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 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.

Comparison of Yield, Antioxidant Activity and Functional Properties of Protein Hydrolysates from Tuna and Pollock Frame

2012 ◽  
Vol 554-556 ◽  
pp. 1327-1331
Author(s):  
Li Jun Zhang ◽  
Qian Cheng Zhao ◽  
Bing Bing Wang ◽  
Xue Wan ◽  
Zhi Bo Li ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Functional Properties ◽  
Protein Hydrolysate ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Basic Composition ◽  
Foaming Ability ◽  
Hydrolysis Of ◽  
Better Than

Protein hydrolysates from Tuna frame (TFPH) and Pollock frame (PFPH) were prepared by papain, respectively.The yield, the basic composition content, the antioxidant activity and functional properties (solubility, emulsifying and foaming ability) and the degree of hydrolysis of the protein hydrolysates were evaluated. Results suggest that solubility, antioxidant activity of protein hydrolysate from Pollock frame are better than that of tuna frame, but the yield is lower than that of tuna frame.

scholarly journals Effects of Enzymatic Hydrolysis on the Functional Properties, Antioxidant Activity and Protein Structure of Black Soldier Fly (Hermetia illucens) Protein

Insects ◽  
2020 ◽  
Vol 11 (12) ◽  
pp. 876
Author(s):  
Inayat Batish ◽  
Devon Brits ◽  
Pedro Valencia ◽  
Caio Miyai ◽  
Shamil Rafeeq ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Protein Structure ◽  
Amino Acid ◽  
Enzymatic Hydrolysis ◽  
Functional Properties ◽  
Amino Acid Content ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Protein Concentrate ◽  
Black Soldier Fly

The effects of chemical protein extraction, and enzymatic hydrolysis with Alcalase, papain and pepsin, on the functional properties, antioxidant activity, amino acid composition and protein structure of black soldier fly (H. illucens) larval protein were examined. Alcalase hydrolysates had the highest degree of hydrolysis (p < 0.05), with the highest hydrolysate and oil fraction yield (p < 0.05). Pepsin hydrolysates showed the lowest oil holding capacity (p < 0.05), whereas no significant differences were observed among other enzymes and protein concentrates (p > 0.05). The emulsifying stability and foam capacity were significantly lower in protein hydrolysates than protein concentrate (p < 0.05). The antioxidant activity of protein hydrolysates from protein concentrate and Alcalase was higher than that with papain and pepsin (p < 0.05), owing to the higher hydrophobic amino acid content. Raman spectroscopy indicated structural changes in protein α-helices and β-sheets after enzymatic hydrolysis.

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 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 Production and characteristics of fish protein hydrolysate from parrotfish (Chlorurus sordidus) head

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e8297 ◽  
Author(s):  
Asep A. Prihanto ◽  
Rahmi Nurdiani ◽  
Annas D. Bagus
Keyword(s):  
Antioxidant Activity ◽  
Protein Hydrolysate ◽  
Essential Amino Acids ◽  
Amino Acid Profile ◽  
Industrial Applications ◽  
Control Treatment ◽  
Degree Of Hydrolysis ◽  
Fish Protein ◽  
Fish Protein Hydrolysate ◽  
High Level

Background Fish byproducts are commonly recognized as low-value resources. In order to increase the value, fish byproducts need to be converted into new products with high functionality such as fish protein hydrolysate (FPH). In this study, FPH manufactured from parrotfish (Chlorurus sordidus) heads using different pH, time and sample ratio was investigated. Methods Hydrolysis reactions were conducted under different pHs (5, 7, and 9) and over different durations (12 and 24 h). Control treatment (without pH adjustment (pH 6.4)) and 0 h hydrolsisis duration were applied. Hydrolysates were characterized with respect to proximate composition, amino acid profile, and molecular weight distribution. The antioxidant activity of the hydrolysate was also observed. Results The pH and duration of hydrolysis significantly affected (p < 0.05) the characteristics of FPH. The highest yield of hydrolysate (49.04 ± 0.90%), with a degree of hydrolysis of 30.65 ± 1.82%, was obtained at pH 9 after 24 h incubation. In addition, the FPH had high antioxidant activity (58.20 ± 0.55%), with a high level of essential amino acids. Results suggested that FPH produced using endogenous enzymes represents a promising additive for food and industrial applications.

A novel Synthesis, Chemical Characterization and Biological Activities of Metal-Leather Protein Hydrolysate Chelates

2021 ◽  
Author(s):  
Rania Jacob ◽  
Hazem Hassan ◽  
Adel Afify ◽  
Gamal Gabr
Keyword(s):  
Melting Point ◽  
Protein Hydrolysate ◽  
Biological Activities ◽  
Chemical Characterization ◽  
Antibacterial Activities ◽  
Biochemical Properties ◽  
Mineral Salts ◽  
Mineral Absorption ◽  
E Coli ◽  
Leather Processing

Abstract Leather industries covers a wide chain of production and indirectly contributes to the economic flow. The different stages used in leather processing led to produce huge solid waste volumes. Because of the great effectiveness of amino acids as naturally chelates for minerals, the present study was carried out to recycling leather waste into its protein hydrolysate by CaO hydrolysis. The Leather protein hydrolysates (LPHs) was used to prepare metal-leather protein hydrolysate chelates (Cu2+-, Zn2+-& Fe2+-LPHCs) and some of their physical properties (i.e. λ-max, FTIR spectra, color, melting point) and biochemical properties as its antibacterial activity, as well as using as micronutrient elements for plant were evaluated. Results showed that the Cu2+-LPHC gave the highest value of melting point and λ-max than other chelates. All chelates shifted the vibration bands toward a higher frequency than LPH/CaO. Metal-leather protein hydrolysate (M-LPHCs) had antibacterial activities against E. coli, B. cereus and Micrococcus spp. mostly with Zn-LPHC and Fe-LPHC. These complexes also increased the growth characteristics and mineral absorption of spinach plants in hydroponic nutrient solution than that of mineral salts (CuSO4, ZnSO4 and FeSO4). Finally, the study concluded that M-LPHCs can be used as antimicrobial agent, micronutrients for plant and support the minerals bioavailability in animals.

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.

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