Search results for: Pepsin

Authors: Ivan Živanović, Žužana Vaštag, Senka Popović, Ljiljana Popović, Draginja Peričin

Abstract:

The present work represents an investigation of the hydrolysis of hull-less pumpkin (Cucurbita Pepo L.) oil cake protein isolate (PuOC PI) by pepsin. To examine the effectiveness and suitability of pepsin towards PuOC PI the kinetic parameters for pepsin on PuOC PI were determined and then, the hydrolysis process was studied using Response Surface Methodology (RSM). The hydrolysis was carried out at temperature of 30°C and pH 3.00. Time and initial enzyme/substrate ratio (E/S) at three levels were selected as the independent parameters. The degree of hydrolysis, DH, was mesuared after 20, 30 and 40 minutes, at initial E/S of 0.7, 1 and 1.3 mA/mg proteins. Since the proposed second-order polynomial model showed good fit with the experimental data (R2 = 0.9822), the obtained mathematical model could be used for monitoring the hydrolysis of PuOC PI by pepsin, under studied experimental conditions, varying the time and initial E/S. To achieve the highest value of DH (39.13 %), the obtained optimum conditions for time and initial E/S were 30 min and 1.024 mA/mg proteins.

Keywords: Enzymatic hydrolysis, Pepsin, Pumpkin (CucurbitaPepo L.) oil cake protein isolate, Response surface methodology.

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Authors: P. Hashim, M. S. Mohd Ridzwan, J. Bakar

Abstract:

Collagen was isolated from chicken feet by using papain and pepsin enzymes in acetic acid solution at 4°C for 24h with a yield of 18.16% and 22.94% by dry weight, respectively. Chemical composition and characteristics of chicken feet collagen such as amino acid composition, SDS-PAGE patterns, FTIR spectra and thermal properties were evaluated. The chicken feet collagen is rich in the amino acids glycine, glutamic acid, proline and hydroxyproline. Electrophoresis pattern demonstrated two distinct α-chains (α1 and α2) and β chain, indicating that type I collagen is a major component of chicken feet collagen. The thermal stability of collagen isolated by papain and pepsin revealed stable denaturation temperatures of 48.40 and 53.35°C, respectively. The FTIR spectra of both collagens were similar with amide regions in A, B, I, II and III. The study demonstrated that chicken feet collagen using papain isolation method is possible as commercial alternative ingredient. 

Keywords: Chicken feet, collagen, papain, pepsin.

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Authors: Ž. Vaštag, Lj. Popović, S. Popović

Abstract:

After cold pressing of pumpkin oil, the defatted oil cake (PUOC) was utilised as raw material for processing of bio-functional hydrolysates. In this study, the in vitro bioactivity of an alcalase (AH) and a pepsin hydrolysate (PH) prepared from the major pumpkin 12S globulin (cucurbitin) are compared. The hydrolysates were produced at optimum reaction conditions (temperature, pH) for the enzymes, during 60min. The bioactivity testing included antioxidant and angiotensin I converting enzyme inhibitory activity assays. The hydrolysates showed high potential as natural antioxidants and possibly antihypertensive agents in functional food or nutraceuticals. Additionally, preliminary studies have shown that both hydrolysates could exhibit modest α-amylase inhibitory activity, which indicates on their hypoglycemic potential.

Keywords: Cucurbitin, alcalase, pepsin, protein hydrolysates, in vitro bioactivity.

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Authors: Parisa Farzaneh, Azade Harati

Abstract:

Mushrooms or macro-fungi, as an important superfood, contain many bioactive compounds, particularly bio-peptides. In this research, mushroom proteins were extracted by buffer or buffer plus salt (0.15 M), along with ultrasound bath to extract the intercellular protein. As a result, the highest amount of proteins in mushrooms were categorized into albumin. Proteins were also hydrolyzed and changed into peptides through endogenous and exogenous proteases, including gastrointestinal enzymes. The potency of endogenous proteases was also higher in Agaricus bisporus than Terfezia claveryi, as their activity ended at 75 for 15 min. The blanching process, endogenous enzymes, the mixture of gastrointestinal enzymes (pepsin-trypsin-α-chymotrypsin or trypsin- α-chymotrypsin) produced the different antioxidant and antibacterial hydrolysates. The peptide fractions produced with different cut-off ultrafilters also had various levels of radical scavenging, lipid peroxidation inhibition, and antibacterial activities. The bio-peptides with the superior bio-activities (less than 3 kD of T. claveryi) were resistance to various environmental conditions (pH and temperatures). Therefore, they are good options to be added in nutraceutical and pharmaceutical preparations or functional foods, even during processing. 

Keywords: Bio-peptides, mushrooms, gastrointestinal enzymes, bioactivities.

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Authors: S. Yodyingyong, C. Chaichana, C. Nuchsuk, S. Roytrakul, N. P. T-Thienprasert, S. Ratanapo

Abstract:

Protein hydrolysates prepared from a number of medicinal plants are promising sources of various bioactive peptides. In this work, proteins from dried whole plant of Euphorbia hirta Linn. were extracted and digested with pepsin for 12h. The hydrolysates of lesser than 3 KDa were fractionated by a cut-off membrane. The peptide hydrolysate was then purified by an anion-exchange chromatography on DEAE-Sephacel™ column and reverse-phase chromatography on Sep-pak C₁₈ column, respectively. The cytotoxic effect of each peptide fraction against a gastric carcinoma cell line (KATO-III, ATCC No. HTB103) was investigated using colorimetric MTT viability assay. A human liver cell line (Chang Liver, CLS No. 300139) was used as a control normal cell line. Two purified peptide peaks, peak l and peak ll at 100µg peptides mL^-1 affected cell viability of the gastric cancer cell lines to 63.85±4.94 and 66.92±6.46%, respectively. Our result showed for the first time that the peptide fractions derived from protein hydrolysate of Euphorbia hirta Linn. have anti-gastric cancer activity, which offers a potential novel and natural anti-gastric cancer remedy.

Keywords: Cytotoxic, peptides, Euphorbia hirta Linn., gastric carcinoma.

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