Proteolytic hydrolysis of cowpea proteins is able to release peptides with hypocholesterolemic activity

2015 ◽  
Vol 77 ◽  
pp. 43-48 ◽  
Author(s):  
Marcelo Rodrigues Marques ◽  
Gustavo Guadagnucci Fontanari ◽  
Daniel Carvalho Pimenta ◽  
Rosana Manólio Soares-Freitas ◽  
José Alfredo Gomes Arêas
Keyword(s):  
Hydrolysis Of ◽  
Proteolytic Hydrolysis ◽  
Cowpea Proteins

Proteolytic Hydrolysis of the Antitumor Peptide HLDF-6-AA in Blood Plasma

2019 ◽  
Vol 45 (5) ◽  
pp. 347-352
Author(s):  
Yu. A. Zolotarev ◽  
A. K. Dadayan ◽  
V. S. Kozik ◽  
S. I. Shram ◽  
I. Yu. Nagaev ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Hydrolysis Of ◽  
Proteolytic Hydrolysis ◽  
In Blood Plasma

Determination of proteolytic hydrolysis of thyroglobulin

1991 ◽  
Vol 566 (2) ◽  
pp. 471-480 ◽  
Author(s):  
Eugène H.J.M. Jansen ◽  
Lambert Doorn ◽  
F.X. Rolaf van Leeuwen
Keyword(s):  
Hydrolysis Of ◽  
Proteolytic Hydrolysis

Proteolytic hydrolysis of muscle proteins of harp seal (Phoca groenlandica)

1994 ◽  
Vol 42 (11) ◽  
pp. 2634-2638 ◽  
Author(s):  
Fereidoon Shahidi ◽  
Jozef Synowiecki ◽  
Jerzy Balejko
Keyword(s):  
Harp Seal ◽  
Muscle Proteins ◽  
Phoca Groenlandica ◽  
Hydrolysis Of ◽  
Proteolytic Hydrolysis

scholarly journals OPTIMIZATION FOR BATCH PROTEOLYTIC HYDROLYSIS OF SPENT BREWER’S YEAST BY USING PROTEASES

2018 ◽  
Vol 54 (4A) ◽  
pp. 181
Author(s):  
Nguyen Thi Thanh Ngoc
Keyword(s):  
Ph Value ◽  
Degree Of Hydrolysis ◽  
Optimal Conditions ◽  
Brewer’S Yeast ◽  
Hydrolysis Time ◽  
Brewer's Yeast ◽  
Factors Influencing ◽  
Hydrolysis Temperature ◽  
Hydrolysis Of ◽  
Proteolytic Hydrolysis

The yield of proteolylic hydrolysis for spent brewer’s yeast by protease and aminoacid contents of hydrolysates (the main  factors influencing in taste of hydrolysed product) depends on factors influencing in catalytic activities of enzymes as temperature, pH value, type of used  enzymes and ratio enzyme/substrate. With the purpose to hydrolyse the spent brewer’s yeast for food application, bitterness of hydrolysate takes the firth consideration, and than the yield of hydrolysing process plays economic role. In this paper, it is dealt with determination of optimal conditions to obtain the highest yield of hydrolysis process and the lowest bitterness of hydrolysate (the bitterness is determined by sensory evaluation, expressed equivalently with concentration of quinine). Response surface methodology (RSM) was used to determine optimum condition for batch proteolytic hydrolysis of spent brewer’s yeast. The influencing factors were investigated as temperature (X1): 40 oC–60 oC; pH (X2): 6.0–9.0, ratio E (flavourzyme)/S (X3): 5–10 U/g and hydrolysis time (X4): 6–9 hours. The experimental responses including degree of hydrolysis (Y1) (%) and bitterness of hydrolysate (Y2) (μmol quinine/ml) are performed in second-degree model. The optimal conditions for obtaining high degree of hydrolysis and low bitterness are determined: Ratio of enzyme mixture (alcalase 7.5 U/g and flavourzyme 8.5 U/g), pH 7.5, hydrolysis temperature at 52oC and hydrolysis time 9 hours. Under the optimal conditions, the actual values obtained for the yield of hydrolysis was 40.81  ± 0.044 % and the bitterness equivalently with concentration of quinine was 16.37 ± 0.03 μmol quinine/ml.

scholarly journals The Effects of a Novel Series of KTTKS Analogues on Cytotoxicity and Proteolytic Activity

Molecules ◽  
2019 ◽  
Vol 24 (20) ◽  
pp. 3698 ◽  
Author(s):  
Urszula Tałałaj ◽  
Paulina Uścinowicz ◽  
Irena Bruzgo ◽  
Arkadiusz Surażyński ◽  
Ilona Zaręba ◽  
...  
Keyword(s):  
Biological Effects ◽  
Stable Form ◽  
Test Results ◽  
Dna Biosynthesis ◽  
Lysine Modification ◽  
Amide Form ◽  
Plasmin Inhibitors ◽  
Hydrolysis Of ◽  
Proteolytic Hydrolysis

KTTKS is a matrikine that originates from the proteolytic hydrolysis of collagen. This peptide stimulates ECM production and types I and III collagen expression in vitro. A more stable form of KTTKS is pal-KTTKS, known as Matrixyl® or palmitoyl pentapeptide-3. A series of novel pentapeptides, analogues of KTTKS with the general formula X-KTTKS-OH(NH2), where X = acetyl, lipoyl, palmitoyl residues, was designed and synthesized. Their effect on amidolytic activity of urokinase, thrombin, trypsin, plasmin, t-PA, and kallikrein were tested. Cytotoxic tests on fibroblasts, as well as collagen and DNA biosynthesis tests for selected peptides, were also carried out. The test results showed that the most active plasmin inhibitors were palmitoyl peptides, whether in acid or amide form. No biological effects of lysine modification to arginine in the synthesized peptides were found. None of the synthesized peptides was not cytotoxic on fibroblasts, and three of them showed cell growth. These three compounds showed no concentration-activity relationship in the collagen and DNA biosynthesis assays.

scholarly journals Optimization for continuous overflow proteolytic hydrolysis of spent brewer’s yeast by using proteases

2018 ◽  
Vol 14 (4) ◽  
pp. 735-742
Author(s):  
Nguyen Thi Thanh Ngoc ◽  
Quan Le Ha ◽  
Dinh Van Thuan
Keyword(s):  
Ph Value ◽  
Degree Of Hydrolysis ◽  
Optimal Conditions ◽  
Brewer’S Yeast ◽  
Hydrolysis Time ◽  
Brewer's Yeast ◽  
Hydrolysis Process ◽  
Amino Acid Contents ◽  
Hydrolysis Of ◽  
Proteolytic Hydrolysis

A large amount of spent yeast as by-product is annually generated from brewing industry and it contains about 50-55% protein with good balance of amino acids. The hydrolysate produced from spent brewer’s yeast may be used in food application. The yield of proteolylic hydrolysis for spent brewer’s yeast and amino acid contents of hydrolysates depend on factors such as temperature, pH value, type of used enzyme and ratio enzyme/substrate, time. Besides, applied hydrolysing methods (batch-, or continuous method) has effected on degree of hydrolysis. With the purpose of how proteolytic hydrolysis having effects on the spent brewer’s yeast for food application in industrial scale, continuous overflow method was used in this study. Bitterness of hydrolysate and the yield of continuous overflow proteolytic hydrolysis process are the two interested factors for protein hydrolysis. In this report, it is dealt with determination for optimal conditions to obtain the highest yield of hydrolysis process and the lowest bitterness of hydrolysate. Response surface methodology (RSM) was used to determine optimal condition for continuous overflow proteolytic hydrolysis of spent brewer’s yeast. The optimal conditions for obtaining high degree of hydrolysis and low bitterness are determined as followings: ratio of enzyme mixture (alcalase 7.5 U/g and flavourzyme 10 U/g), pH at 7.5, hydrolysis temperature at 51oC and hydrolysis time of 9 hours. Under the optimal conditions, the yield of hydrolysis was 59.62% ± 0.027 and the bitterness equivalently with concentration of quinine was 7.86 ± 0.033 μmol /ml.

Fine Structural Localization of Acyltransferases Involved in Lipid Synthesis in Intestinal Mucosa.

1970 ◽  
Vol 28 ◽  
pp. 54-55
Author(s):  
R. J. Barrnett ◽  
J. A. Higgins
Keyword(s):  
Smooth Endoplasmic Reticulum ◽  
Lipid Synthesis ◽  
Mucosal Cell ◽  
Structural Localization ◽  
Morphological Studies ◽  
Mucosal Cells ◽  
Initial Appearance ◽  
Sh Group ◽  
Hydrolysis Of ◽  
Intestinal Mucosal Cells

The main products of intestinal hydrolysis of dietary triglycerides are free fatty acids and monoglycerides. These form micelles from which the lipids are absorbed across the mucosal cell brush border. Biochemical studies have indicated that intestinal mucosal cells possess a triglyceride synthesising system, which uses monoglyceride directly as an acylacceptor as well as the system found in other tissues in which alphaglycerophosphate is the acylacceptor. The former pathway is used preferentially for the resynthesis of triglyceride from absorbed lipid, while the latter is used mainly for phospholipid synthesis. Both lipids are incorporated into chylomicrons. Morphological studies have shown that during fat absorption there is an initial appearance of fat droplets within the cisternae of the smooth endoplasmic reticulum and that these subsequently accumulate in the golgi elements from which they are released at the lateral borders of the cell as chylomicrons.We have recently developed several methods for the fine structural localization of acyltransferases dependent on the precipitation, in an electron dense form, of CoA released during the transfer of the acyl group to an acceptor, and have now applied these methods to a study of the fine structural localization of the enzymes involved in chylomicron lipid biosynthesis. These methods are based on the reduction of ferricyanide ions by the free SH group of CoA.

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