Cross-Linking Of Soy Protein Isolate Using Microbial Transglutaminase Followed By Ribose-Induced Maillard Reaction

Tesis ini menjelaskan tentang penggunaan pengolahan hubung-silang gabungan untuk mengubahsuaikan sifat-sifat berfungsi isolat protein soya (SPI). This thesis describes the use of combined cross-linking treatment techniques to modify functional properties of soy protein isolate (SPI)

Development of electropulsation for the extraction of protein from underutilized agro-source pinto bean, as an alternative solution to the issue of protein malnutrition.

Pinto bean showed its potential as an alternative source of protein. High amount of protein was successfully extracted from pinto bean. An optimum condition for the extraction was obtained. Therefore, this protein source could be used to overcome protein-malnutrition issue

Comprehensive review on some food-derived bioactive peptides with anti-hypertension therapeutic potential for angiotensin-converting enzyme (ACE) inhibition

Angiotensin-converting enzyme (ACE) inhibitory peptides have lately attracted interest since functional foods that help maintain homeostatic regulations have been developed. Rarely discussed are the intrinsic ACE-peptide interactions and their positioning, both of which help illustrate the ACE inhibitory functionalities in food-derived peptides. In this study, 173 ACE inhibitory peptides were collated using the UWM-BIOPEP database. The sequences were grouped into short, medium, and long peptides. The hydrophobicity/hydrophilicity property of peptides was analyzed using Peptide2 and the peptide binding site on ACE was predicted using PepSite2. Peptide residues interacting with ACE were denoted as reactive amino acids. Molecular docking analysis was conducted to simulate ACE-peptide binding and delineate the roles of reactive amino acids at the ultimate, penultimate, and antepenultimate positions of N—(N1, N2, and N3) and C—(C1, C2, and C3) terminals. Peptide2 analysis suggested that hydrophobic property was prominent in the peptides. The C-terminals were prominent in ACE binding for long-chained peptides through interaction with ACE hotspots. Moreover, branched-chain amino acids (BCAA) such as leucine and isoleucine were crucial at the N-terminals. The bulky side chain of BCAA forms a hydrophobic shield that protects the Zn-peptide chelate complex from water attacks. The hydrophobic fence in turn stabilizes the disrupted tetrahedral Zn-coordinate complex of ACE. This finding provided a thorough exploration of how peptide structures are related and what function they play in ACE inhibitory action. The database analysis, therefore, gave a clearer insight and comprehensive understanding into the protein-peptide interactions and provided a mechanistic explanation

Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization

The sea cucumber (Stichopus vastus) is an underutilized species, as most of its parts, including the integument (high collagen content) are thrown away during processing. The aim of this study was to investigate the effects of different hydrolysis conditions (substrate to enzyme ratio (S/E), reaction temperature, and hydrolysis time) on the angiotensin I converting enzyme (ACE) inhibitory and radical scavenging (RSc) activities of the hydrolysates produced from trypsin hydrolysis of S. vastus collagen. Optimal conditions predicted by Box-Behnken Design modelling for producing ACE inhibitory and RSc hydrolysates were found to be S/E ratio (15), reaction temperature (55°C), and hydrolysis time (1 h). Under optimal conditions, ACE inhibitory and RSc activities were estimated to be as high as 67.8% and 77.9%, respectively. Besides, some novel bioactive peptides were identified through mass spectrometry analysis. These results indicate that S. vastus hydrolysates might be used as a functional ingredient in food and nutraceutical products

ACE Inhibitory and Antioxidant Activities of Collagen Hydrolysates from the Ribbon Jellyfish (Chrysaora sp.)

Za izdvajanje bioaktivnih peptida iz kompas meduze (Chrysaora sp.) izoliran je kolagen, te je hidroliziran s pomoću tri proteaze: tripsina, alkalaze i komercijalnog prozivoda Protamex. Izmjeren je i uspoređen učinak različito inhibiranih peptida na inhibiciju angiotenzin konvertirajućeg enzima (ACE), te je pomoću metoda FRAP i DPPH ispitana njihova antioksidativna aktivnost. Osim toga, ispitan je utjecaj trajanja hidrolize na bioaktivnost peptida, tj. na inhibiciju ACE i antioksidativnu aktivnost. Najveća je ukupna antioksidacijska aktivnost (FRAP) izmjerena u hidrolizatima dobivenim pomoću komercijalne proteaze Protamex (25-27 mM) nakon 7 sati hidrolize, te nakon 9 sati hidrolize pomoću tripsina (24-26 mM). Nasuprot tome, hidrolizati dobiveni pomoću tripsina imali su najveću sposobnost uklanjanja DPPH radikala (94 % nakon 1 sata i 92 % nakon 3 sata). Hidrolizati dobiveni pomoću tripsina imali su najbolju sposobnost inhibicije ACE (89 % nakon 3 sata). Pomoću dvojne masene spektrometrije određene su sekvencije peptida koje su imale najveću aktivnost, a rezultati pokazuju da su hidrolizati imali veći udjel hidrofobnih aminokiselina i jedinstvenih sekvencija aminokiselina, što vjerojatno pridonosi njihovoj biološkoj aktivnosti.Collagen isolated from the ribbon jellyfish (Chrysaora sp.) was hydrolysed using three different proteases (i.e. trypsin, alcalase and Protamex) to obtain bioactive peptides. Angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant activities (i.e. ferric reducing antioxidant power (FRAP) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity) of the peptides were measured and compared, and the effect of the duration of hydrolysis on the bioactivity (ACE inhibitory and antioxidant activities) of peptides was also evaluated. FRAP activity was the highest in Protamex-induced (25–27mM) and trypsin-induced hydrolysates (24–26 mM) at 7 and 9 h, respectively. Conversely, hydrolysates produced by trypsin for 1 and 3 h showed the highest DPPH radical scavenging activities (94 and 92 %, respectively). Trypsin-induced hydrolysates (at 3 h) also showed the highest ACE inhibitory activity (89 %). The peptide sequences with the highest activities were identified using tandem mass spectrometry, and the results show that the hydrolysates had a high content of hydrophobic amino acids as well as unique amino acid sequences, which likely contribute to their biological activities

Microstructural and microchemical characterization of valorized cola nitida pod wastes

The inherent environmental effects of the accumulated kola nut pod waste products have become a subject of discussion among many researchers. The need then arises for their alternative use as nutraceutical bioproducts. The physical and chemical analytical techniques are often required for the standardization of these bioproducts in order to determine and maintain their quality characteristics. The dataset presented in this study provided information on the chemical profile, physisorption and thermo-analytical screening of Cola nut pod extracts. Six sets of physicochemical methods were employed to characterize the phenolic extracts. The result obtained clearly revealed the presence of two-hundred and fifty-five phenolic bioactive. Also presented was the thermal stability, morphological and microstructural surface area configuration of the Cola nitida pod extracts. The information obtained from this study could be used in determining the quality of food wastes bioproducts in nutria-pharmaceutical applications

Physicochemical and biochemical properties of pepsin-solubilized collagen isolated from the integument of Sea Cucumber (Stichopus vastus)

The integument (high collagen content) of sea cucumber Stichopus vastus is generally wasted after harvesting, whereas only its stomach and intestines are eaten in few Asian countries. Amino acid composition, thermal transition temperature (Tm), zeta potential, solubility, moisture absorption and retention capacities, proximate composition and morphology of pepsin-solubilized collagen (PSC) isolated from the integument of S. vastus were studied. Amino acid composition revealed that glycine was dominant in the isolated collagen. PSC was found to have an isoelectric pH of 4.67, good moisture absorption and retention capacity at higher humidity, a sharp effect of pH and NaCl concentration on solubility, and an inverse relationship between temperature and viscosity. PSC also showed the maximum Tm to be 37.3C, very high protein content and ultrastructural characteristics. Hence, the PSC has the potential to be used as a functional ingredient in food, cosmetics and nutraceutical products

Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides

Active fragments (bioactive peptides) from the chicken egg white proteins were expected to exert tyrosinase inhibitory activities in which skin hyperpigmentation could be prevented. Egg white was hydrolyzed by trypsin, chymotrypsin and the combination of both enzymes. The enzyme treatments achieved >50% degree of hydrolysis (DH) at substrate-to-enzyme (S/E) ratio of 10–30 (w/w) and hydrolysis time of 2–5 h. A crossed D-optimal experimental design was then used to determine the optimal enzyme composition, S/E ratio and hydrolysis time in order to yield hydrolysates with strong monophenolase and diphenolase inhibitory activities. The optimized conditions 55% trypsin, 45% chymotrypsin, S/E 10:1 w/w and 2 h achieved 45.9% monophenolase activity inhibition whereas 100% trypsin, S/E 22.13:1 w/w and 3.18 h achieved 48.1% diphenolase activity inhibition. LC/MS and MS/MS analyses identified the peptide sequences and the subsequent screening had identified 7 peptides (ILELPFASGDLLML, GYSLGNWVCAAK, YFGYTGALRCLV, HIATNAVLFFGR, FMMFESQNKDLLFK, SGALHCLK and YFGYTGALR) as the potential inhibitor peptides. These peptides were able to bind to H85, H94, H259, H263, and H296 (hotspots for active residues) as well as F92, M280 and F292 (stabilizing residues) of tyrosinase based on structure-activity relationship analysis. These findings demonstrated the potential of egg white-derived bioactive peptides as skin health therapy