scholarly journals Antioxidant, ACE-Inhibitory and Antimicrobial Activities of Kluyveromyces marxianus Protein Hydrolysates and Their Peptide Fractions

2016 ◽  
Vol 6 (7) ◽  
pp. 425 ◽  
Author(s):  
Mahta Mirzaei ◽  
Mahmoud Aminlari ◽  
Ebrahim Hosseini
Keyword(s):  
Enzymatic Hydrolysis ◽  
Antimicrobial Peptides ◽  
Kluyveromyces Marxianus ◽  
Protein Hydrolysate ◽  
Radical Scavenging ◽  
Protein Hydrolysates ◽  
Antimicrobial Protein ◽  
Degree Of Hydrolysis ◽  
Peptide Fractions ◽  
Ace Inhibitory

Background: There has been some evidence that proteins are potentially excellent source of antioxidants, antihypertensive and antimicrobial peptides and enzymatic hydrolysis is an effective method to release these peptides from protein molecules. The functional properties of protein hydrolysates depends on the protein substrate, the specificity of the enzymes, the conditions used during proteolysis, degree of hydrolysis, and the nature of peptides released including molecular weight, amino acid composition, and hydrophobicity.Context and purpose of this study: The biomass of Kluyveromyces marxianus was considered as a source of ACE inhibitory, antioxidant and antimicrobial peptides. Results: Autolysis and enzymatic hydrolysis were completed respectively, after 96 h and 5 h. Overall, trypsin (18.52% DH) and chymotrypsin (21.59% DH) treatments were successful in releasing antioxidant and ACE inhibitory peptides. Autolysate sample (39.51% DH) demonstrated a poor antioxidant and ACE inhibitory activity compared to trypsin and chymotrypsin hydrolysates. The chymotrypsin 3-5 kDa (301.6±22.81 μM TEAC/mg protein) and trypsin< 3 kDa (280.16±39.16) permeate peptide fractions showed the highest DPPH radical scavenging activity. The trypsin <3 kDa permeate peptide fraction showed the highest ABTS radical scavenging (1691.1±48.68 μMTE/mg protein) and ACE inhibitory (IC50=0.03±0.001 mg/ml) activities. The fraction (MW=5-10 kD) obtained after autolysis treatment showed antibacterial activity against St. aureus and Lis. monocytogenes in well diffusion screening. The minimum inhibitory concentration (MIC) value was 13.3 mg/ml against St. aureus and Lis. monocytogenes calculated by turbidimetric assay and it showed bactericidal activity against St. aureus at 21.3 mg/ml protein concentration. Conclusions: Taken together, the results of this study reveal that K. marxianus proteins contain specific peptides in their sequences which can be released by enzymatic hydrolysis and autolysis. Key words: Kluyveromyces marxianus; Antioxidant activity; ACE-inhibitory; Antimicrobial; Protein hydrolysate; Peptide 

scholarly journals Degree of Hydrolysis Affects the Techno-Functional Properties of Lesser Mealworm Protein Hydrolysates

Foods ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 381 ◽  
Author(s):  
Giulia Leni ◽  
Lise Soetemans ◽  
Augusta Caligiani ◽  
Stefano Sforza ◽  
Leen Bastiaens
Keyword(s):  
Enzymatic Hydrolysis ◽  
Functional Properties ◽  
Protein Hydrolysate ◽  
Preliminary Test ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Potential Implication ◽  
Alphitobius Diaperinus ◽  
Positive Effects ◽  
Lesser Mealworm

Protein hydrolysates from lesser mealworm (Alphitobius diaperinus, LM) were obtained by enzymatic hydrolysis with protease from Bacillus licheniformis. A preliminary test performed for five hours of hydrolysis generated an insect protein hydrolysate with 15% of degree of hydrolysis (DH), optimum solubility property and oil holding capacity, but emulsifying and foaming ability were completely impaired. In order to investigate the potential implication of DH on techno-functional properties, a set of protein hydrolysates with a different DH was obtained by sub-sampling at different time points during three hours of enzymatic hydrolysis process. An increase in DH% had positive effects on the solubility property and oil holding ability, while a reduced emulsifying ability was observed up to five hours of hydrolysis. These results demonstrated that the enzymatic hydrolysis, if performed under controlled conditions and not for a long period, represents a valid method to extract high quality protein from insects with tailored techno-functionality, in order to produce tailored ingredients for feed and food purpose.

Characterization, ACE inhibitory and Antioxidative Properties of Peptide Fractions Obtained from White Shrimp (Litopenaeus vannamei)

2021 ◽  
Vol 17 ◽  
Author(s):  
Juliana Latorres ◽  
Wilson Wasielesky Jr ◽  
Carlos Prentice
Keyword(s):  
Antioxidant Activity ◽  
Litopenaeus Vannamei ◽  
Reducing Power ◽  
Protein Hydrolysates ◽  
Raw Material ◽  
White Shrimp ◽  
Antihypertensive Activity ◽  
Degree Of Hydrolysis ◽  
Peptide Fractions ◽  
Ace Inhibitory

Background: Aquatic organisms are considered to be an important source of bioactive peptides with a high antioxidant and antihypertensive capacity. Therefore, the objective of this study was to hydrolyse peptide fractions from white shrimp (Litopenaeus vannamei) muscle by Alcalase and Protamex and to evaluate the angiotensin I-converting enzyme (ACE) inhibitory and the antioxidant activities. Methods: Protein hydrolysates of White shrimp were obtained by enzymatic hydrolysis using Alcalase and Protamex until the degree of hydrolysis reached 10% and 20%. Peptide fractions were obtained from White shrimp protein hydrolysates by ultrafiltration using membranes with sizes of 10 and 3 kDa. The antioxidant activity was evaluated for the three peptide fractions (F1: >10 kDa, F2: 3-10 kDa and F3: <3 kDa). To measure the antihypertensive activity, fractions with molecular sizes of less than 3 kDa were used. Results: The fractions obtained with Alcalase showed greater inhibitory effects on the ACE. In general, the molecular weight of the fractions influenced the antioxidant activity, with fractions smaller than 3 kDa having a high capacity for sequestering the DPPH radical, while peptide fractions with a size greater than 10 kDa presented higher reducing power. However, in capturing the ABTS radical, a high antioxidant capacity was observed for both fractions. Conclusion: The results suggest white shrimp would be an attractive raw material for the manufacture of antioxidant and anti-hypertensive nutraceutical ingredients.

scholarly journals ANTIOXIDANT ACTIVITY OF PROTEIN HYDROLYSATE PRODUCED FROM TUNA EYE (Thunnus sp.) BY ENZYMATIC HYDROLYSIS

2018 ◽  
Vol 21 (3) ◽  
pp. 522 ◽  
Author(s):  
Dewi Mutamimah ◽  
Bustami Ibrahim ◽  
Wini Trilaksani
Keyword(s):  
Antioxidant Activity ◽  
Enzymatic Hydrolysis ◽  
Protein Hydrolysate ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Degree Of Hydrolysis ◽  
Protective Agent ◽  
Ic50 Value ◽  
Canning Industry ◽  
Hydrolysis Of

Tuna (Thunnus sp.) by-products from frozen loin and canning industry especially the eye is rich in proteins and in lipids consisting of polyunsaturated fatty acids (PUFA). That requires protective agent (antioxidant) to inhibit the oxidation naturally present and predicted to be protein peptides. Enzymatic hydrolysis of protein is an appropriate method to produce bioactive peptide with such nutraceutical/pharmaceutical function such as an antioxidant peptide. This study aimed to produce protein hydrolysate having a function as anwith an antioxidant activity from eye of tuna through enzymatic hydrolysis and determining the antioxidant activity by DPPH methods. Protein soluble content of tuna’s eye protein hydrolysate (TEPH) ranged from 59.98±0.130 to 94.90±0.002%. The degree of hydrolysis (DH) of TEPH was about 9.10±0.28 to 16.14±0.09%. The highest inhibition of DPPH radical scavenging activity was 93.57±0.05% (at 5 mg/mL) was obtained with a DH of 11.35±0.002% at the concentration 0.1% of papain for 6 hours hydrolysis. The IC50 value of was 1.08±0.008 mg/mL

scholarly journals SCREENING POTENTIAL ANTIOXIDANT AND ANTIBACTERIAL ACTIVITIES OF PROTEIN HYDROLYSATES DERIVED FROM GERMINATED LABLAB BEAN, PIGEON PEA AND KIDNEY BEAN

2017 ◽  
Vol 1 (1) ◽  
pp. 24
Author(s):  
Ketut Ratnayani ◽  
Indriani Wisnu Susanto Panjaitan ◽  
Ni Made Puspawati
Keyword(s):  
Antioxidant Activity ◽  
Enzymatic Hydrolysis ◽  
Total Protein ◽  
Protein Hydrolysate ◽  
Biological Activities ◽  
Antibacterial Activities ◽  
Pigeon Pea ◽  
Protein Hydrolysates ◽  
Kidney Bean ◽  
Degree Of Hydrolysis

Abstract Protein hydrolysate contains a mixture of various lengths of short peptides chain and free amino acids that may excert biological activities. This research aims to screen potential antioxidant and antibacterial activities of protein hydrolysate produced from three kinds of germinated beans i.e. lablab bean (Lablab purpureus), pigeon pea (Cajanus cajan (L.) Millsp) and kidney bean (Phaseolus vulgaris) through enzymatic hydrolysis process. The steps of research included germination process of the beans prior to total protein isolation, enzymatic hydrolysis of total protein isolates using pancreatin enzyme, evaluation of in vitro antioxidant activity of the hydrolysates protein using DPPH (1,1-diphenyl-2-picryl hydrazyl) method, and antibaterial activity testing towards Eschericia coli and Staphyllococcus aureus bacteria. The results revealed that pancreatine enzyme was able to hydrolyse germinated protein of lablab bean, pigeon pea and kidney bean at the experiment condition applied with degree of hydrolysis 34.12%, 27.44%, and 30,93% respectively. It was also found that protein hydrolysates of lablab bean, pigeon pea, and kidney bean demonstrated antioxidant activity which percentage radical DPPH scavenging activity of 84.02%, 68.97% and 67.89 %. On the other hand, all of those protein hydrolysates did not show any antibacterial activity towards Eschericia coli and Staphyllococcus aureus bacteria.

scholarly journals Antioxidant and antihypertensive activities of wonderful cola (Buchholzia coriacea) seed protein and enzymatic protein hydrolysates

2018 ◽  
Vol 3 ◽  
pp. 133-143 ◽  
Author(s):  
Oluwole S. Ijarotimi ◽  
Sunday A. Malomo ◽  
Adeola M. Alashi ◽  
Ifeanyi D. Nwachukwu ◽  
Tayo N. Fagbemi ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Protein Hydrolysate ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Protein Isolate ◽  
Active Inhibitor ◽  
Spontaneously Hypertensive ◽  
Reducing Ability ◽  
Peptide Fractions

The aim of this work was to produce wonderful cola protein hydrolysate fractions with in vitro antioxidant properties coupled with blood pressure-reducing ability when orally administered to spontaneously hypertensive rats (SHRs). Wonderful cola protein isolate (WCI) was hydrolyzed with pancreatin to produce a hydrolysate (WCH), which was subjected to ultrafiltration separation using 1, 3, 5, and 10 kDa molecular weight cut-off membranes to obtain <1, 1–3, 3–5 and 5–10 kDa peptide fractions, respectively. The <1 and 1–3 kDa fractions had higher contents of arginine when compared to the 3–5 and 5–10 kDa peptides. The WCH and <1 kDa peptide fraction had significantly (p < 0.05) better DPPH radical scavenging (55–67%) and metal chelation (83–93%) activities but lower hydroxyl radical scavenging power (10–32%) than the WCI (46, 46 and 63%, respectively). The <1 kDa had significantly (p < 0.05) higher in vitro inhibition (80%) of angiotensin converting enzyme (ACE) activity while the 5–10 kDa was the most active inhibitor (90%) of renin activity. All peptide fractions so produced had better systolic and diastolic blood pressure-lowering effects than WCH and WCI. However, the <1 kDa fraction produced significantly (p < 0.05) stronger systolic (−33 mmHg) and diastolic (−30 mmHg) blood pressure reductions 6 h after oral gavage to SHRs. Thus, wonderful cola proteins contain encrypted bioactive peptides that may be used to formulate antioxidant and antihypertensive products.

scholarly journals Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates

2011 ◽  
Vol 20 (No. 1) ◽  
pp. 7-14 ◽  
Author(s):  
M. Hrčková ◽  
M. Rusňáková ◽  
J. Zemanovič
Keyword(s):  
Enzymatic Hydrolysis ◽  
Functional Properties ◽  
Aqueous Dispersion ◽  
Protein Hydrolysates ◽  
Soy Flour ◽  
Degree Of Hydrolysis ◽  
Defatted Soy Flour ◽  
Sds Page ◽  
Soy Protein Hydrolysates ◽  
Hydrolysis Of

Commercial defatted soy flour (DSF) was dispersed in distilled water at pH 7 to prepare 5% aqueous dispersion. Soy protein hydrolysates (SPH) were obtained by enzymatic hydrolysis of the DSF using three different proteases (Flavourzyme 1000 L, No-vozym FM 2.0 L and Alcalase 2.4 L FG). The highest degree of hydrolysis (DH 39.5) was observed in the presence of protease Flavourzyme. SPH were used for measuring functional properties (foaming stability, gelation). Treatment with Flavourzyme improved foaming of proteins of DSF. Foaming stability was low in the presence of Novozym. Proteases treated DSF showed good gelation properties, mainly in the case of treatment with Flavourzyme. SDS-PAGE analysis showed that after enzyme ad-dition to the 5% aqueous dispersion of DSF each enzyme degraded both b-conglycinin and glycinin. In general, the basic polypeptide from glycinin showed the highest resistance to proteolytic activity. The most abundant free amino acids in the hydrolysates were histidine (30%), leucine (24%) and tyrosine (19%) in the case of the treatment with proteases Alcalase and Novozym, and arginine (22.1%), leucine (10.6%) and phenylalanine (12.9%) in the case of the treatment with Flavourzyme. &nbsp;

scholarly journals Debittering of Protein Hydrolysates by Lactobacillus LBL-4 Aminopeptidase

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Bozhidar Tchorbanov ◽  
Margarita Marinova ◽  
Lydia Grozeva
Keyword(s):  
Culture Media ◽  
Protein Hydrolysate ◽  
Protein Hydrolysates ◽  
Cell Protein ◽  
Degree Of Hydrolysis ◽  
Gel Chromatography ◽  
Cell Free Extract ◽  
Food Grade ◽  
Enzyme Action

Yoghurt strain Lactobacillus LBL-4 cultivated for 8–10 h at pH ~6.0 was investigated as a considerable food-grade source of intracellular aminopeptidase. Cell-free extract manifesting >200 AP U/l was obtained from cells harvested from 1 L culture media. Subtilisin-induced hydrolysates of casein, soybean isolate, and Scenedesmus cell protein with degree of hydrolysis 20–22% incubated at 45∘C for 10 h by 10 AP U/g peptides caused an enlarging of DH up to 40–42%, 46–48%, and 38–40% respectively. The DH increased rapidly during the first 4 h, but gel chromatography studies on BioGel P-2 showed significant changes occurred during 4–10 h of enzyme action when the DH increased gradually. After the digestion, the remained AP activity can be recovered by ultrafiltration (yield 40–50%). Scenedesmus protein hydrolysate with DH 20% was inoculated by Lactobacillus LBL-4 cells, and after 72 h cultivation the DH reached 32%. The protein hydrolysates (DH above 40%) obtained from casein and soybean isolate (high Q value) demonstrated a negligible bitterness while Scenedesmus protein hydrolysates (low Q value) after both treatments were free of bitterness.

Antioxidant Properties of Microalgae Protein Hydrolysates Prepared by Neutral Protease Digestion

2014 ◽  
Vol 707 ◽  
pp. 149-153 ◽  
Author(s):  
Xiao Hu ◽  
Xian Qing Yang ◽  
Lai Hao Li ◽  
Yan Yan Wu ◽  
Wan Ling Lin ◽  
...  
Keyword(s):  
Antioxidant Activities ◽  
Radical Scavenging Activity ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Protein Hydrolysates ◽  
Neutral Protease ◽  
Degree Of Hydrolysis ◽  
Protease Digestion ◽  
Hydrolysis Of

Microalgae protein hydrolysates (MPH) were obtained by enzymatic hydrolysis of defatted microalgae meal using neutral protease. The protein recovery, degree of hydrolysis, and the antioxidant activities of the hydrolysates were investigated. The results demonstrated that hydrolysates prepared by neutral protease at 50 °C for 4 h exhibited the strongest antioxidant activity. Under these conditions, the 1,1-diphenyl-2-picrylhydrazyl (DPPH), hydroxyl radical scavenging activity and the reducing power of the hydrolysates were 68.3%, 50.8% and 1.303, respectively.

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