the results using Dowex MAC-2. Two columns packed with conditioned Amberlite IR120 (120 × 10 mm,12–15 g resin) and (200 × 25.4 mm, 60–65 g resin) were used to isolate two batches (2.5–3.0 mg and 13–15 mg) of free amino acids, respectively. A relatively inexpensive analytical methodology was developed for rapid analysis of the free amino acids contained within the enzyme hydrolysate. Commercially available enzymes, when employed in optimized reaction conditions, are very effective for enzymatic conversion of tobacco F1 protein to free amino acids.

scholarly journals Action of protease from Aspergillus sojae and pancreatin in the hydrolysis of whey protein concentrate

2013 ◽  
Vol 3 (1) ◽  
pp. 19
Author(s):  
Marialice Pinto Coelho Silvestre ◽  
Harriman Aley Morais ◽  
Mauro Ramalho Silva ◽  
Viviane Dias Medeiros Silva ◽  
Mariana Wanessa Santana de Souza
Keyword(s):  
Amino Acids ◽  
Whey Protein ◽  
Free Amino Acids ◽  
Free Amino ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Peptide Profile ◽  
Aspergillus Sojae ◽  
Enzyme Substrate ◽  
Substrate Ratio

<p>The preparation of hydrolysates from whey protein concentrate with high contents of di- and tripeptides and free amino acids, and reduced amount of large peptides, was the objective of this study. The actions of a protease from Aspergillus sojae and a pancreatin at six enzyme:substrate ratios, pH 7.0, at 50 &deg;C for 5 h were evaluated. The size-exclusion-high performance liquid chromatography and the method of the Correct Fraction Area were used for the fractionation and quantification of peptides and free amino acids in the hydrolysates. It was observed that the type of enzyme and the enzyme: substrate ratio affected significantly the peptide profile of the hydrolysates. The chromatograms obtained by the action of two enzymes were different and varied according to the specificity or enzymatic activity. The best peptide profile was found for the hydrolysate obtained using pancreatin at an enzyme: substrate ratio of 8:100 that showed the smallest amount of large peptides (41.13%), and the greatest di- and tripeptide (6.46%) and free amino acid (8.22%) contents.</p><p>&nbsp;</p><p>DOI: http://dx.doi.org/10.14685/rebrapa.v3i1.69</p><br />

Biotechnological Aspects of obtaining Functional Ingredients by the Conversion of Saccharomyces cerevisiae 985-Т Biomass

2020 ◽  
Vol 36 (4) ◽  
pp. 34-41
Author(s):  
L.V. Rimareva ◽  
M.B. Overchenko ◽  
N.I. Ignatova ◽  
N.V. Shelekhova ◽  
N.S. Pogorzhelskaya ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Fractional Composition ◽  
Amino Nitrogen ◽  
Degree Of Hydrolysis ◽  
Amine Nitrogen ◽  
Functional Ingredients ◽  
Hydrolysis Of

An algorithm for the biocatalytic conversion of polymers of subcellular structures of Saccharomyces cerevisiae 985-T has been developed. It was shown that the action of enzymes on cell wall mannoproteins and (3-glucans led to deformation of their structure and the transfer of more than 50% of polysaccharides to a soluble state with the formation of 13.4% reducing carbohydrates, 1.8% amine nitrogen and 7.7% free amino acids (biological-1). Biological-2 had an increased content of total carbohydrates (32.2%) and fiber (10.5%). It was found that the combined action of the complex of proteinases and peptidases contributed to an increase in the degree of hydrolysis of subcellular structures, which was accompanied by a growth of the content of amino nitrogen by 2.7 times, free amino acids by 3.1 times, and low-molecular peptides (up to 500 Da) by 3.5 times (biological-3). The obtained biologicals were characterized by a high content of phosphorus and potassium. It was shown that the use of enzyme systems that catalyze the hydrolysis of intracellular polymers in yeast biomass allows us to obtain products with different biochemical and structural-fractional composition, which determines their properties. Saccharomyces cerevisiae, enzymes, structural-fractional composition, functional ingredients The work was carried out at the expense of the subsidy for the implementation of the State Task.

Availability of amino acids supplied by constant intravenous infusion of synthetic dipeptides in healthy man

1989 ◽  
Vol 76 (6) ◽  
pp. 643-648 ◽  
Author(s):  
S. Albers ◽  
J. Wernerman ◽  
P. Stehle ◽  
E. Vinnars ◽  
P. Fürst
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Metabolic Clearance ◽  
Amino Acid Solution ◽  
Appreciable Change ◽  
Total Body ◽  
Hydrolysis Of ◽  
Firm Evidence ◽  
Apparently Healthy

1. A commercial amino acid solution supplemented with two synthetic dipeptides, l-alanyl-l-glutamine (Ala-Gln) and glycyl-l-tyrosine (Gly-Tyr), or alternatively with isonitrogenous amounts of free alanine and glycine has been continuously infused over 4 h in six apparently healthy volunteers. 2. The infusion of the solutions was not accompanied by any side effects and the volunteers reported no complaints. 3. Infusion of the alanine- and glycine-supplemented control solution resulted in an increase of the concentration of these amino acids, while no appreciable change in free glutamine concentration was observed and free tyrosine revealed a steady decrease throughout the infusion. 4. Infusion of the peptide-supplemented solution resulted in a prompt equimolar liberation of the constituent free amino acids (glutamine, alanine, tyrosine and glycine), approaching steady state after about 30 min infusion, while only trace but stable concentrations of the two dipeptides were measured throughout the infusion. No peptides were detectable in urine. The findings suggest a nearly quantitative extracellular hydrolysis of the infused dipeptides and indicate a subsequent utilization of the liberated free amino acids. 5. The estimated metabolic clearance rates and total body plasma clearances were very similar for the two dipeptides (Ala-Gln 35.9 ± 9.5 ml min−1 kg−1 and 2.9 ± 0.9 1/min, respectively; Gly-Tyr 33.7 ± 9.5 ml min−1 kg−1 and 2.7 ± 0.9 1/min, respectively); thus there is little difference in the metabolic handling of these dipeptides. 6. The study provides firm evidence that the synthetic dipeptides Ala-Gln and Gly-Tyr are quantitatively hydrolysed and that these peptides can be used as a safe and efficient source of free glutamine and tyrosine as part of a commercial solution.

scholarly journals Changes in flavor compounds of Aloididae aloidi during enzymatic hydrolysis

2021 ◽  
Vol 233 ◽  
pp. 02040
Author(s):  
Xuting Bai ◽  
Tao Li ◽  
Honglei Zhao ◽  
Xuepeng Li ◽  
Wenhui Zhu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Enzymatic Hydrolysis ◽  
Free Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Flavor Compounds ◽  
Peptide Analysis ◽  
Soluble Peptide ◽  
Maximum Value

Protamex was selected to prepare the hydrolysate. E-tongue, free amino acid combined with soluble peptide analysis were used to detect the flavor changes of Aloididae aloidi during enzymolysis. Degree of proteolysis increased with the prolongation of enzymolysis time, and reached the maximum value at 8 hours. The content of soluble peptide of hydrolysate increased firstly and then decreased in the later process. The E-tongue could effectively distinguish the taste difference of hydrolysates at different enzymolysis time, and the hydrolysate presented strong bitterness and astringency during the whole enzymolysis. The total amount of free amino acids in the hydrolysate increased gradually, and some sweet, umami and bitter amino acids increased in varying degrees during the process of enzymolysis.

scholarly journals The Effect of Fermentation with Kefir Grains on the Physicochemical and Antioxidant Properties of Beverages from Blue Lupin (Lupinus angustifolius L.) Seeds

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 5791
Author(s):  
Łukasz Łopusiewicz ◽  
Emilia Drozłowska ◽  
Paulina Trocer ◽  
Paweł Kwiatkowski ◽  
Artur Bartkowiak ◽  
...  
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Microbial Population ◽  
Antioxidant Properties ◽  
Lupinus Angustifolius ◽  
Kefir Grains ◽  
Antioxidant Properties Of Beverages ◽  
Hydrolysis Of ◽  
Free Radicals Scavenging

Plant derived fermented beverages have recently gained consumers’ interest, particularly due to their intrinsic functional properties and presence of beneficial microorganisms. Three variants containing 5%, 10%, and 15% (w/w) of sweet blue lupin (Lupinus angustifolius L. cv. “Boregine”) seeds were inoculated with kefir grains and incubated at 25 °C for 24 h. After processing, beverages were stored in refrigerated conditions (6 °C) for 21 days. Changes in microbial population, pH, bioactive compounds (polyphenolics, flavonoids, ascorbic acid), reducing sugars, and free amino acids were estimated. Additionally, viscosity, firmness, color, and free radicals scavenging properties were determined. Results showed that lactic acid bacteria as well as yeast were capable of growing well in the lupin matrix without any supplementation. During the process of refrigeration, the viability of the microorganisms was over the recommended minimum level for kefir products. Hydrolysis of polysaccharides as well as increase of free amino acids was observed. As a result of fermentation, the beverages showed excellent DPPH, ABTS+·, ·OH, and O2− radicals scavenging activities with a potential when considering diseases associated with oxidative stress. This beverages could be used as a new, non-dairy vehicle for beneficial microflora consumption, especially by vegans and lactose-intolerant consumers.

Dietary regulation of intestinal transport of the dipeptide carnosine

1988 ◽  
Vol 255 (2) ◽  
pp. G143-G150 ◽  
Author(s):  
R. P. Ferraris ◽  
J. Diamond ◽  
W. W. Kwan
Keyword(s):  
Amino Acids ◽  
Cell Surface ◽  
Dietary Protein ◽  
Free Amino Acids ◽  
Free Amino ◽  
Intestinal Transport ◽  
Dietary Regulation ◽  
Dietary Protein Level ◽  
Low Protein ◽  
Hydrolysis Of

Uptake of the dipeptide L-carnosine was measured in everted intestinal sleeves of mice whose dietary protein level or else proportion of protein in the form of free amino acids was varied experimentally. Carnosine uptake was highest in the jejunum, regardless of ration. Compared with a low-protein (18%) ration, a high-protein (72%) ration stimulated carnosine uptake by 30-70% in duodenum and jejunum (but not in ileum). This stimulation was observed even in the presence of peptidase inhibitors that inhibit cell surface hydrolysis of dipeptides. Measured carnosine hydrolysis was low or negligible. Carnosine uptake was the same in mice fed 54% unhydrolyzed casein, 54% partly hydrolyzed casein, and 54% free amino acids formulated so as to stimulate a complete hydrolysate of casein. Thus carnosine uptake is regulated by dietary levels of amino acids, peptides, and proteins, all of which seem equally effective at inducing carnosine transporters.

Dipeptide utilization by starter streptococci

1977 ◽  
Vol 44 (2) ◽  
pp. 309-317 ◽  
Author(s):  
B. A. Law
Keyword(s):  
Amino Acids ◽  
Transport System ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
Exponential Phase ◽  
Whole Cells ◽  
Streptococcus Cremoris ◽  
Defined Media ◽  
Hydrolysis Of

SummaryOf 8 strains ofStreptococcus cremoristested, 5 grew almost as well in defined media in which various essential amino acids were supplied in dipeptides as they did in media containing the equivalent free amino acids. The remainder grew poorly or not at all in the peptide-containing media. Growth of peptide-utilizing strains was inhibited by also including structurally-related dipeptides in the medium, presumably due to competition for uptake by transport system carriers. Both types of starters produced cell-free dipeptidases recoverable from the medium of exponential phase cultures. Addition of the partly-purified extracellular dipeptidases to dipeptidecontaining test media initiated growth in strains unable to use peptides.Str. lactisgrew in defined peptide media, but the further addition of structurally-related dipeptides did not inhibit growth, either bcause each dipeptide was transported by a specific carrier or because peptides were hydrolysed extracellularly. The presence of cell-bound extracellular dipeptidase was indicated by the hydrolysis of dipeptides with washed whole cells in buffer. This was not observed withStr. cremorisstrains.

Alkaline hydrolysis of porcine blood haemoglobin: applications for peptide and amino acid production

2013 ◽  
Vol 53 (2) ◽  
pp. 121 ◽  
Author(s):  
Carlos Álvarez ◽  
Manuel Rendueles ◽  
Mario Díaz
Keyword(s):  
Amino Acids ◽  
Alkaline Hydrolysis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Animal Feed ◽  
Low Cost ◽  
Current Trend ◽  
Amino Acid Production ◽  
Blood Haemoglobin ◽  
Hydrolysis Of

Alkaline hydrolysis of proteins recovered from slaughterhouse blood is a method to obtain profitable peptides and free amino acids for animal feed, besides decreasing the waste produced by this industry. The current trend to use enzymatic hydrolysis may need reconsidering due to its high cost in materials and the need for control processes that are both complex and expensive. The use of caustic soda (NaOH), which is a low-cost product, to obtain useful peptides from porcine haemoglobin is studied in this paper. Concentrations of 6 M NaOH at 50°C for 24 h afforded an 80% peptide recovery yield with an average peptide size of 13 kDa. Product obtained at 24 h was composed of soluble haemoglobin (7%), peptides larger than 10 kDa (63%), peptides between 6 and 10 kDa (16%), peptides between 1 and 6 kDa (1%), free amino acids (4%) and non-soluble compounds (8%). A kinetic model was subsequently developed. It is proposed that neutralising the alkaline product using acid products allows the processing of a higher amount of protein while employing the same amounts of reagents, although this topic requires further research.

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