Displaying all 8 publications

Abstract:
Sort:
  1. Borhan FP, Abd Gani SS, Shamsuddin R
    ScientificWorldJournal, 2014;2014:173979.
    PMID: 25548777 DOI: 10.1155/2014/173979
    Okara, soybean waste from tofu and soymilk production, was utilised as a natural antioxidant in soap formulation for stratum corneum application. D-optimal mixture design was employed to investigate the influence of the main compositions of okara soap containing different fatty acid and oils (virgin coconut oil A (24-28% w/w), olive oil B (15-20% w/w), palm oil C (6-10% w/w), castor oil D (15-20% w/w), cocoa butter E (6-10% w/w), and okara F (2-7% w/w)) by saponification process on the response hardness of the soap. The experimental data were utilized to carry out analysis of variance (ANOVA) and to develop a polynomial regression model for okara soap hardness in terms of the six design factors considered in this study. Results revealed that the best mixture was the formulation that included 26.537% A, 19.999% B, 9.998% C, 16.241% D, 7.633% E, and 7.000% F. The results proved that the difference in the level of fatty acid and oils in the formulation significantly affects the hardness of soap. Depending on the desirable level of those six variables, creation of okara based soap with desirable properties better than those of commercial ones is possible.
    Matched MeSH terms: Plant Proteins/pharmacology*
  2. Shirasuka Y, Nakajima K, Asakura T, Yamashita H, Yamamoto A, Hata S, et al.
    Biosci Biotechnol Biochem, 2004 Jun;68(6):1403-7.
    PMID: 15215616
    A unique taste-modifying activity that converts the sense of sourness to the sense of sweetness occurs in the fruit of the plant Curculigo latifolia, intrinsic to West Malaysia. The active component, known as curculin, is a protein consisting of two identical subunits. We have found a new taste-modifying protein, named neoculin, of the same origin. Both chemical analysis and cDNA cloning characterized neoculin as a heterodimeric protein consisting of an acidic, glycosylated subunit of 113 amino acid residues and a basic subunit that is the monomeric curculin itself.
    Matched MeSH terms: Plant Proteins/pharmacology
  3. Ngoh YY, Gan CY
    Food Chem, 2018 Nov 30;267:124-131.
    PMID: 29934146 DOI: 10.1016/j.foodchem.2017.04.166
    Five Pinto bean peptides with α-amylase and angiotensin converting enzyme (ACE) inhibitory activities were successfully identified using the integrated bioinformatics approach. By using PEAKS studio, 511 peptide sequences were first shortlisted based on their de novo sequence property and average local confidence (ALC) yield of ≥60%. Subsequently, only five peptides were found to have high potential (score ≥0.80) for contributing bioactivy. The important sites which were potentially bound by the peptides: (a) Trp58, Trp59, Tyr 62, Asp96, Arg195, Asp197, Glu233, His299, Asp300 and His305 for α-amylase; (b) His353, Ala354, His383, Glu384, His387, Glu411, Lys511, His513, Tyr520 and Tyr523 for ACE had corresponded to the catalytic and substrate binding sites of the two enzymes. A validation assay was then conducted and IC50 values were determined. The range of the values for α-amylase inhibitory activity was 10.03-23.33mM, whereas the values for ACE inhibitory activity were of 1.52-31.88μM.
    Matched MeSH terms: Plant Proteins/pharmacology
  4. Hew CS, Khoo BY, Gam LH
    PLoS One, 2013;8(7):e68524.
    PMID: 23874655 DOI: 10.1371/journal.pone.0068524
    Gynura procumbens (Lour.) Merr. belongs to the Asteraceae Family. The plant is a well-known traditional herb in South East Asia and it is widely used to treat inflammation, kidney discomfort, high cholesterol level, diabetic, cancer and high blood pressure. Our earlier study showed the presence of valuable plant defense proteins, such as peroxidase, thaumatin-like proteins and miraculin in the leaf of G. procumbens. However, the effects of these defense proteins on cancers have never been determined previously. In the present study, we investigated the bioactivity of gel filtration fractionated proteins of G. procumbens leaf extract. The active protein fraction, SN-F11/12, was found to inhibit the growth of a breast cancer cell line, MDA-MB-231, at an EC50 value of 3.8 µg/mL. The mRNA expressions of proliferation markers, Ki67 and PCNA, were reduced significantly in the MDA-MB-23 cells treated with SN-F11/12. The expression of invasion marker, CCL2, was also found reduced in the treated MDA-MB-231 cells. All these findings highlight the anti-cancer property of SN-F11/12, therefore, the proteins in this fraction can be a potential chemotherapeutic agent for breast cancer treatment.
    Matched MeSH terms: Plant Proteins/pharmacology*
  5. Tan YN, Ayob MK, Osman MA, Matthews KR
    Lett Appl Microbiol, 2011 Nov;53(5):509-17.
    PMID: 21848644 DOI: 10.1111/j.1472-765X.2011.03137.x
    The goal of this study was to determine inhibitory effect of palm kernel expeller (PKE) peptides of different degree of hydrolysis (DH %) against spore-forming bacteria Bacillus cereus, Bacillus circulans, Bacillus coagulans, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus stearothermophillus, Bacillus subtilis, Bacillus thuringiensis, Clostridium perfringens; and non-spore-forming bacteria Escherichia coli, Lisinibacillus sphaericus, Listeria monocytogenes, Pseudomonas aeruginosa, Salmonella Typhimurium and Staphylococcus aureus.
    Matched MeSH terms: Plant Proteins/pharmacology*
  6. Ngoh YY, Lim TS, Gan CY
    Enzyme Microb Technol, 2016 Jul;89:76-84.
    PMID: 27233130 DOI: 10.1016/j.enzmictec.2016.04.001
    The objective of this study was to screen and identify α-amylase inhibitor peptides from Pinto bean. Five Pinto bean bioactive peptides were successfully identified: PPHMLP (P1), PLPWGAGF (P3), PPHMGGP (P6), PLPLHMLP (P7) and LSSLEMGSLGALFVCM (P9). Based on ELISA results, their promising optical density values were 1.27; 3.71, 1.67, 3.20 and 1.03, respectively, which indicated the binding interaction between the peptide and α-amylase occurred. The highest inhibitory activity (66.72%) of the chemically synthesized peptide was shown in SyP9 followed by SyP1 (48.86%), SyP3 (31.17%), SyP7 (27.88%) and SyP6 (23.96%). The IC50 values were 1.97, 8.96, 14.63, 18.45 and 20.56mgml(-1), respectively. Structure activity relationship study revealed that α-amylase was inhibited due to its residues of Ala230, Asp229, Asp326, Tyr54, Met195, Leu194 and His233 were bound. On the other hand, the residues of PBBP (i.e. histidine, proline and methionine) were found to have the highest potency in the binding interaction.
    Matched MeSH terms: Plant Proteins/pharmacology*
  7. Shami AM, Philip K, Muniandy S
    BMC Complement Altern Med, 2013 Dec 16;13:360.
    PMID: 24330547 DOI: 10.1186/1472-6882-13-360
    BACKGROUND: A plant mixture containing indigenous Australian plants was examined for synergistic antimicrobial activity using selected test microorganisms. This study aims to investigate antibacterial activities, antioxidant potential and the content of phenolic compounds in aqueous, ethanolic and peptide extracts of plant mixture.

    METHODS: Well diffusion, minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) assays were used to test antibacterial activity against four pathogenic bacteria namely Staphylococcus aureus, Escherichia coli, Bacillus cereus, and Pseudomonas aeruginosa. DPPH (2, 2-diphenyl-1- picrylhydrazyl) and superoxide dismutase (SOD) assays were used to evaluate antioxidant activity. HPLC and gel filtration were used for purification of the peptides. Scanning electron microscope was applied to investigate the mode of attachment of the peptides on target microbial membranes.

    RESULTS: Aqueous extraction of the mixture showed no inhibition zones against all the test bacteria. Mean diameter of inhibition zones for ethanol extraction of this mixture attained 8.33 mm, 7.33 mm, and 6.33 mm against S. aureus at corresponding concentrations of 500, 250 and 125 mg/ml while E .coli showed inhibition zones of 9.33 mm, 8.00 mm and 6.66 mm at the same concentrations. B. cereus exhibited inhibition zones of 11.33 mm, 10.33 mm and 10.00 mm at concentrations of 500, 250 and 125 mg/ml respectively. The peptide extract demonstrated antibacterial activity against S. aureus, E. coli and B. cereus. The MIC and MBC values for ethanol extracts were determined at 125 mg/ml concentration against S. aureus and E. coli and B. cereus value was 31.5 mg/ml. MIC and MBC values showed that the peptide extract was significantly effective at low concentration of the Australian plant mixture (APM). Phenolic compounds were detected in hot aqueous and ethanolic extracts of the plant mixture. Hot aqueous, ethanol and peptides extracts also exhibited antioxidant activities.

    CONCLUSIONS: It was concluded that APM possessed good antibacterial and antioxidant activities following extraction with different solvents. The results suggest that APM provide a new source with antibacterial agents and antioxidant activity for nutraceutical or medical applications.

    Matched MeSH terms: Plant Proteins/pharmacology*
  8. Boldbaatar D, Gunasekera S, El-Seedi HR, Göransson U
    J Nat Prod, 2015 Nov 25;78(11):2545-51.
    PMID: 26509914 DOI: 10.1021/acs.jnatprod.5b00463
    The Ricinus communis biomarker peptides RCB-1 to -3 comprise homologous sequences of 19 (RCB-1) or 18 (RCB-2 and -3) amino acid residues. They all include four cysteine moieties, which form two disulfide bonds. However, neither the 3D structure nor the biological activity of any of these peptides is known. The synthesis of RCB-1, using microwave-assisted, Fmoc-based solid-phase peptide synthesis, and a method for its oxidative folding are reported. The tertiary structure of RCB-1, subsequently established using solution-state NMR, reveals a twisted loop fold with antiparallel β-sheets reinforced by the two disulfide bonds. Moreover, RCB-1 was tested for antibacterial, antifungal, and cytotoxic activity, as well as in a serum stability assay, in which it proved to be remarkably stable.
    Matched MeSH terms: Plant Proteins/pharmacology
Filters
Contact Us

Please provide feedback to Administrator (afdal@afpm.org.my)

External Links