Reduction of hexavalent chromium by digested oat bran proteins

Tsopmo, Apollinaire; Gao, Qing Feng; Baakdah, Morooj M.

doi:10.1016/j.foodchem.2013.12.049

Cited by 12 publications

(12 citation statements)

References 26 publications

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“…As the amount of amino acids increases due to concentration of FPH, the rate of chromium reduction has also substantially increased. Tsopmo et al ( 2014 ) have also previously described the reduction of hexavalent chromium by digested oat bran protein and role of cysteine in reduction process. Since, reduction of hexavalent chromium has also been reported by S. maltophilia (Alam and Ahmad 2012 ).…”

Section: Resultsmentioning

confidence: 99%

Feather degradation potential of Stenotrophomonas maltophilia KB13 and feather protein hydrolysate (FPH) mediated reduction of hexavalent chromium

2016

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An efficient keratinolytic strain of Stenorophomonas maltophilia KB13 was isolated from feather disposal site of Bilaspur, Chhattisgarh, India. The strain could metabolize 10 g/l chicken feathers as sole source of carbon and nitrogen. Soluble protein, amino acid, and cysteine content were found to be maximum (690.6 ± 8.7, 688.9 ± 9.12 and 21 ± 0.36 µg/ml, respectively) at late logarithmic phase of growth. Protease and keratinase activity reached its maximum level (103.26 ± 7.09 and 178.5 ± 9.10 U/ml) at the 4th day of incubation. The feather protein hydrolysate (FPH) obtained after degradation of chicken feathers was utilized to reduce hexavalent chromium. About 78.4 ± 2.4 and 63.6 ± 2.2 % reduction of 50 and 100 mg/l Cr(VI), respectively, was observed after 60 min of incubation with FPH. Further, there was no effect of autoclaved FPH on Cr(VI) reduction indicating that any bacterial enzyme was not involved in reduction process. Cr(VI) reduction was significantly inhibited by 10 mm Hg2+ ions indicating the role of sulfur-containing amino acids in reduction process. FTIR analysis confirmed that chromium reduction occurred due to oxidation of amino acids cysteine and cystine. This study shows that FPH arising after feather degradation can be employed as a potential candidate for the reduction of hexavalant chromium.

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Section: Resultsmentioning

confidence: 99%

Feather degradation potential of Stenotrophomonas maltophilia KB13 and feather protein hydrolysate (FPH) mediated reduction of hexavalent chromium

2016

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“…Carbohydrase such as cellulase, amyloglucosidase and viscozyme are used to enhance the efficiency of protein extraction from cereal brans (Jodayree, Smith, & Tsopmo, 2012). Some of the proteases commonly used for in vitro digestion of food proteins are alcalase, papain, nutrase, flavourzyme and protamex (Ou et al, 2010;Tsopmo, Gao, & Baakdah, 2014).…”

Section: Project Descriptionmentioning

confidence: 99%

“…After exposures, metal-ion transporters help in maintaining the required levels of metal ions in various compartments of the cell. The breakdown of metal-ion homeostasis can lead to the metal binding to protein sites that they are not supposed to or the metal-ion replace other metals from their natural binding sites and if the situation remains uncontrolled, there will be formation of deleterious free radicals, modifications of DNA bases, enhanced lipid peroxidation and altered calcium and thiol homeostasis (Klaudia Jomova & Valko, 2011;Tsopmo et al, 2014). Reactive oxygen species (ROS), products of metal-catalyzed reactions are classified as redox-active metals.…”

Section: Metal Toxicity and Oxidative Stressmentioning

confidence: 99%

Effects of Hydrolyzed Oat Bran Proteins on Free Radicals, Toxic Metals and Lipid Oxidation

Shittu¹

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Transition metals play an important role in wide variety of biological processes in living system. Exposure to toxic metals, specifically arsenic (As) and chromium (Cr), has been associated with inflammation, cellular damage, and cardiovascular diseases as a result of As/Cr-mediated oxidative stress. In recent years, food proteins have been of major interest because in addition to being sources of essential amino acids they can also provide bioactive peptides. Several studies have found that these food peptides exhibit antioxidant, anti-inflammatory and anti-hypertensive properties. Oat is the sixth consumed type of cereal and its use in human nutrition has been increasing in recent years because of the discovery of functional and biological activity of some of its constituents. In the present study, medium oat bran was pre-treated with cellulase and viscozyme to degrade the carbohydrase, followed by the hydrolysis of the isolated proteins with proteases; alcalase (AL), papain (PA), flavourzyme (FL), and protamex (PRO). We investigated the characteristics of the oat bran protein isolates (OBPI) and the oat bran protein hydrolysates (OBPH), their ability to reduce the toxicity of arsenic and chromium as well as their radical scavenging properties. OBPI samples include cellulase (CELL) and viscozyme (VISC) pre-treated protein isolates respectively. OBPH samples were named based on the carbohyrase and protease used in hydrolysis; CAL, CPA, CFL, CPRO, VAL, VPA, VFL, VPRO. Results showed that OBPIs possessed higher protein contents (80%) and higher molecular weight (MW > 20kDa) than the OBPH with an average of 45% protein content and MW < 15kDa. OBPIs exhibited higher levels of aromatic amino acid residue (p < 0.05) compared to OBPHs. Meanwhile, aromatic amino acid contents varied among OBPHs due to difference in specificities of proteases. In the peroxyl radical scavenging (ORAC) assay, OBPHs from viscozyme treated brans performed better than those from cellulase. VFL and VAL had the highest ORAC value ranging from 565 ± 80 -640 ± 57 µM TE/g respectively compared to 406.3 ± 43 -506.7 ± 65 µM TE/g for hydrolysates from cellulase treated bran. VISC and iv CELL isolates had lower ORAC values ranging from 107.9 ± 13.5 -305.8 ± 28.3 µM TE/g respectively compared to OBPHs. Hydrolysis increased peroxyl radical scavenging activities (ORAC) but lowered hydroxyl radical (HO•) potentials while only minor changes were observed in the superoxide anion radical scavenging power. OBPIs and OBPHs had no effect on lipid peroxides in non-stored samples (NS) and -20 0 C storage, however storage at 4 0 C, cellulase treated OBPHs had lower concentration of lipid peroxide compared to viscozyme.Data on the effect of OBPI and OBPH on arsenic showed that at -20 0 C, treated samples had higher concentration of As (III) compared to NS, but mostly lower concentration compared to 4 0 C.Concentration of As (V) in treated samples is mostly lower compared to NS and 4 0 C. Non-stored samples (NS) treated with CELL and CFL had the highest (p < 0.05) c...

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“…So far literature has reported that oat protein hydrolysates treated with thermolysin and alcalase & trypsin, have demonstrated an ACEinhibitory effect and antioxidant activities respectively (Cheung, Nakayama, Hsu, Samaranayaka, & Li-Chan, 2009) (Vanvi & Tsopmo, 2016). Additionally, oat bran protein hydrolysates, treated with proteases such as protamex, and pepsin have shown biological activities such as metal chelating activities and radical scavenging properties (Baakdah & Tsopmo, 2016) (Tsopmo, Gao, & Baakdah, 2014a). Oat bran protein hydrolysates pre-treated with cell wall degrading enzymes have resulted in a protein content increase and antioxidant properties (Jodayree, Smith, & Tsopmo, 2012).…”

Section: Oat Protein Hydrolysatesmentioning

confidence: 99%

“…One group of molecules is dietary fibre and graduating other compounds such as protein hydrolysate. Radical scavenging, inhibition of linoleic acid oxidation and iron chelating properties of hydrolyzed oat proteins have studies(Vanvi & Tsopmo, 2016)(Tsopmo, Gao, & Baakdah, 2014b); however their potential in other model systems is needed. Furthermore, there is no report in the literature regarding the ability of oat bran protein hydrolysates to chelate bile acids.…”

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confidence: 99%

Inhibitory Effects of Hydrolyzed Oat Bran Proteins on Human LDL Oxidation and Their Bile Acid Binding Capacity

Espinosa¹,

Yunuen²

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Free radicals attack to biological molecules can initiate their oxidation and contribute to the development of several chronic diseases. Oxidation of low density lipoprotein, as well as a higher concentration of cholesterol, have been implicated in the development of atherosclerotic lesions and increased risks of cardiovascular diseases. Strategies to decrease the risks then include scavenging of free radicals and the reduction of cholesterol (e.g. binding of bile acids). In this regard, the aim of this project was; 1) to produce and characterize various hydrolyzed proteins from oat brans; 2) determine their antioxidant, metal binding and bile chelating capacities as well as their ability to inhibit low density lipoprotein oxidation (LDL). Medium oat bran samples were treated with two cell wall polysaccharide degrading enzymes (cellulase and viscozyme) to generate two protein isolates named CPI and VPI respectively. Ten hydrolysates were subsequently prepared by treating CPI or VPI with five proteases protamex, alcalase, flavourzyme, pepsin and pepsin+pancreatin. The two highest degrees of hydrolysis (26.4 ± 0.5 and 22.0 ± 0.1%) were obtained under simulated gastrointestinal digestion with pepsin and pancreatin. Intrinsic absorbance showed that CPI-alcalase and CPI-pepsin/pancreatin had a higher content of aromatic amino acids. In the antioxidant oxidant assays, VPI-pepsin better scavenged ROO • radicals (496.77±5.83 μM Trolox Equivalents (TE)/g) while VPI-flavourzyme and VPI-pepsin had better quenching for HO • (27.95 ±1.580 and and O2 •-(45.31±6.6%) radicals, respectively. In the metal

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Reduction of hexavalent chromium by digested oat bran proteins

Cited by 12 publications

References 26 publications

Feather degradation potential of Stenotrophomonas maltophilia KB13 and feather protein hydrolysate (FPH) mediated reduction of hexavalent chromium

Feather degradation potential of Stenotrophomonas maltophilia KB13 and feather protein hydrolysate (FPH) mediated reduction of hexavalent chromium

Effects of Hydrolyzed Oat Bran Proteins on Free Radicals, Toxic Metals and Lipid Oxidation

Inhibitory Effects of Hydrolyzed Oat Bran Proteins on Human LDL Oxidation and Their Bile Acid Binding Capacity

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