Enzymatic Hydrolysis of Marine Collagen and Fibrinogen Proteins in the Presence of Thrombin

Enzymatic hydrolysis of native collagen and fibrinogen was carried out under comparable conditions at room temperature. The molecular weight parameters of proteins before and after hydrolysis by thrombin were monitored by gel-penetrating chromatography (GPC). An analysis of the experiment results shows that the molecular weight parameters of the initial fibrinogen (Fn) and cod collagen (CC) are very similar. High molecular CC decays within the first minute, forming two low molecular fractions. The main part (~80%) falls on the fraction with a value of Mw less than 10 kDa. The initial high molecular fraction of Fn with Mw ~320–340 kDa is not completely hydrolyzed even after three days of control. The presence of low molecular fractions with Mw ~17 and Mw ~10 kDa in the solution slightly increases within an hour and noticeably increases for three days. The destruction of macromolecules of high molecular collagen to hydrolysis products appears almost completely within the first minute mainly to the polymer with Mw ~10 kDa, and enzymatic hydrolysis of fibrinogen proceeds slower than that of collagen, but also mainly to the polymer with Mw ~10 kDa. Comparative photos of the surfaces of native collagen, fibrinogen and the scaffold based on them were obtained.

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Synthesis and properties of oligochitosan ascorbate from Bombyx mori

Bulletin of the Karaganda University Chemistry series ◽

10.31489/2021ch1/91-98 ◽

2021 ◽

Vol 101 (1) ◽

pp. 91-98

Author(s):

K.K. Pirniyazov ◽

◽

V.E. Tikhonov ◽

S.Sh. Rashidova ◽

◽

...

Keyword(s):

Molecular Weight ◽

Acid Hydrolysis ◽

Bombyx Mori ◽

Antimicrobial Properties ◽

A Value ◽

Optimal Duration ◽

Physicochemical Methods ◽

Composition Structure ◽

Hydrolysis Of ◽

High Molecular Weight Chitosan

Oligochitosan samples were obtained by acid hydrolysis of high molecular weight chitosan isolated from Bombyx mori (B.M.). Carrying out acid hydrolysis for 6 hours, it was found that after 4 hours and further with increasing duration, the molecular weight of chitosan decreases to a value corresponding to the ranges of mo-lecular weights of oligochitosan 2–16 kDa. It has been seen that the optimal duration of hydrolysis, leading to the production of oligochitosan with a molecular weight of less than 16 kDa, should be considered 4–5 hours. Depolymerization of chitosan with a molecular weight of 177 kDa was carried out using sodium nitrite in so-lution to obtain oligochitosan with a molecular weight of 6 kDa. On the basis of oligochitosan samples ob-tained by two methods, their ascorbates were received. Under constant conditions with varying the ratio of the components (ChS:AA) and the pH of the solution, the reaction of chitosan ascorbate formation was car-ried out on the basis of the suspension method. The composition, structure, and molecular weight characteris-tics of oligochitosan ascorbate and oligochitosan Bombyx morisamples were confirmed by physicochemical methods. It has been seen that the obtained samples have antimicrobial properties against Fuzarium oxysporum.

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Effects of Enzymatic Hydrolysis Conditions on the Antioxidant Activity of Red Tilapia (Oreochromis spp.) Viscera Hydrolysates

Current Pharmaceutical Biotechnology ◽

10.2174/1389201021666200506072526 ◽

2020 ◽

Vol 21 (12) ◽

pp. 1249-1258

Author(s):

Cindy T. Sepúlveda ◽

José E. Zapata

Keyword(s):

Molecular Weight ◽

Antioxidant Activity ◽

Enzymatic Hydrolysis ◽

Protein Concentration ◽

Polynomial Equation ◽

Degree Of Hydrolysis ◽

Red Tilapia ◽

Hydrolysis Conditions ◽

Hydrolysis Of ◽

By Products

Background: Fish is an essential source of nutrients for human nutrition due to the composition of proteins, vitamins, and minerals, among other nutrients. Enzymatic hydrolysis represents an alternative for the use of by-products of the aquaculture industry. Objective: We propose to evaluate the effect of stirring speed, temperature, and initial protein concentration on the degree of hydrolysis of proteins and antioxidant activity of red tilapia (Oreochromis spp.) viscera hydrolysates. Methods: The effect of stirring speed, temperature, and initial protein concentration on the degree of hydrolysis of proteins and antioxidant activity was evaluated using an experimental design that was adjusted to a polynomial equation. The hydrolysate was fractioned to determine the antioxidant activity of the fractions, and functional properties were also measured. Results: Stirring speed and protein concentration presented a statistically significant effect (p <0.05) on all the response variables. However, the temperature did not present a statistically significant effect on the degree of hydrolysis. Discussion: The best conditions of hydrolysis were stirring speed of 51.44 rpm, a temperature of 59.15°C, and the protein concentration of 10 g L-1. The solubility of the hydrolysate protein was high at different pH, and the hydrolysate fraction with the highest antioxidant activity has a molecular weight <1 kDa. Conclusion: The degree of hydrolysis and the biological activity of red tilapia viscera hydrolysates (Oreochromis spp.) are affected by temperature, substrate concentration, and stirring speed. The optimal conditions of hydrolysis allowed to obtain a hydrolysate with antioxidant activity are due to the peptides with low molecular weight.

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EFFECTS OF ASCORBIC ACID AND FERUM IONS CONCENTRATION ON THE HYDROLYSIS OF GLUCOSINOLATE AND MYROSINASE ACTIVITY IN THE WATERCRESS (Nasturtium officinale sp.)

Jurnal Teknologi ◽

10.11113/jt.v78.5092 ◽

2016 ◽

Vol 78 (8) ◽

Cited By ~ 1

Author(s):

Syamimi Mohd Zul ◽

Noumie Surugau

Keyword(s):

Ascorbic Acid ◽

Enzymatic Hydrolysis ◽

Hydrolysis Product ◽

Carcinogenic Activity ◽

Nasturtium Officinale ◽

Hydrolysis Products ◽

Low Concentrations ◽

Health Promoting ◽

Hydrolysis Of ◽

Myrosinase Activity

Watercress (Nasturtium officinale sp.) from the Brassicae family contains phenethyl glucosinolates (gluconasturtiin) as the main glucosinolate (GLS). The enzymatic hydrolysis products by naturally-occuring myrosinase produced phenethyl isothicyanate (PEITC) which reported to possess anti-carcinogenic activity. Depending on several factors, its counterpart, phenethyl nitrile (PEN) can also be formed as hydrolysis product. This study investigated the effects of adding ascorbic acid and Fe2+ ions at different concentration on the hydrolysis of gluconasturtiin. Hydrolysis products were extracted using dichloromethane and analyzed semi-quantitatively by using GCMS. The results showed that PEITC increased at the low concentration of ascorbic acid (up to 0.06M). Similarly, addition of up to 0.06M Fe2+ ions increased PEITC; higher than 0.06M inhibits the formation of PEITC. Interestingly, similar trend for the production of PEN was detected. This study also investigated myrosinase activity both by exogenous and endogenous methods at different concentrations of ascorbic acid and Fe2+ ions using standard sinigrin as subsrat. Overall, the myrosinase activity was more active at the low concentrations of ascorbic acid. Also, the exogenous method is more efficient than endogenous. This study proved that the presence of reducing agents such as ascorbic acid and Fe2+ ions during the preparation of watercress as food would affect the production of the health-promoting PEITC.

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THE ENZYMATIC HYDROLYSIS PRODUCTS OF SARIN

Canadian Journal of Biochemistry and Physiology ◽

10.1139/o56-009 ◽

1956 ◽

Vol 34 (1) ◽

pp. 75-79 ◽

Cited By ~ 15

Author(s):

F. C. G. Hoskin

Keyword(s):

Enzymatic Hydrolysis ◽

Cholinesterase Inhibitor ◽

Methylphosphonic Acid ◽

Serum Enzyme ◽

Rat Serum ◽

Hydrolysis Products ◽

Hydrolysis Of

The hydrolysis of the powerful cholinesterase inhibitor, sarin, by a rat serum enzyme leads almost exclusively to isopropyl methylphosphonic acid, neither methylphosphonic acid nor hydrogen methylphosphonofluoridate being formed. When isopropyl methylphosphonic acid is administered to the intact rat, it is excreted unchanged in the urine. It is inferred, therefore, that the metabolism of sarin by the intact rat would lead almost exclusively to isopropyl methylphosphonic acid.

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CRYSTALLINE INORGANIC PYROPHOSPHATASE ISOLATED FROM BAKER'S YEAST

The Journal of General Physiology ◽

10.1085/jgp.35.3.423 ◽

1952 ◽

Vol 35 (3) ◽

pp. 423-450 ◽

Cited By ~ 327

Author(s):

M. Kunitz

Keyword(s):

Molecular Weight ◽

Enzymatic Hydrolysis ◽

Isoelectric Point ◽

Calcium Ions ◽

Baker’S Yeast ◽

Thiamine Pyrophosphate ◽

Inorganic Pyrophosphatase ◽

Baker's Yeast ◽

Inorganic Pyrophosphate ◽

Hydrolysis Of

Crystalline inorganic pyrophosphatase has been isolated from baker's yeast. The crystalline enzyme is a protein of the albumin type with an isoelectric point near pH 4.8. Its molecular weight is of the order of 100,000. It contains about 5 per cent tyrosine and 3.5 per cent tryptophane. It is most stable at pH 6.8. The new crystalline protein acts as a specific catalyst for the hydrolysis of inorganic pyrophosphate into orthophosphate ions. It does not catalyze the hydrolysis of the pyrophosphate radical of such organic esters as adenosine di- and triphosphate, or thiamine pyrophosphate. Crystalline pyrophosphatase requires the presence of Mg, Co, or Mn ions as activators. These ions are antagonized by calcium ions. Mg is also antagonized by Co or Mn ions. The rate of the enzymatic hydrolysis of inorganic pyrophosphate is proportional to the concentration of enzyme and is a function of pH, temperature, concentration of substrate, and concentration of activating ion. The approximate conditions for optimum rate are: 40°C. and pH 7.0 at a concentration of 3 to 4 x 10–3 M Na4P2O7 and an equivalent concentration of magnesium salt. The enzymatic hydrolysis of Na4P2O7 or K4P2O7 proceeds to completion and is irreversible under the conditions at which hydrolysis is occurring. Details are given of the method of isolation of the crystalline enzyme.

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Utilization of Agricultural Waste for the Production of Xylooligosaccharides Using Response Surface Methodology and Their In Vitro Prebiotic Efficacy

10.21203/rs.3.rs-748907/v2 ◽

2021 ◽

Author(s):

Nagamani Kathiresan ◽

Lingesh Gopal ◽

Vijay Karuppiah ◽

Renuka Naveenethan ◽

David Ravindran Abraham ◽

...

Keyword(s):

Response Surface Methodology ◽

Enzymatic Hydrolysis ◽

Response Surface ◽

Sugarcane Bagasse ◽

Agricultural Waste ◽

Relative Yield ◽

Value Added ◽

A Value ◽

Hydrolysis Of

Abstract Air pollution is a prominent problem recently faced in various parts of India due to the burning of stubbles (coconut husk, corn cob, paddy stubbles, sugarcane bagasse, etc.) which are rich in a lignocellulosic component that can be converted into a prebiotic known as Xylooliogsaccaride (XOS). They can be produced by autohydrolysis, acid hydrolysis and enzymatic hydrolysis of xylan. In the present study, Xylan was extracted from sugarcane bagasse using two alkalis (NaOH and KOH) and the yield was compared. Xylooligosaccharide produced by enzymatic hydrolysis and their factors influencing the yield were optimized using Response Surface Methodology. Xylan and Xylooligosaccharide was characterized by FTIR, NMR, XRD, TGA and ESI-MS. Xylooligosaccharides was investigated for their prebiotic potential by in vitro study. The maximum (Relative yield of 86%) yield of xylan was observed in 20% of NaOH. Xylan peaks at 3762cm− 1, 3347 cm− 1, 2917cm− 1 represents the OH and CH stretching of xylan. The main signals at 4.26 (H-1), 3.19 (H-2), 3.59 (H-3), 3.63 (H-4) and 3.98 (H-5) ppm determines the existence of xylan. The higher amount of XOS is pH 4.75, temperature 45°C, enzyme 4U/ml and for time of 16h. The spectrum of 5.0-5.40ppm and 4.30-4.60ppm represents the α anomeric and β anomeric protons in XOS. They are resistant digested and the reaching percentage to the intestine is 95% unhydrolyzed. The maximum prebiotic index was noted in L.plantarum (1.92) and L.fermentum (1.61). The highest prebiotic index and score was observed in L.plantarum (1.9) and L.fermentum (17). The maximum bacteriocin production of Enterococcus faecium against E.fecalis (13mm) and Streptococcus pyogenes (11mm). Therefore, utilization of agricultural residues for a value-added product not only shows a great impact on environmental issues but also could double the farmer’s income

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Inhitive ability collagenase of N-(cinnamyl) chitooligosaccharide derivative

Science and Technology Development Journal ◽

10.32508/stdj.v20ik3.1096 ◽

2017 ◽

Vol 20 (K3) ◽

pp. 83-91

Author(s):

Xuan Minh Le ◽

Khanh Duy Nguyen ◽

Khoa Dang Tran ◽

Tuan Quoc Tran ◽

Nghiep Dai Ngo

Keyword(s):

Molecular Weight ◽

Room Temperature ◽

Positive Control ◽

Living Systems ◽

Amino Groups ◽

Animal Cells ◽

Chemically Modified ◽

Mtt Method ◽

Hydrolysis Of ◽

Derivatives Of

Chitooligosaccharides (COS) with molecular weight 4633 Da and 84.67% of deacetylation were synthesized by hydrolysis of chitosan by cellulase at room temperature (33 ± 1 ° C). This COS, then, were chemically modified by grafting cinnamaldehyde at amino groups on the COS. Derivatives of N- (cinnamyl) chitooligosaccharides (CCOS) synthesized with 50.64% of yield and 72.22% of extent of substitution had inhibitory activity enzyme collagenase (a group of matrix metalloproteinases, enzyme family related to metastatic ability of cancer). Compared with the positive control, 58.23% of the effective to inhibit collagenase of CCOS at 1000 μg/ml concentrate. In addition, the CCOS cytotoxicity of CCOS was also assessed by MTT method, the results showed that non-toxic derivatives of animal cells and thus can be tested and applied in living systems.

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