scholarly journals Development of antimicrobial packaging materials with immobilized glucose oxidase and lysozyme

2013 ◽  
Vol 11 (7) ◽  
pp. 1066-1078 ◽  
Author(s):  
Kristýna Hanušová ◽  
Lukáš Vápenka ◽  
Jaroslav Dobiáš ◽  
Linda Mišková
Keyword(s):  
Glucose Oxidase ◽  
Specific Activity ◽  
Immobilized Enzymes ◽  
Lactobacillus Helveticus ◽  
Listeria Ivanovii ◽  
Agar Media ◽  
Ft Ir ◽  
Immobilized Glucose Oxidase ◽  
And Storage ◽  
Ft Ir Spectroscopy

AbstractPackaging based on immobilization of antimicrobial enzymes provides a promising form of active packaging systems applicable in food processing. Glucose oxidase and lysozyme were immobilized by the Ugi reaction with cyclohexyl isocyanide and glutaraldehyde on polyamide and ionomer films partially hydrolysed by hydrochloric acid. The immobilization of the enzymes on the surface of films was confirmed by FT-IR spectroscopy and the films were characterized by the specific activity of the immobilized enzymes. The enzyme migration into model solutions and the effect of pH, temperature and storage time on the activity of immobilized enzyme were also evaluated. Immobilization of lysozyme onto polyamide and ionomer films resulted in the loss of enzyme activity. The polyamide and ionomer films with immobilized glucose oxidase inhibited the growth of bacteria Escherichia coli CNCTC 6859, Pseudomonas fluorescens CNCTC 5793, Lactobacillus helveticus CH-1, Listeria ivanovii CCM 5884 and Listeria innocua CCM 4030 on agar media.

scholarly journals Polyethylene Migration from Food Packaging on Cheese Detected by Raman and Infrared (ATR/FT-IR) Spectroscopy

Materials ◽  
2021 ◽  
Vol 14 (14) ◽  
pp. 3872
Author(s):  
Klytaimnistra Katsara ◽  
George Kenanakis ◽  
Zacharias Viskadourakis ◽  
Vassilis M. Papadakis
Keyword(s):  
Vibrational Spectroscopy ◽  
Food Packaging ◽  
Time Frame ◽  
Low Density Polyethylene ◽  
Low Density ◽  
Ft Ir ◽  
Comparative Results ◽  
Short Time ◽  
And Storage ◽  
Ft Ir Spectroscopy

For multiple years, food packaging migration has been a major concern in food and health sciences. Plastics, such as polyethylene, are continuously utilized in food packaging for preservation and easy handling purposes during transportation and storage. In this work, three types of cheese, Edam, Kefalotyri and Parmesan, of different hardness were studied under two complementary vibrational spectroscopy methods, ATR-FTIR and Raman spectroscopy, to determine the migration of low-density polyethylene from plastic packaging to the surface of cheese samples. The experimental duration of this study was set to 28 days due to the degradation time of the selected cheese samples, which is clearly visible after 1 month in refrigerated conditions at 4 °C. Raman and ATR-FTIR measurements were performed at a 4–3–4–3 day pattern to obtain comparative results. Initially, consistency/repeatability measurement tests were performed on Day0 for each sample of all cheese specimens to understand if there is any overlap between the characteristic Raman and ATR-FTIR peaks of the cheese with the ones from the low-density polyethylene package. We provide evidence that on Day14, peaks of low-density polyethylene appeared due to polymeric migration in all three cheese types we tested. In all cheese samples, microbial outgrowth started to develop after Day21, as observed visually and under the bright-field microscope, causing peak reverse. Food packaging migration was validated using two different approaches of vibrational spectroscopy (Raman and FT-IR), revealing that cheese needs to be consumed within a short time frame in refrigerated conditions at 4 °C.

Immobilization of urease in poly(1-vinyl imidazole)/poly(acrylic acid) network

2010 ◽  
Vol 64 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Mehmet Şenel ◽  
Agah Coşkun ◽  
M. Fatih Abasıyanık ◽  
Ayhan Bozkurt
Keyword(s):  
Acrylic Acid ◽  
Enzyme Immobilization ◽  
Storage Stability ◽  
Polymer Network ◽  
Ft Ir ◽  
Basic Characteristics ◽  
And Storage ◽  
Menten Constant ◽  
Ft Ir Spectroscopy ◽  
Poly Acrylic Acid

AbstractIn this study, urease was immobilized in a polymer network obtained by complexation of poly(1-vinyl imidazole) (PVI) with poly(acrylic acid) (PAA). Preparation of the polymer network was monitored by FT-IR spectroscopy. Scanning electron microscopy (SEM) revealed that enzyme immobilization had a strong effect on film morphology. Proton conductivity of the PVI/PAA network was measured via impedance spectroscopy under humidified conditions. Values of the Michaelis-Menten constant (K M) for immobilized urease were higher than for the free enzyme, indicating a decreased affinity of the enzyme to its substrate. The basic characteristics (pHopt, pHstability, T opt, T stability, reusability, and storage stability) of immobilized urease were determined. The results show that the PAA/PVI polymer network is suitable for enzyme immobilization.

scholarly journals Characterization of the Spindle Morphology Nanomicelles Assembled from Sericin and Gelatin

2017 ◽  
Vol 2017 ◽  
pp. 1-9
Author(s):  
Xiaozhou Su ◽  
Lei Li ◽  
Weihan Huang
Keyword(s):  
Electron Microscopy ◽  
Protein Concentration ◽  
Scanning Calorimetry ◽  
Force Microscopy ◽  
Atomic Force ◽  
Transmission Electron ◽  
Ft Ir ◽  
And Storage ◽  
Ft Ir Spectroscopy

Complex nanomicelles were prepared by sericin and type A gelatin with molecular weight of 5789 Da and 128664 Da separately. The assembling conditions were as follows: mass ratio (sericin/gelatin) was 1 : 1, protein concentration was 0.5%, temperature was 35°C, and assembling time was 18 hours. Scanning electron microscopy (SEM), atomic force microscopy (AFM), transmission electron microscopy (TEM), Fourier transform infrared (FT-IR) spectroscopy, differential scanning calorimetry (DSC), and dynamic light scattering (DLS) were conducted to observe and characterize the complex nanomicelles. Results showed that the complex sericin/gelatin micelles was a kind of nanospindle micelles. The micelles had high electrochemical stability, thermal stability, antidilution stability, and storage stability.

scholarly journals Immobilization of Alkaline Collagenase from Bacillus subtilis onto Sulfonated Polystyrene Nanospheres for Hydrolysis of Tilapia Collagen

2019 ◽  
Vol 2019 ◽  
pp. 1-14
Author(s):  
Ling Zhang ◽  
Xiaocui Yang ◽  
Kaijun Xiao ◽  
Yuyi Lu ◽  
Chunhai Li ◽  
...  
Keyword(s):  
Particle Size ◽  
Bacillus Subtilis ◽  
Ir Spectroscopy ◽  
Specific Activity ◽  
Average Particle ◽  
Enzyme Protein ◽  
Sulfonated Polystyrene ◽  
Polystyrene Nanospheres ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

The structure of an alkaline protease from Bacillus subtilis used by a tilapia collagen peptide manufacturer was analyzed, and the technology of the enzyme immobilized by sulfonated polystyrene (SPS) nanoparticles was studied. The particle size distribution, SEM, EDS, TEM, and FT-IR spectroscopy of the carrier before and after immobilization were analyzed. The results showed that the molecular weight of the purified enzyme protein was 31.0 kDa. The amino acid sequence with a consistency of 64.04% and one three-dimensional structure simulation diagram of the purified enzyme protein were obtained by LC-MS-MS, which suggested that the protein might belong to subtilisin. The optimal immobilization conditions were as follows: the volume ratio of the immobilization carrier to the enzyme was 3 : 50 (mL : mL), the immobilized temperature was 25°C, and the system pH was 4.5. Under this condition, the immobilization ratio of collagenase was 73.48%, the specific activity was 274.05 U/μg, and the specific activity of the immobilized enzyme was about 53.74% that of the free enzyme. The average particle size of SPS nanospheres was 155.1 nm. The characterization results of SEM, EDS, TEM, and FT-IR spectroscopy showed that the collagenase was successfully immobilized onto SPS nanospheres. The experimental results also showed that the collagenase could be immobilized effectively under the optimal conditions by using SPS nanospheres, and the operation process was simple, feasible, and of low cost with good prospect of industrial application.

Measurement of glucose in plasma, with use of immobilized glucose oxidase and peroxidase.

1976 ◽  
Vol 22 (8) ◽  
pp. 1378-1382 ◽  
Author(s):  
S W Kiang ◽  
J W Kuan ◽  
S S Kuan ◽  
G G Guilbault
Keyword(s):  
Uric Acid ◽  
Blood Plasma ◽  
Glucose Oxidase ◽  
Immobilized Enzymes ◽  
Magnetic Stirrer ◽  
Immobilized Glucose Oxidase

Abstract We describe a novel fluorometric technique for simple, rapid, and economical assay of glucose by use of immobilized glucose oxidase and peroxidase. A cylindrical magnetic stirrer was specially designed to hold the immobilized enzymes firmly and to allow the reaction minzymic transformation quickly. Blood plasma can be assayed directly with no pretreatment. Ascrobic acid, uric acid, and creatinine in concenctrations of 0.25, 0.25, and 0.2 g/liter, respectively, did not interfere. The linearity of the assay was extended to 4.0 g of glucose concentrations. Results by our technique and by the otoluidine or hexokinase methods agreed well. The immobilized enzymes are stable for several months and can be used for several hundred highly accurate and reproducible assays.

Application of immobilized enzymes to clinical analyses : use of co-immobilized glucose oxidase and peroxidase in column form

Biochimie ◽  
1980 ◽  
Vol 62 (8-9) ◽  
pp. 581-585 ◽  
Author(s):  
Takashi Murachi ◽  
Yoshiaki Sakaguchi ◽  
Masayoshi Tabata ◽  
Megumi Sugahara ◽  
Jiro Endo
Keyword(s):  
Glucose Oxidase ◽  
Immobilized Enzymes ◽  
Immobilized Glucose Oxidase

scholarly journals Determination of Glucose in Dried Serum Samples by Fourier-Transform Infrared Spectroscopy

1999 ◽  
Vol 45 (9) ◽  
pp. 1530-1535 ◽  
Author(s):  
Cyril Petibois ◽  
Vincent Rigalleau ◽  
Anne-Marie Melin ◽  
Annie Perromat ◽  
Georges Cazorla ◽  
...  
Keyword(s):  
Fourier Transform ◽  
Ir Spectroscopy ◽  
Glucose Oxidase ◽  
Glucose Concentration ◽  
Internal Standard ◽  
Fourier Transform Infrared ◽  
Serum Samples ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Abstract Background: Practical improvements are needed to allow measurement of glucose concentrations by Fourier- transform infrared (FT-IR) spectroscopy. We developed a new method that allows determination of the glucose concentration in dried sera. Methods: We studied 32 serum samples after fourfold dilution and desiccation before FT-IR analyses on a spectrometer operated at a resolution of 2.0 cm−1. We integrated all spectral windows at the surface of the spectrum in the C—O region. For comparison, glucose was measured in the sera by a glucose oxidase method. Results: One peak within the spectrum was most specific for glucose (997–1062 cm−1). Its surface integration showed a strong relationship with reference data (r = 0.998; P <0.001). FT-IR analyses of five glucose solutions were performed to determine its specific absorption at the same peak. In this way, glucose concentrations in serum spectra could be measured. For the first time while using FT-IR spectroscopy, no manipulation of spectra nor use of internal standard was necessary to obtain results in high accordance with glucose concentration measured by a conventional (glucose-oxidase) method (Sy|x = 0.25 mmol/L; r = 0.998). Conclusions: FT-IR spectroscopy appears to be an easy and accurate method to determine glucose concentration and could be widely used to simultaneously identify and quantify several metabolites in biological fluids or tissues.

Novelty of Penicillium camembertii Lipase Supported on Glutaraldehyde Activated-SBA-15 Mesoporous Silica for Mono-Esterification of Bioglycerol in Non-Aqueous Media

2016 ◽  
Vol 14 (4) ◽  
pp. 919-928 ◽  
Author(s):  
Moreshwar P. Hude ◽  
Janusz Kozinski ◽  
Ajay K. Dalai ◽  
Ganapati D. Yadav
Keyword(s):  
Food Industry ◽  
Immobilized Lipase ◽  
Aqueous Media ◽  
Immobilized Enzymes ◽  
X Ray Diffraction ◽  
X Ray ◽  
Penicillium Camembertii ◽  
Ft Ir ◽  
Environmentally Friendly Approach ◽  
Ft Ir Spectroscopy

Abstract Hexagonal mesoporous type silica SBA-15 with pore sizes in the range 5.0–8.3 nm was synthesized using non-ionic triblock copolymer and characterized by Accelerated Surface Area Porosimetry (ASAP), FT-IR spectroscopy, X-ray diffraction (XRD) and Scanning Electron Microscopy (SEM). Different lipases were immobilized in glutaraldehyde activated mesoporous SBA-15 support. The resulting supported enzymes were shown to be active and stable catalysts for esterification of glycerol with oleic acid to produce monoglyceride (MG) which is commonly used in food industry. Various parameters were studied systematically to study kinetics. MG Synthesis using enzymatic process is an environmentally friendly approach. Enzyme immobilized on SBA-15 showed the best stability and catalytic activity in organic solvents. Out of various lipases studied penicillium camembertii (Lipase G) produced MG efficiently at low temperature. Reusability was studied on immobilized enzymes. Immobilized lipase maintained 90 % of its esterification activity in non-aqueous media even after 4 cycles of use. The selectivity of Lipase G is found to be 98 % for monoacylglyceride.

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