Nitrophenyl glucoside hydrolysis as a potential time-temperature integrator reaction

Adams, J.B.; Langley, F.M.

doi:10.1016/s0308-8146(97)00143-x

Cited by 9 publications

(2 citation statements)

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“…Enzymatic TTIs use lipase (Agerhem and Nilsson, 1981;Blixt et al, 1977), a-amylase (Van Loey et al, 1997;Guiavarc'h et al, 2004;Yan et al, 2008) or b-glucosidase (Adams and Langley, 1998). Currently, the Vitsab TTI (Vitsab A.B., Malmö, Sweden), which uses lipase, is a commercially available, typical enzymatic TTI that can be used to check the quality assurance during ambient temperature marketing.…”

Section: Introductionmentioning

confidence: 99%

New enzymatic time–temperature integrator (TTI) that uses laccase

Kim

Lee

2012

Journal of Food Engineering

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Section: Introductionmentioning

confidence: 99%

New enzymatic time–temperature integrator (TTI) that uses laccase

Kim

Lee

2012

Journal of Food Engineering

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“…The more inhibitory activity the extract has, the less yellow the solution will have (measurable, lower absorbance value at 405 nm). To enhance colour, a basic solution must be added (optimal efficient medium pH 6.8) [35] so that there are enough electrons for the p-nitrophenolate anion to make resonance and stabilize [36]. This protocol was established in the laboratory.…”

Section: In Vitro α-Glucosidase Activity Assaymentioning

confidence: 99%

A New In Vivo Method for the Determination of α-Glucosidase Inhibition in Natural Products as Treatment for Diabetes Mellitus Type II

Torre¹,

Vizmanos²,

Cavero³

et al. 2023

Preprint

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Background: One of the main diseases of worldwide concern is non–insulin dependent Diabetes mellitus. 90-95% of patients with diabetes suffers from Type II diabetes, a metabolic diabetes whose prevalence is increasing in the world.Given the current prevalence of diabetes type II in society, research of natural compounds able to regulate glycaemia and insulin–resistance is nowadays covering importance, as alternative or co–adjuvant treatment to existing hypoglycaemic medicines. In pre–clinical steps of research, C. elegans is considered a promising in vivo model for the study of the molecular mechanism of glucose as part of anti–diabetic bioactivity.Most of the studies of insulin resistance with this in vivo model are carried out by using mutant strains such as daf-2 and the effects of the compounds are attributed a posteriori, after a physiological response of the worms rather than directly measuring preservation of activity inside the worm. Methods: The in vitro α-glucosidase inhibition of two oral formulations with Origanum vulgare extract before and after a simulated process of gastrointestinal digestion was evaluated. After confirming the in vitro activity, the α-glucosidase inhibition was tested in vivo through the new method proposed. Results: The crude extract showed an IC50 value similar to acarbose (positive control), before and after the gastrointestinal digestion. The encapsulated extract (111.86±1.25 µg/mL) did not present statistical differences with the positive control (110.10±1.15 µg/mL) after digestion. However, the powder formulation showed the highest hypoglycaemic activity (59.55±0.85 µg/mL).In vivo, the IC50 values showed similar profile than in vitro. Conclusion: A new simple and reliable method has been developed to determine pharmacological activities inside in vivo model C. elegans.The method has been evaluated with a hydroalcoholic extract of O. vulgare. The method is accurate and valid for the quantification of the inhibition of in vivo, allowing the direct attribution of this in vivo hypoglycaemic activity to the treatment. In addition, it opens the door to further research into in vitro pharmacological activities that require an in vivo counterpart.

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Microbial Methods

Holdsworth¹,

Simpson²

2015

Food Engineering Series

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Nitrophenyl glucoside hydrolysis as a potential time-temperature integrator reaction

Cited by 9 publications

References 3 publications

New enzymatic time–temperature integrator (TTI) that uses laccase

New enzymatic time–temperature integrator (TTI) that uses laccase

A New In Vivo Method for the Determination of α-Glucosidase Inhibition in Natural Products as Treatment for Diabetes Mellitus Type II

Microbial Methods

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