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Nanotechnology Applications in Packaging of Dairy and Meat Products
Published in Lohith Kumar Dasarahally-Huligowda, Megh R. Goyal, Hafiz Ansar Rasul Suleria, Nanotechnology Applications in Dairy Science, 2019
Preeti Birwal, Priyanka Rangi, Menon Rekha Ravindra
A variation of this approach involves the incorporation of metal or metal oxide nanoparticles in polymer nanocomposites to give antimicrobial “active” packaging. In comparison to molecular antimicrobials, inorganic nanoparticles can be assimilated easily into polymers, improving the suitability and functionality of the engineered material as a food package.7,28 The Ag, Zn, Mg, Cu, and Ti are metal nanomaterials, which are commonly used for antimicrobial activity, antimicrobial films like sodium benzoate and benomyl, acid, and ethanol. Other elements (Si, Na, Al, S, Cl, Ca, Fe, Pd), edible clove, pepper, cinnamon, coffee, chitosan, antimicrobial lysozyme, and bacteriophages, and gas scavengers are being evaluated in the development of active packaging.3 Enzymatic oxygen scavenging is achieved by alcohol oxidase enzyme.53
Biodegradation of Lignin
Published in Jean-Luc Wertz, Magali Deleu, Séverine Coppée, Aurore Richel, Hemicelluloses and Lignin in Biorefineries, 2017
Jean-Luc Wertz, Magali Deleu, Séverine Coppée, Aurore Richel
Besides ligninases, other fungal extracellular enzymes, which act as accessory enzymes, are involved in lignin degradation.1 These include oxidases generating hydrogen peroxide required by peroxidases, and mycelium-associated dehydrogenases, which reduce lignin-derived compounds (Figure 7.1l). Oxidases generating hydrogen peroxide include aryl-alcohol oxidase (AAO) found in various fungi, such as P. eryngii, and glyoxal oxidase (GLOX, a copper-radical protein) found in P. chrysosporium. Furthermore, aryl-alcohol dehydrogenases (AAD) and quinone reductases (QR) are also involved in lignin degradation by fungi (Figure 7.1m). Moreover, it has been shown that cellulose dehydrogenase (CDH), which is produced by many different fungi under cellulolytic conditions, is also involved in lignin degradation in the presence of hydrogen peroxide and chelated Fe ions. It has been proposed that the effect of CDH on lignin degradation is through the reduction of quinones, to be used by ligninolytic enzymes or the support of a Mn-peroxidase reaction (Figure 7.1n).1
A novel amperometric bienzymatic biosensor based on alcohol oxidase coupled PVC reaction cell and nanomaterials modified working electrode for rapid quantification of alcohol
Published in Preparative Biochemistry and Biotechnology, 2018
Vinita Hooda, Vikas Kumar, Anjum Gahlaut, Vikas Hooda
An amperometric alcohol biosensor was fabricated by covalently immobilizing alcohol oxidase onto PVC surface and HRP onto the CHIT/AgNPs/c-MWCNT/Nf modified Au electrode. To evaluate the redox potentials of the fabricated biosensor, cyclic voltammetry was done as shown in Figure 7. There were no clear peaks for bare Au electrode (curve a). The working electrode HRP/AgNPs/CHIT/c-MWCNT/Nf/Au prepared by immobilizing AgNPs-CHIT and HRP on the c-MWCNT/Nf film showed a pair of redox peaks at −0.24 V and −0.35 V, which highlights the characteristic potential for direct electrochemistry of HRP[34] (curve b). Subsequent immobilization of AOX onto the surface of PVC beaker was done to generate complete assembly of the biosensor. The generated assembly (curve c) displayed redox peaks comparable to curve b but with enhanced peak currents. The formal potential of the redox couple at the bioelectrode assembly was −0.29 V, calculated from the average value of anodic and cathodic peak potentials [(Epa+Epc)/2]. This potential was nearly conforming to the earlier reports for HRP (FeIII/FeII) on direct electrochemistry.[35] With addition of ethanol to the fabricated biosensor, the magnitude of cathodic peak current was found to be considerably higher relative to the anodic peak current (curve d) which further confirmed the redox potential of HRP. Alcohol oxidase (immobilized on to PVC beaker) catalyze the oxidation of alcohol to generate H2O2 which is then biocatalytically reduced by the HRP (present on the working electrode) resulting in the formation of HRP (Ox). At potential of −0.35 V, HRP (Ox) electrocatalytically reduced to HRP (Red) on the electrode surface through DET mechanism and revived the reaction for the next cycle as shown in equation below.