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Oladunjoye, Adebola Olubukola,Singh, Suren,Ijabadeniyi, Oluwatosin Ademola 한국식품과학회 2016 Food Science and Biotechnology Vol.25 No.5
The biocontrol of Listeria monocytogenes on fresh-cut tomato using nisin and organic acids was investigated. Fresh-cut samples inoculated with $10^8CFU/mL$ of L. monocytogenes, treated with nisin (5,000 IU/mL), a combination of nisin and organic acids (acetic and citric acids at 3 and 5% each), with chlorine at 200 ppm as a control, and stored for six days at 4, 10, and $25^{\circ}C$ were used to evaluate certain physicochemical qualities (pH, titratable acidity, soluble solid content, vitamin C content, and color). Nisin treatment significantly (p<0.05) reduced bacterial population by 1.91-3.07 log CFU/mL. Nisin-citric acid combination provided 2.65-3.29 log CFU/mL reduction, while nisin-acetic acid combination provided 2.93-4.15 log CFU/mL reduction. The control treatment provided <1-2 fold log reductions. Slight variations in physicochemical properties of fresh-cut tomato were observed. Nisin and organic acids can be used to improve the microbial safety of fresh-cut tomato.
Adebola Olubukola Oladunjoye,Suren Singh,Oluwatosin Ademola Ijabadeniyi 한국식품과학회 2016 Food Science and Biotechnology Vol.25 No.5
The biocontrol of Listeria monocytogenes on fresh-cut tomato using nisin and organic acids was investigated. Fresh-cut samples inoculated with 108 CFU/mL of L. monocytogenes, treated with nisin (5,000 IU/mL), a combination of nisin and organic acids (acetic and citric acids at 3 and 5% each), with chlorine at 200 ppm as a control, and stored for six days at 4, 10, and 25oC were used to evaluate certain physicochemical qualities (pH, titratable acidity, soluble solid content, vitamin C content, and color). Nisin treatment significantly (p<0.05) reduced bacterial population by 1.91-3.07 log CFU/mL. Nisin-citric acid combination provided 2.65-3.29 log CFU/mL reduction, while nisin-acetic acid combination provided 2.93-4.15 log CFU/mL reduction. The control treatment provided <1-2 fold log reductions. Slight variations in physicochemical properties of fresh-cut tomato were observed. Nisin and organic acids can be used to improve the microbial safety of fresh-cut tomato.
Jun Wang,Wei Li,Dandan Niu,Suren Singh,Fuping Lu,Xiaoguang Liu 한국식품과학회 2017 Food Science and Biotechnology Vol.26 No.3
a-Glucosidase was immobilized onto an epoxyactivated resin (Eupergit C) to catalyze maltose into isomaltooligosaccharides (IMO), and then the effects of organic–aqueous media on the enzymatic properties of immobilized a-glucosidase were examined. An immobilization efficiency of 79.61% was obtained under the condition of pH 6.0, ionic strength of 2.0 M, and 30 mg of protein/g of resin. The butyl acetate-aqueous biphasic system was found to significantly improve the catalytic activity of the immobilized enzyme and the yield of IMO. The highest yield of IMO (50.83%, w/w) was obtained at pH 4.5 and 55 C in a butyl acetate/buffer system (25:75, v/v). In addition, the immobilized enzyme particles were distributed into the organic phase after the completion of transglycosylation, which facilitates the separation and recycling use of the immobilized enzyme. Immobilized aglucosidase retains a robust reusability in this continuous operation model. The present findings are of potential in improving the IMO manufacturing process.
Peng Song,Lei Cheng,Kangming Tian,Meng Zhang,Suren Singh,Dandan Niu,Bernard Prior,Nokuthula Peace Mchunu,Zheng-Xiang Wang 한국식품과학회 2020 Food Science and Biotechnology Vol.29 No.11
A new aminopeptidase (An-APa) was identified and biochemically characterized from Aspergillus niger CICIM F0215. It had maximal activity at 40 °C and pH 7.0 and exhibited a broad substrate specificity both on hydrophilic and hydrophobic amino acid residues at N-terminals. With An-APa hydrolysis for 1 h, the casein-pepsin and soybean protein isolates (SPI)-pepsin hydrolysates released both hydrophilic and hydrophobic amino acids and the hydrophobic amino acids having Q values (degree of hydrophobicity) greater than 1500 cal/mol were remarkably released. Leu, Ile, Phe, Tyr, Trp, Pro, Val and Lys in the casein hydrolysate after treatment with An-APa increased 18.61, 0.84, 11.35, 13.18, 3.34, 6.30, 7.46, and 8.19 mg/100 mL, respectively, and 19.72, 1.47, 18.37, 11.72, 4.61, 4.10, 8.13, and 5.85 mg/100 mL, respectively, in the SPI hydrolysate. Both accounted for 65.0% and 64.4% of total released free amino acids from casein and SPI hydrolysates, respectively. This indicated that An-APa could be potentially applicable in debittering protein hydrolysates.
( Zixing Dong ),( Xiaoling Chen ),( Ke Cai ),( Zhixin Chen ),( Hongbin Wang ),( Peng Jin ),( Xiaoguang Liu ),( Kugenthiren Permaul ),( Suren Singh ),( Zhengxiang Wang ) 한국미생물생명공학회(구 한국산업미생물학회) 2018 Journal of microbiology and biotechnology Vol.28 No.3
Owing to its high protein secretion capacity, simple nutritional requirements, and GRAS (generally regarded as safe) status, Bacillus licheniformis is widely used as a host for the industrial production of enzymes, antibiotics, and peptides. However, as compared with its close relative Bacillus subtilis, little is known about the physiology and stress responses of B. licheniformis. To explore its temperature-stress metabolome, B. licheniformis strains ATCC 14580 and B186, with respective optimal growth temperatures of 42℃ and 50℃, were cultured at 42℃, 50℃, and 60℃ and their corresponding metabolic profiles were determined by gas chromatography/mass spectrometry and multivariate statistical analyses. It was found that with increased growth temperatures, the two B. licheniformis strains displayed elevated cellular levels of proline, glutamate, lysine, pentadecanoic acid, hexadecanoic acid, heptadecanoic acid, and octadecanoic acid, and decreased levels of glutamine and octadecenoic acid. Regulation of amino acid and fatty acid metabolism is likely to be associated with the evolution of protective biochemical mechanisms of B. licheniformis. Our results will help to optimize the industrial use of B. licheniformis and other important Bacillus species.