scholarly journals Purification and Identification of Cholesterol Micelle Formation Inhibitory Peptides of Hydrolysate from High Hydrostatic Pressure-Assisted Protease Hydrolysis of Fermented Seabass Byproduct

2021 ◽  
Vol 22 (10) ◽  
pp. 5295
Author(s):  
Guan-Wen Chen ◽  
Hong-Ting Victor Lin ◽  
Li-Wen Huang ◽  
Chia-Hua Lin ◽  
Yu-Hsin Lin
Keyword(s):  
Inhibitory Activity ◽  
Gel Filtration ◽  
Micelle Formation ◽  
Sea Bass ◽  
Hydrolysis Time ◽  
Inhibitory Peptides ◽  
Freeze Dried ◽  
Inhibitory Efficiency ◽  
Gastrointestinal Enzymes ◽  
Hydrolysis Of

This research focuses on the proteolytic capacity of sea bass byproduct (SB) and their hypocholesterolemic activity via the cholesterol micelle formation (CMF) inhibition. SB was fermented with seven mixed lactic acid bacteria for 5 h at 42 °C. The lactic fermented SB was hydrolyzed with Protease N for 6 h under HHP to obtain the SB hydrolysates (HHP-assisted Protease N hydrolysis after fermentation, F-HHP-PN6). The supernatant was separated from the SB hydrolysate and freeze-dried. As the hydrolysis time extended to 6 h, soluble protein content increased from 187.1 to 565.8 mg/g, and peptide content increased from 112.8 to 421.9 mg/g, while inhibition of CMF increased from 75.0% to 88.4%. Decreasing the CMF inhibitory activity from 88.4% to 42.1% by simulated gastrointestinal digestion (FHHP-PN6 was further hydrolyzed by gastrointestinal enzymes, F-HHP-PN6-PP) reduced the CMF inhibitory activity of F-HHP-PN6. Using gel filtration chromatography, the F-HHP-PN6-PP was fractioned into six fractions. The molecular weight of the fifth fraction from F-HHP-PN6-PP was between 340 and 290 Da, and the highest inhibitory efficiency ratio (IER) on CMF was 238.9%/mg/mL. Further purification and identification of new peptides with CMF inhibitory activity presented the peptide sequences in Ser-Ala-Gln, Pro-Trp, and Val-Gly-Gly-Thr; the IERs were 361.7, 3230.0, and 302.9%/mg/mL, respectively.

scholarly journals The analysis of Angiotensin-I Converting Enzyme (ACE) by maitake (Grifrola frondosa) mycelia

2021 ◽  
Vol 8 (2) ◽  
pp. 69-72
Author(s):  
Yuen Sim Kheng ◽  
Young Liew Jeng ◽  
Maryana Mohamad Nor ◽  
Geng Boon Jia
Keyword(s):  
Inhibitory Activity ◽  
Protein Concentration ◽  
Bioactive Peptides ◽  
Biological Properties ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Hydrolysis Time ◽  
Angiotensin I Converting Enzyme ◽  
Freeze Dried

The Maitake (Grifola frondosa) is useful in treating diseases, specifically hypertension. Research on the maitake mycelia’s biological properties, nevertheless, are limited in the literature. This study aimed to (i) produce mushroom biomass adopting submerged fermentation, and (ii) investigate the Angiotensin-I Converting Enzyme inhibitory activity. Maitake mycelia’s yield after 14 days of fermentation under controlled conditions (approx. 1.32 g/L) were freeze-dried into powder and later were hydrolysed for analyses of Angiotensin-I Converting Enzyme inhibitory activity. Current results showed that the degree of hydrolysis increased in line with hydrolysis time, as the protein concentration for hydrolysed sample was 283.61 ± 7.14 µg/mL, however, the non-hydrolysed sample resulted in lesser protein content (46.76 ± 1.09 µg/mL). The hydrolysate maitake mycelia has higher Angiotensin-I Converting Enzyme inhibitory activity (46.48%) as compared to the non-hydrolysate maitake mycelia (20.19 ± 0.17%). This finding suggested maitake mycelia hydrolysate can be a source of potential bioactive peptides used in treating hypertension.

scholarly journals Dipeptidyl Peptidase-IV Inhibitory Activity and Related Molecular Mechanism of Bovine α-Lactalbumin-Derived Peptides

Molecules ◽  
2020 ◽  
Vol 25 (13) ◽  
pp. 3009
Author(s):  
Jing Gao ◽  
Han Gong ◽  
Xueying Mao
Keyword(s):  
Liquid Chromatography ◽  
Inhibitory Activity ◽  
High Performance ◽  
Gel Filtration ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Salt Bridges ◽  
Docking Analysis ◽  
Inhibitory Peptides ◽  
Dpp Iv

Identifying DPP-IV inhibitory peptides from dietary protein has attracted increased attention. In the present study, bovine α-lactalbumin hydrolysates were generated by alcalase for various hydrolysis times, and DPP-IV inhibitory activity of these hydrolysates was determined. The 4 h hydrolysates displayed the most potent DPP-IV inhibitory activity, with DPP-IV inhibition rate of 82.30 ± 1.39% at concentration of 1.0 mg/mL. DPP-IV inhibitory peptides were isolated from the 4 h-hydrolysates with gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC). Using liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI MS/MS), two DPP-IV inhibitory peptides were identified, and their amino acid sequences were Glu-Leu-Lys-Asp-Leu-Lys-Gly-Tyr (ELKDLKGY) and Ile-Leu-Asp-Lys-Val-Gly-Ile-Asn-Tyr (ILDKVGINY), respectively. Furthermore, molecular docking analysis showed that peptides ELKDLKGY and ILDKVGINY could form hydrogen bonds, pi-cation interactions, and salt bridges with DPP-IV. These findings indicated that bovine α-lactalbumin may be a potential source of natural DPP-IV inhibitor.

scholarly journals Preparation of ACE Inhibitory Peptides fromMytilus coruscusHydrolysate Using Uniform Design

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Jin-Chao Wu ◽  
Jie Cheng ◽  
Xiao-lai Shi
Keyword(s):  
Inhibitory Activity ◽  
Uniform Design ◽  
Composition Analysis ◽  
Ace Inhibitory Activity ◽  
Hydrolysis Time ◽  
Inhibitory Peptides ◽  
Mytilus Coruscus ◽  
Ace Inhibitory Peptides ◽  
Hydrolysis Conditions ◽  
Ace Inhibitory

The angiotensin-I-converting enzyme (ACE) inhibitory peptides from mussel,Mytilus coruscus, were investigated and the variable factors, protease concentration, hydrolysis time, pH, and temperature, were optimized using Uniform Design, a new statistical experimental method. The results proved that the hydrolysate of alkali proteases had high ACE-inhibitory activity, especially the alkali protease E1. Optimization by Uniform Design showed that the best hydrolysis conditions for preparation of ACE-inhibitory peptides fromMytilus coruscuswere protease concentration of 36.0 U/mL, hydrolysis time of 2.7 hours, pH 8.2, and Temperature at 59.5°C, respectively. The verification experiments under optimum conditions showed that the ACE-inhibitory activity (91.3%) were agreed closely with the predicted activity of 90.7%. The amino acid composition analysis ofMytilus coruscusACE-inhibitory peptides proved that it had high percent of lysine, leucine, glycine, aspartic acid, and glutamic acid.

Mechanism of Inhibitory Action on Platelet Activation of a Phospholipase A2 Isolated from Lachesis muta (Bushmaster) Snake Venom

1997 ◽  
Vol 78 (05) ◽  
pp. 1372-1380 ◽  
Author(s):  
André L Fuly ◽  
Olga L T Machado ◽  
Elias W Alves ◽  
Célia R Carlinis
Keyword(s):  
Platelet Aggregation ◽  
Enzymatic Activity ◽  
Phospholipase A2 ◽  
Inhibitory Activity ◽  
Thermal Inactivation ◽  
Anticoagulant Activity ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Crude Venom ◽  
Lachesis Muta

SummaryCrude venom from Lachesis muta exhibited procoagulant, proteolytic and phospholipase A2 activities. A phospholipase A2, denoted LM-PLA2 was purified from L. muta venom to homogeneity, through a combination of chromatographic steps involving gel-filtration on Sephacryl S-200 HR and reverse phase chromatography on a C2/C18 column. LM-PLA2 presented a single polypeptide chain with an isoelectric point at pH 4.7 and apparent molecular weight of 17 kDa. Partial aminoacid sequence indicated a high degree of homology for LM-PLA2 with other PLA2 from different sources.LM-PLA2 displayed a potent enzymatic activity as measured by indirect hemolysis of red blood cells but it was neither lethal when injected i.p. into mice nor did it present anticoagulant activity. Furthermore, LM-PLA2 displayed a moderate inhibitory activity on the aggregation of rabbit platelets induced by low levels of ADP, thrombin and arachidonate. In contrast, platelet aggregation induced by high doses of collagen was strongly inhibited by LM-PLA2 as well as ATP-release. Treatment of the protein with p-bromophenacyl bromide or 2-mercapto-ethanol, as well as thermal inactivation studies, suggested that the platelet inhibitory effect of LM-PLA2 is dependent on its enzymatic activity. Thus, the platelet inhibitory activity of LM-PLA2 was shown to be dependent on the hydrolysis of plasma phospholipids and/or lipoproteins, most probably those rich in phosphatidylcholine. Surprisingly, lyso-phosphatidylcholine released by LM-PLA2 from plasma was shown to preferentially inhibited collagen-induced platelet aggregation, in contrast to other PLA2s, whose plasma hydrolytic products indistinctly affect platelet’s response to several agonists.

scholarly journals The effect of drying temperature on the properties of gelatin from carps (Cyprinus carpio) skin

2019 ◽  
Vol 37 (No. 4) ◽  
pp. 246-251 ◽  
Author(s):  
Joanna Tkaczewska ◽  
Maciej Wielgosz ◽  
Piotr Kulawik ◽  
Marzena Zajac
Keyword(s):  
Cyprinus Carpio ◽  
Freeze Drying ◽  
Treatment Method ◽  
Thermal Hydrolysis ◽  
Gel Properties ◽  
Drying Temperature ◽  
Freeze Dried ◽  
Different Temperatures ◽  
Pre Treatment ◽  
Hydrolysis Of

The influence of drying temperature on the characteristics and gel properties of gelatine from Cyprinus carpio L. skin was studied. Gelatine was extracted from the carp skin using NaOH and ethanol pre-treatment method, extracted in water in 45°C and then dried in 4 different temperatures: 50, 70, 80°C and freeze-dried. The  electrophoresis and functional properties of gelatines were investigated. Freeze drying allowed to obtain a high gelling force, and all other methods did not give satisfactory results. The proteins in gelatines dried at higher temperatures separated by electrophoresis gave severely blurred bands. It may be explained by thermal hydrolysis of collagen fibrils. Freeze drying is the only effective method for drying this product, which can be used in industry.

scholarly journals Effect of Different Proteases on the Degree of Hydrolysis and Angiotensin I-Converting Enzyme-Inhibitory Activity in Goat and Cow Milk

Biomolecules ◽  
2018 ◽  
Vol 8 (4) ◽  
pp. 101 ◽  
Author(s):  
Guowei Shu ◽  
Jie Huang ◽  
Chunju Bao ◽  
Jiangpeng Meng ◽  
He Chen ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Goat Milk ◽  
Cow Milk ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Angiotensin I-converting enzyme (ACE) peptides are bioactive peptides that have important value in terms of research and application in the prevention and treatment of hypertension. While widespread literature is concentrated on casein or whey protein for production of ACE-inhibitory peptides, relatively little information is available on selecting the proper proteases to hydrolyze the protein. In this study, skimmed cow and goat milk were hydrolyzed by four commercial proteases, including alkaline protease, trypsin, bromelain, and papain. Angiotensin I-converting enzyme-inhibitory peptides and degree of hydrolysis (DH) of hydrolysates were measured. Moreover, we compared the difference in ACE-inhibitory activity between cow and goat milk. The results indicated that the DH increased with the increase in hydrolysis time. The alkaline protease-treated hydrolysates exhibited the highest DH value and ACE-inhibitory activity. Additionally, the ACE-inhibitory activity of hydrolysates from goat milk was higher than that of cow milk-derived hydrolysates. Therefore, goat milk is a good source to obtain bioactive peptides with ACE-inhibitory activity, as compared with cow milk. A proper enzyme to produce ACE-inhibitory peptides is important for the development of functional milk products and will provide the theoretical basis for industrial production.

scholarly journals Gel Filtration Chromatographic Study on the Micelle Formation of Triton X-100

1989 ◽  
Vol 62 (6) ◽  
pp. 1725-1730 ◽  
Author(s):  
Noriaki Funasaki ◽  
Sakae Hada ◽  
Saburo Neya
Keyword(s):  
Gel Filtration ◽  
Micelle Formation ◽  
Chromatographic Study ◽  
Triton X

Hydrolysis of intralipid by pancreatic lipase and phospholipase A2-gel filtration studies

Lipids ◽  
1985 ◽  
Vol 20 (11) ◽  
pp. 765-772 ◽  
Author(s):  
Renée Grataroli ◽  
Monique Charbonnier ◽  
Gilles Nalbone ◽  
Denis Lairon ◽  
Christiane Chabert ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Pancreatic Lipase ◽  
Gel Filtration ◽  
Hydrolysis Of

scholarly journals Purification and properties of three (1→3)-β-d-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)

1993 ◽  
Vol 289 (2) ◽  
pp. 453-461 ◽  
Author(s):  
M Hrmova ◽  
G B Fincher
Keyword(s):  
Hordeum Vulgare ◽  
Elevated Temperatures ◽  
Gel Filtration ◽  
Degree Of Polymerization ◽  
Exchange Chromatography ◽  
Purification And Properties ◽  
Young Leaves ◽  
Monomeric Proteins ◽  
Ph Range ◽  
Hydrolysis Of

Three (1->3)-beta-D-glucan glucanohydrolase (EC 3.2.1.39) isoenzymes GI, GII and GIII were purified from young leaves of barley (Hordeum vulgare) using (NH4)2SO4 fractional precipitation, ion-exchange chromatography, chromatofocusing and gel-filtration chromatography. The three (1->3)-beta-D-glucanases are monomeric proteins of apparent M(r)32,000 with pI values in the range 8.8-10.3. N-terminal amino-acid-sequence analyses confirmed that the three isoenzymes represent the products of separate genes. Isoenzymes GI and GII are less stable at elevated temperatures and are active over a narrower pH range than is isoenzyme GIII, which is a glycoprotein containing 20-30 mol of hexose equivalents/mol of enzyme. The preferred substrate for the enzymes is laminarin from the brown alga Laminaria digitata, an essentially linear (1->3)-beta-D-glucan with a low degree of glucosyl substitution at 0-6 and a degree of polymerization of approx. 25. The three enzymes are classified as endohydrolases, because they yield (1->3)-beta-D-oligoglucosides with degrees of polymerization of 3-8 in the initial stages of hydrolysis of laminarin. Kinetic analyses indicate apparent Km values in the range 172-208 microM, kcat. constants of 36-155 s-1 and pH optima of 4.8. Substrate specificity studies show that the three isoenzymes hydrolyse substituted (1->3)-beta-D-glucans with degrees of polymerization of 25-31 and various high-M(r), substituted and side-branched fungal (1->3;1->6)-beta-D-glucans. However, the isoenzymes differ in their rates of hydrolysis of a (1->3;1->6)-beta-D-glucan from baker's yeast and their specific activities against laminarin vary significantly. The enzymes do not hydrolyse (1->3;1->4)-beta-D-glucans, (1->6)-beta-D-glucan, CM-cellulose, insoluble (1->3)-beta-D-glucans or aryl beta-D-glycosides.

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