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1.
J Agric Food Chem ; 60(38): 9770-8, 2012 Sep 26.
Article in English | MEDLINE | ID: mdl-22950859

ABSTRACT

In this study with aflatoxin-contaminated peanuts, the effectiveness of electrolyzed oxidizing water (EOW) in the decontamination of aflatoxin B(1) was investigated. The aflatoxin B(1) content was markedly reduced upon treatment with EOW, particularly with neutral electrolyzed oxidizing water (NEW). The conversion product of EOW treatment was isolated and identified as 8-chloro-9-hydroxy aflatoxin B(1) (compound 1), which is an amphiphilic molecule, in contrast to fat-soluble aflatoxin B(1). A mutagenic response study revealed that the number of revertants per plate after treatment of bacterial strains TA-97, TA-98, TA-100, and TA-102 with NEW was within the standard value range. The HepG2 cell viability assay yielded an IC(50) value of compound 1 approximately 150 mM. This study indicates that EOW had the ability to decontaminate aflatoxin B(1), and the conversion product, compound 1, did not exhibit mutagenic activity or cytotoxic effects.


Subject(s)
Aflatoxin B1/chemistry , Arachis/chemistry , Decontamination , Electrolysis/methods , Food Contamination , Food Safety/methods , Aflatoxin B1/analysis , Aflatoxins/chemistry , Aflatoxins/toxicity , Arachis/microbiology , Aspergillus flavus/pathogenicity , Chromatography, High Pressure Liquid , Hep G2 Cells , Humans , Molecular Structure , Mutagenicity Tests/methods , Salmonella typhimurium/drug effects , Salmonella typhimurium/genetics
2.
Food Chem ; 134(3): 1263-6, 2012 Oct 01.
Article in English | MEDLINE | ID: mdl-25005942

ABSTRACT

Acetylcholinesterase (AChE) inhibitory activities of commercial sufu and self-produced sufu were investigated in this experiment. The anti-AChE activities of commercial sufu samples of 15 brands, sourcing from various parts of China, and self-produced sufu, fermented with Actinomucor elegans 3.118, were measured. The results indicated that ethanol extract of Chinese sufu exhibited significant inhibitory activity against AChE in vitro. The inhibitory activity of No. 5 sufu was the strongest (IC50, 0.191 mg/ml), while the pre-fermented sufu showed the highest inhibitory activity during sufu manufacturing. In addition, soybean extracts and potato extracts were used to culture A. elegans 3.118 in order to estimate which culture was preferable for the production of these AChE inhibitors. The soybean extracts, after fermentation by A. elegans 3.118, showed higher anti-AChE activity than did the potato extracts. The IC50 of the soybean extracts was 1.29 µg/ml.


Subject(s)
Acetylcholinesterase/chemistry , Cholinesterase Inhibitors/pharmacology , Ethanol/chemistry , Fermentation , Plant Extracts/pharmacology , Soy Foods/microbiology , Acetylcholinesterase/metabolism , China , Cholinesterase Inhibitors/chemistry , Cholinesterase Inhibitors/isolation & purification
3.
J Food Prot ; 73(3): 483-7, 2010 Mar.
Article in English | MEDLINE | ID: mdl-20202333

ABSTRACT

Electrolyzed oxidizing water (EOW) has been regarded as a potential environmentally friendly broad spectrum microbial decontaminant. EOW with a pH of 3.0 and oxidation reduction potential of 1,079.0 mV were generated by the electrolysis of a dilute NaCl solution (20 mM) in an electrochemical cell. The effects of EOW, 1% NaClO solution, and alkaline electrolyzed water on controlling microbial growth, germination ratio, and enrichment of gamma-aminobutyric acid in germinated brown rice (GBR) were evaluated in this study. Results show that EOW was the most effective at inhibiting microbial growth during germination. Rinsing the rice grains with EOW at 12-h intervals resulted in aerobic plate count reductions of 4.82 log CFU/g, while soaking resulted in bacterial count reductions of 5.38 log CFU/g after 72 h of germination. Moreover, EOW significantly enriched gamma-aminobutyric acid content in GBR (P < 0.05); content was increased 1.6 times in grain rinsed with EOW and 1.8 times in grain soaked in EOW. The findings indicate that EOW is a feasible disinfectant for industrial GBR production.


Subject(s)
Food Contamination/prevention & control , Food Handling/methods , Oryza/microbiology , Water/pharmacology , gamma-Aminobutyric Acid/analysis , Colony Count, Microbial , Consumer Product Safety , Electrolysis , Food Microbiology , Germination , Humans , Hydrogen-Ion Concentration , Oxidation-Reduction , Treatment Outcome , Water/chemistry , Water Microbiology
4.
J Agric Food Chem ; 58(7): 4097-103, 2010 Apr 14.
Article in English | MEDLINE | ID: mdl-20196601

ABSTRACT

This study was to purify an alpha-glucosidase inhibitor from okara (soy pulp) fermented by Bacillus subtilis B2 and to identify its chemical structure. Membrane dialysis, active charcoal, CM-Sepharose chromatography, and preparative thin-layer chromatography (TLC) were used in the purification, while positive mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectrometry were used in the identification. The MS and NMR data showed that the purified alpha-glucosidase inhibitor was 1-deoxynojirimycin (DNJ) with a molecular weight of 163 Da. This is the first time that DNJ was isolated from foods fermented with Bacillus species. Okara fermentation with B. subtilis B2 might be used to produce a food-derived DNJ product as a functional food for diabetic patients.


Subject(s)
1-Deoxynojirimycin/isolation & purification , Bacillus subtilis/metabolism , Fermentation , Food Microbiology , 1-Deoxynojirimycin/chemistry , 1-Deoxynojirimycin/metabolism , Bacillus subtilis/genetics , Bacillus subtilis/isolation & purification , Enzyme Inhibitors/chemistry , Enzyme Inhibitors/isolation & purification , Enzyme Inhibitors/metabolism , Glycoside Hydrolase Inhibitors
5.
Int J Food Microbiol ; 137(1): 67-75, 2010 Jan 31.
Article in English | MEDLINE | ID: mdl-19926156

ABSTRACT

Neutralized electrolyzed oxidizing water (NEW) and acidic electrolyzed oxidizing water (AcEW) are electrolyzed oxidizing waters (EOW) that have significantly different fungicidal efficiencies against Aspergillus flavus (A. flavus) (The actuation durations of no survival population to NEW and AcEW were 90s and 120s, respectively.), even when used at the same available chlorine concentration (30ppm). It has been verified by our previous research. This study hypothesized that this difference did not originate from the structure of water but based on the OH radical (OH). It was proved by the UV spectroscopy, (17)O-NMR spectroscopy and electron spin resonance analysis. NEW contains more OH compared with AcEW in the same available chlorine concentration level. The OH that exists in NEW and AcEW was found to have an important fungicidal factor that destroys the cellular structures of the A. flavus conidia. It also damages the cellular normal function of A. flavus conidia that brought about K+ and Mg2+ leakages. The levels of OH that exist in NEW and AcEW could be the important reason that leads to significant fungicidal efficiencies against A. flavus.


Subject(s)
Aspergillus flavus/drug effects , Food Microbiology , Hydrogen Peroxide/pharmacology , Aspergillus flavus/metabolism , Aspergillus flavus/pathogenicity , Aspergillus flavus/ultrastructure , Cell Membrane Permeability/drug effects , Chemical Phenomena , Disinfectants/pharmacology , Drug Combinations , Electron Spin Resonance Spectroscopy , Food Contamination/prevention & control , Free Radical Scavengers/pharmacology , Humans , Magnesium/metabolism , Magnetic Resonance Spectroscopy , Microscopy, Electron, Scanning , Mycotoxins/biosynthesis , Mycotoxins/toxicity , Oils , Phenols , Potassium/metabolism , Spectrophotometry, Ultraviolet , Superoxides/pharmacology
6.
Food Chem ; 109(4): 737-42, 2008 Aug 15.
Article in English | MEDLINE | ID: mdl-26049986

ABSTRACT

This study examined production of α-glucosidase inhibitors by Bacillus subtilis B2 in Luria-Bertani (LB) fermentation with okara, soy powder, starch or pectin as additional source of carbon and nitrogen. All the fermentation broths of B. subtilis B2 exhibited gradual increase in α-glucosidase inhibitory activity during the fermentation process with or without supplemented source of carbon or nitrogen. Addition of okara into the LB medium greatly enhanced the strength (nearly twice as much of that without okara supplement) of α-glucosidase inhibitory activity of fermentation broth. The α-glucosidase inhibitory activity of B. subtilis B2 fermentation broth was positively correlated (p<0.05) with the bacterial populations grown in LB medium containing okara. Glucose and sucrose were not detected in LB medium during the entire fermentation process and were both reduced drastically in media containing okara, soy powder, starch or pectin after 6days of fermentation. The fermented LB medium containing okara by B. subtilis B2 possessed very strong α-glucosidase inhibitory activity and contained little glucose and sucrose, suggesting that fermentation of B. subtilis B2 in LB added with okara might be considered as a strategy for preparing functional foods for diabetic patients.

7.
Appl Microbiol Biotechnol ; 73(4): 763-70, 2006 Dec.
Article in English | MEDLINE | ID: mdl-16977469

ABSTRACT

Hydrolysate of extruded corn gluten with higher solubility and antioxidative property was prepared. Extrusion and starch removal of corn gluten were applied as pretreatment before enzymatic hydrolysis by Alcalase. The amylase hydrolysis of starch at 70 degrees C for 3 h resulted in the removal of the starch from the extruded corn gluten. The best hydrolysis results can be obtained by conducting the hydrolysis at 60 degrees C with water addition 20 g/g protein, enzyme addition 0.048 Ansen units/g protein, pH 8.5, and 120 min. Degree of hydrolysis of extruded and nonextruded corn gluten reached 39.54 and 31.16%, respectively, under the optimal condition. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the optimal hydrolysate revealed that proteolysis of extruded corn gluten was more extensive than proteolysis of its counterpart which was not subjected to extrusion. The molecular weight of the peptides in the optimal hydrolysate was mainly over 3,710-660 Da as determined by gel filtration chromatography. The hydrolysates displayed good solubility and antioxidative activity. The separation profile of the hydrolysate on an ion exchange chromatography of Q-Sepharose Fast Flow showed that many kinds of peptides had antioxidative effect. A new peptide with antioxidative activity was purified, and its amino acid sequence was Phe-Pro-Leu-Glu-Met-Met-Pro-Phe, which was identified by Q-TOF2 mass spectrometry.


Subject(s)
Antioxidants/metabolism , Antioxidants/pharmacology , Glutens/metabolism , Protein Hydrolysates/metabolism , Protein Hydrolysates/pharmacology , Subtilisins/metabolism , Amino Acid Sequence , Biotechnology/methods , Chromatography, Gel , Chromatography, Ion Exchange , Electrophoresis, Polyacrylamide Gel , Glutens/isolation & purification , Hydrogen-Ion Concentration , Hydrolysis , Mass Spectrometry , Molecular Weight , Peptides/chemistry , Peptides/isolation & purification , Peptides/pharmacology , Protein Hydrolysates/chemistry , Protein Hydrolysates/isolation & purification , Solubility , Starch/isolation & purification , Temperature , Time Factors , Zea mays
8.
Biotechnol Lett ; 27(6): 429-33, 2005 Mar.
Article in English | MEDLINE | ID: mdl-15834809

ABSTRACT

Besides affecting the xylanases production, different nitrogen sources present in the media also caused changes in the xylanosomal subunit composition of Streptomyces olivaceoviridis E-86. Four xylanosome fractions, purified from the culture supernatant of S. olivaceoviridis E-86 grown on different nitrogen sources, exhibited high specificity towards different xylans and were composed of different subunits. Thus, S. olivaceoviridis E-86 regulates the expression of xylanase activity and varies the xylanosome composition according to the nitrogen sources possibly through the action of the secreted proteases.


Subject(s)
Nitrogen/metabolism , Streptomyces/metabolism , Xylans/metabolism , Culture Media , Multienzyme Complexes , Protein Subunits , Substrate Specificity , Xylans/chemistry , Xylosidases/chemistry , Xylosidases/metabolism
9.
Biosci Biotechnol Biochem ; 69(2): 267-72, 2005 Feb.
Article in English | MEDLINE | ID: mdl-15725649

ABSTRACT

Sufu is a popular fermented tofu product in China. The low quality of sufu produced in the hot summer is a big problem in sufu manufacture, so we prepared sufu at two different temperatures, 26 degrees C as normal and 32 degrees C as high temperature, and the effects of temperature on isoflavones and beta-glucosidase activity were investigated. Fermentation temperature did not cause significant differences in the recovery of isoflavones, but resulted in a different redistribution of isoflavone isomers in sufu. Sufu fermented at 26 degrees C was richer in isoflavone aglycones than at 32 degrees C; the enrichment of isoflavone aglycones might have the advantage of enhancing the physiological function. No 6''-O-malonyl-glucosides were detected in sufu fermented at 26 degrees C, whereas some 6''-O-malonyl-glucosides were found at 32 degrees C. A fermentation temperature of 26 degrees C benefited the beta-glucosidase production by fungi, which contributed to valid conversion from beta-glucosides to aglycones. It was also found that beta-glucosidase converted beta-glucosides more effectively than 6''-O-malonyl-glucosides and 6''-O-acetyl-glucosides into aglycones.


Subject(s)
Fermentation , Isoflavones/analysis , Soy Foods/analysis , Temperature , beta-Glucosidase/metabolism , Time Factors , beta-Glucosidase/analysis
10.
Biotechnol Lett ; 26(5): 431-6, 2004 Mar.
Article in English | MEDLINE | ID: mdl-15104143

ABSTRACT

The production of a novel, very large xylanolytic complex (xylanosome) by Streptomyces olivaceoviridis E-86 is reported. The molecular weight was approx. 1200 kDa as determined by native gradient gel electrophoresis. Corncob xylan was the best inducer of xylanosome formation. The xylanosome was produced when the organism was grown for 5 d between pH 4.5-6 and at 27.5 to 35 degrees C.


Subject(s)
Cell Culture Techniques/methods , Endo-1,4-beta Xylanases/biosynthesis , Multienzyme Complexes/biosynthesis , Streptomyces/enzymology , Xylans/metabolism , Endo-1,4-beta Xylanases/chemistry , Enzyme Stability , Hydrogen-Ion Concentration , Molecular Weight , Multienzyme Complexes/chemistry , Species Specificity , Streptomyces/chemistry , Streptomyces/classification , Streptomyces/growth & development , Temperature , Xylans/classification
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