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INTERNATIONAL JOURNAL OF PHARMACEUTICAL RESEARCH

A Step Towards Excellence
Published by : Advanced Scientific Research
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0975-2366
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IJPR 9[3] July - September 2017 Special Issue

July - September 9[3] 2017

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Biodegradation of Toluene Driven Egg Albumin preparation by Alkaline Protease for Release of Entrapped Glycine Max Amylase

Author: KIRTI SHARMA
Abstract: Albumin is main constituent of total protein in human plasma and biodegrades into amino acids as its natural products which are non-toxic in nature as well as easily metabolized in body too. Due to these exploitable features, it is excellent bio-matrix material used for the enzyme entrapment. Amylase is a well known industrial important enzyme which digests starch into maltose from the non-reducing end and produces limit dextrins. This property of amylase has a wide application in food, pharmaceutical, paper, leather, detergent and textile industries. Hence, in present study, egg albumin was used for entrapment of Glycine max amylase as biocompatible and eco-friendly matrix in which chemically modification was done by toluene. Various kinetic properties were studied for Glycine max amylase and its % of entrapment of enzyme into toluene driven chemically modified egg albumin was estimated. . Biodegradation was done by incubating it with varying unites of alkaline protease (5U, 10U, 15U, 20U and 25U) to study controlled and consistent release of entrapped Glycine max amylase from toluene driven chemically modified egg albumin preparation. This entrapment of Glycine max amylase into toluene driven chemically modified egg albumin was led to have enhanced stability for 6 months upon preservation with 40% activity loss as compared to free Glycine max amylase.
Keyword: Glycine max; egg albumin; glutaraldehyde; toluene
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