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ISSN: 2167-065X

Clinical Pharmacology & Biopharmaceutics
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Research Article

Evaluation of the Impact of Biofield Treatment on Physical and Thermal Properties of Casein Enzyme Hydrolysate and Casein Yeas t Peptone

Trivedi MK, Nayak G, Patil S*, Tallapragada RM, Jana S and Mishra R
Trivedi Global Inc., 10624 S Eastern Avenue Suite A-969, Henderson, NV 89052, USA
*Corresponding Author : Shrikant Patil
Trivedi Global Inc., 10624 S Eastern
Avenue Suite A-969, Henderson, NV 89052, USA
Tel: +1 602-531-5400
E-mail: publication@ trivedieffect.com
Received: June 10, 2015 Accepted: June 29, 2015 Published: July 06, 2015
Citation: Trivedi MK, Nayak G, Patil S, Tallapragada RM, Jana S, et al (2015) Evaluation of the Impact of Biofield Treatment on Physical and Thermal Properties of Casein Enzyme Hydrolysate and Casein Yeast Peptone. Clin Pharmacol Biopharm 4:138. doi:10.4172/2167-065X.1000138
Copyright: © 2015 Trivedi MK, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

In the present study, the influence of biofield treatment on physical and thermal properties of Casein Enzyme Hydrolysate (CEH) and Casein Yeast Peptone (CYP) were investigated. The control and treated samples were characterized by Fourier transform infrared (FT-IR) spectroscopy, differential scanning calorimetry (DSC), Thermo Gravimetric Analysis (TGA), particle size and surface area analysis. The FTIR results revealed that biofield treatment has caused reduction of amide group (amide-I and amide-II) stretching vibration peak that is associated with strong intermolecular hydrogen bonding in treated CEH as compared to control. However, no significant changes were observed in FTIR spectrum of treated CYP. The TGA analysis of treated CEH showed a substantial improvement in thermal stability which was confirmed by increase in maximum thermal decomposition temperature (217°C) as compared to control (209°C). Similarly, the treated CYP also showed enhanced thermal stability as compared to control. DSC showed increase in melting temperature of treated CYP as compared to control. However the melting peak was absent in DSC of treated CEH which was probably due to rigid chain of the protein. The surface area of treated CEH was increased by 83% as compared to control. However, a decrease (7.3%) in surface area was observed in treated CYP. The particle size analysis of treated CEH showed a significant increase in average particle size (d50) and d99 value (maximum particle size below which 99% of particles are present) as compared to control sample. Similarly, the treated CYP also showed a substantial increase in d50 and d99 values which was probably due to the agglomeration of the particles which led to formation of bigger microparticles. The result showed that the biofield treated CEH and CYP could be used as a matrix for pharmaceutical applications.

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