detergent enzyme
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2018 ◽  
Vol 30 (1) ◽  
pp. 24
Author(s):  
Nunung Rusminah ◽  
Indra Mustika Setia Pribadi ◽  
Komala Thillainathan

Introduction: Salvadora persica, also known as miswak (Kayu sugi), has been used as natural toothbrushing compound for centuries. Many research suggested that it contains medically beneficial properties such as abrasives, antiseptics, astringent, detergent, enzyme inhibitors, and fluoride. The objective of this study was to assess the efficacy of miswak containing toothpaste on dental plaque accumulation. Methods: The total of 30 subjects consisted of male students of Bandung Institute of Technology, aged between 18 – 26 years old. The plaque value was measured using the Turesky Gilmore & Glickman Index Modification of Quigley & Hein at baseline (day 0), day 1, day 3, and day 7. Commercial toothpaste (Pepsodent®) was used as the control group in this pre and post-test designed, single-blind study. Results: After analysed using the paired t-test, the data showed that the mean plaque index of respondents using miswak and non-miswak containing toothpaste from baseline until day 7, were 1.70/1.19 and 1.61/1.44 respectively (p < 0.05). The mean plaque index reduction of respondents using miswak and non-miswak containing toothpaste from baseline until day 7, were 0.39 and 0.25 respectively (p = 0.00). Conclusion: Both kinds of toothpaste were able to reduce plaque, but miswak containing toothpaste was found to be more effective in reducing dental plaque accumulation.


2016 ◽  
Vol 18 (3(71)) ◽  
pp. 195-200
Author(s):  
O.Y. Shynkaruk

We have developed a liquid enzyme detergent «Enzymyi» for sanitization of CIP–installations on milk plants that includes potassium hydroxide, complexones, proteolytic enzyme, stabilizers, and distilled water.The previous laboratory studies showed that the peak activity of «Enzymyi» on milk proteins was observed at as high as 65.8% at 60°C. Its activity decrease with the rise of temperature above 60 °C due to denaturation of enzymes since the heat causes changes in the primary structure and conformation of enzyme. It is also established that at pH solutions of 8.35 units proteolytic activity increased 1.7 times (P ≤ 0.01) compared to 7.2 pH units and reached its maximum activity 65.8 – 64%. Further increase of pH solutions from 8.35 units to 8.6 units contributed to gradual inhibition of enzymes resulting in reduction of proteolytic activity to 0. Proteolytic activity of the studied sample of enzyme detergent at water hardness of 0.357 mg–eq/l also reached the maximum of 60.5% and at increasing water hardness from 0.714 to 1.071 mg– eq/l PA decreased by 25.4% (P ≤ 0,05), i.e. with increasing water hardness PA reduced respectively. The article presents the study results as regards foam generating ability, foam stability and surface tension of solutions. The liquid detergent enzyme «Enzymyi» in concentrations of 0.03; 0.05; 0.07; 0.1; 0.3; 0.5; 0.7; 1% at the temperatures 20 °C and 60 °C was used for study. The article presents the study results as regards foam generating ability, foam stability and surface tension of solutions. The liquid detergent enzyme «Enzymyi» in concentrations of 0.03; 0.05; 0.07; 0.1; 0.3; 0.5; 0.7; 1% at the temperatures 20 °C and 60 °C was used for study.The results showed that «Enzymyi» practically doesn’t develop foam generating ability at the concentration from 0.03 to 1%. Foam stability does not exceed the standard, thus no more than 50% of the solution in 5 minutes that allows using the available composition for circulation washing of dairy equipment without its dismounting. 


2009 ◽  
Vol 390 (1) ◽  
Author(s):  
Martina Zimmermann ◽  
Martin S. Westwell ◽  
Susan A. Greenfield

Abstract Acetylcholinesterase (AChE) plays a central role in the development of Alzheimer's disease: AChE inhibition for preventing the characteristic dwindling of acetylcholine levels constitutes the current standard treatment for the disorder. Amongst the diverse risk factors contributing to the degenerative process, high cholesterol causes a reduction in the effectiveness of the otherwise therapeutic inhibitors of AChE. Our biochemical study on the activity of AChE elucidates the effect of amphiphilic molecules on the activity and kinetics of AChE, and sheds light onto the nature of the impact of these amphiphilic molecules on enzyme-inhibitor interactions. Using kinetic studies we discovered that detergents alter the enzymatic activity of AChE through an uncompetitive mechanism. Additional experiments using AChE inhibitors (amphiphilic procaine hydrochloride, hydrophobic tetrabutylammonium bromide) in the absence or presence of detergent further illustrate the detergent-enzyme-solvent interactions. The results contribute to the understanding of the importance of hydrophobic-lipophilic interactions for the correct function of AChE and its inhibitors. We present a model system for the study of lipid-related alterations in the activity of isolated AChE in the central nervous system. This model may also be used to assess and predict the effectiveness of AChE inhibitors, which are traditionally used for the treatment of cognitive impairment, under pathological (high-cholesterol) conditions.


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