Ultraviolet irradiation of trypsin, lysozyme and β-galactosidase: how does UVC affect these enzymes when used as a secondary barrier against adventitious agents?

Gabriel, Michelle; Dare, Emma V.; Meunier, Sarah M.; Campbell, J. Larry; Sasges, Michael; Aucoin, Marc G.

doi:10.1016/j.vaccine.2019.08.063

Cited by 6 publications

(5 citation statements)

References 34 publications

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“…In general, the results demonstrated that EA tend to decrease as ultraviolet (UV) irradiation exposure time increase. This findings aligns with previous study which indicated the protein denaturation and enzyme inactivation due to UV irradiation [12,13,16]. Another study by Kristo et al…”

Section: Enzyme Activity Of Crude Enzymesupporting

confidence: 93%

“…Their previous study also exploited the ultraviolet (UV) irradiation to enhance EA of protease from head shrimp [8,11]. Their findings contradicted other studies that generally reported enzyme inactivity after UV exposure [12,13]. However, the use of UV irradiation as a pretreatment to retrieve protease from AC intestines has not been explored yet.…”

Section: Introductionmentioning

confidence: 94%

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Ultraviolet irradiation effect on characteristics of protease enzyme from African catfish (Clarias sp.) intestines

Tamaya,

Suwanto,

Hernawan

et al. 2023

IOP Conf. Ser.: Earth Environ. Sci.

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The goal of this study was to investigate the impact of UV-C irradiation on the activity of crude enzymes derived from African Catfish intestines as well the optimum conditions for subsequent autolysis processes. Three key variables were assessed: UV-C exposure time, pH and temperature. The experiments involved the homogenization of intestines in cold distilled water followed by subjecting the mixture into UV-C treatment for exposure times of 0, 10, 20 and 30 minutes. After centrifugation process, the collected supernatant was utilized as the crude enzyme. At various level of temperature (40, 50, 60°C) and pH (6, 7, 8) the activity of crude enzyme was assayed with casein as substrate. The findings revealed the increasing of EA as the UV-C exposure time decreased and pH increased, while the highest EA value was observed at temperature of 50°C. Consequently, the optimal conditions were identified as follows: 0 minutes of UV-C exposure time, pH of 8, and temperature of 50°C. Furthermore, UV-Vis absorption, FTIR, and fluorescence spectroscopy of the crude enzyme after UV-C irradiation induction was studied to investigate the its conformational changes. These additional analyses provided valuable insights into the structural alterations of the crude enzyme caused by the UV-C treatment.

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Section: Enzyme Activity Of Crude Enzymesupporting

confidence: 93%

Section: Introductionmentioning

confidence: 94%

Ultraviolet irradiation effect on characteristics of protease enzyme from African catfish (Clarias sp.) intestines

Tamaya,

Suwanto,

Hernawan

et al. 2023

IOP Conf. Ser.: Earth Environ. Sci.

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show abstract

“…Moreover, a redshift of protease absorption peaks occurred at 220–225 and 280–285 nm, suggesting that UV‐C irradiation changed the microenvironment of some amino acids. UV‐C irradiation may lead to the modification of aromatic residues (Gabriel et al ., 2019), resulting in structural changes. At the same time, the side chain groups of aromatic amino acid molecules were gradually exposed to the solution.…”

Section: Resultsmentioning

confidence: 99%

“…UV‐C is ultraviolet light with a wavelength of 200 to 280 nm. Owing to the presence of aromatic residues (tryptophan, tyrosine, and phenylalanine) and disulphide bonds, proteins strongly absorb UV light at around 280 nm (Gabriel et al ., 2019). Consequently, UV‐C irradiation resulted in modifications of aromatic and cystine residues, which result in structural changes that affect protein function.…”

Section: Introductionmentioning

confidence: 99%

Activation of the endogenous acid protease in the head of Litopenaeus vannamei induced by UV‐C irradiation

Dou

Wang

Cao

et al. 2023

Int J of Food Sci Tech

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Previous studies have found that UV-C irradiation activated endogenous acid protease (EAP) in shrimp heads. Aiming at understanding the effect of UV-C irradiation on the activation of EAP and improving the utilisation of EAP, the effect of UV-C irradiation on the enzymatic properties and conformation of EAP was investigated. The enzymatic properties of EAP were unaltered after UV-C irradiation, and the optimum pH, temperature, and NaCl concentration were 3, 60°C, and 0.5 mol/L, respectively. Ca 2+ and Mg 2+ activated the enzyme. The molecular weight of the purified endogenous acid protease (P-EAP) was 32 kDa. UV-Vis, FTIR, circular dichroism, and fluorescence spectroscopy indicated that the increase in enzyme activity by UV-C irradiation was related to an increase in tryptophan and hydrogen bonding, implying that it may be the change in the spatial structure of the protein that caused the activation of the enzyme. Results revealed that UV-C irradiation can be used to activate proteases and provide a reference for enhancing the enzymatic activity of other enzymes from shrimp heads.

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“…This trypsinization process to solubilize wall proteins has been revealed by Iranzo et al (2002), herein, its effect on UV inactivation was further evidenced. Gabriel et al (2019) reported that extreme UV irradiation of trypsin displayed minimal impact on trypsin function, the activity and structure of trypsin was metastable. That means the added trypsin could be active throughout the whole trails (see Fig.…”

Section: Effect Of Trypsin-uv Sequential Disinfection On Viabilitymentioning

confidence: 99%

WITHDRAWN: Synergism in sequential inactivation of Cryptosporidiumparvum with trypsin and UV irradiation

Xiao

Wang

Chen

et al. 2022

Preprint

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Cryptosporidium in wastewater presents a major public health concern for water safety. However, bactericidal efficiencies of Cryptosporidium oocysts using conventional disinfection methods are still hampered due to the resistance produced by their thick outer wall. In this study, we present a novel UV inactivation with significantly enhanced efficiency by trypsin pretreatment. Notably, the inactivation performance (log-reduction) of oocysts was 73.75-294.72% higher than that obtained in individual UV irradiation under identical conditions. Experimental observations and supporting mechanistic analyses suggest that the trypsin can cleave proteins layer on oocyst wall, which facilitates UV irradiation to penetrate into the oocysts and attack their genomic DNA (gDNA). The trypsin displayed considerable operational stability in the reaction mixture, and its dissociation effect of oocyst wall was indicated by the fact that 64.50% of oocysts displayed early apoptosis after trypsinization. The combined treatment almost totally destroyed the oocysts coat and deformed their shape according to scanning electron microscopy. This resulted in the release of cellular proteins and gDNA, and their concentrations in bulk solution increased by 1.22–8.60 times. As UV irradiation time was prolonged, gDNA was degraded into small fragments with lower molecular weight. Both the laddering and diffuse smear patterns in the gel indicated significant detrimental effect on gDNA and viability of oocysts. Overall, this study demonstrates the enhanced UV inactivation of Cryptosporidium oocysts by trypsin and provides the underlying mechanisms for the process.

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Ultraviolet irradiation of trypsin, lysozyme and β-galactosidase: how does UVC affect these enzymes when used as a secondary barrier against adventitious agents?

Cited by 6 publications

References 34 publications

Ultraviolet irradiation effect on characteristics of protease enzyme from African catfish (Clarias sp.) intestines

Ultraviolet irradiation effect on characteristics of protease enzyme from African catfish (Clarias sp.) intestines

Activation of the endogenous acid protease in the head of Litopenaeus vannamei induced by UV‐C irradiation

WITHDRAWN: Synergism in sequential inactivation of Cryptosporidiumparvum with trypsin and UV irradiation

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