ISOLATION AND PURIFICATION OF 3-MERCAPTOPYRUVATE SULFURTRANSFERASE FROM THE GUT OF RHINOCEROS LARVA (ORYCTES RHINOCEROS) | Blazingprojects Postgraduate Thesis
Home / Biochemistry / ISOLATION AND PURIFICATION OF 3-MERCAPTOPYRUVATE SULFURTRANSFERASE FROM THE GUT OF RHINOCEROS LARVA (ORYCTES RHINOCEROS)

ISOLATION AND PURIFICATION OF 3-MERCAPTOPYRUVATE SULFURTRANSFERASE FROM THE GUT OF RHINOCEROS LARVA (ORYCTES RHINOCEROS)

 

Table Of Contents


  • Title page   —       –       –       –       –       –       –       –       –       –       – i     Declaration —       –       –       –       –       –       –       –       –       –       -iiApproval page —   –       –       –       –       –       –       –       –       –       -iiiDedication —         –       –       –       –       –       –       –       –       –       -ivAcknowledgement —       –       –       –       –       –       –       –       –       -v     Table of content   —         –       –       –       –       –       –       –       –       -vi                 Abstract —   –       –       –       –       –       –       –       –       –       –       -vii

Thesis Abstract

Cyanide is known to be one of the most toxic substances present in a wide variety of food materials that are consumed by animals.
One of the cyanide detoxifying enzymes is 3-mercaptopyruvate sulfurtransferase (3-MST). Indeed, recent studies have clearly shown that 3-MST is involved in the detoxification of cyanide.
Rhinoceros (Oryctes rhinoceros) larva feeds on dead, decayed and living plants, wood and palm. Plants are known to contain cyanide as a defence mechanism for intruding/pesting organisms. Thus, for rhinoceros larva to be able to live on plants, it must have possessed a cyanide-detoxifying enzyme.
3-MST, a cyanide-detoxifying enzyme was purified from Rhinoceros (Oryctes rhinoceros) larva in this work.
The 3-MST enzyme was isolated from the gut of Oryctes rhinoceros larvae and purified using Ammonium Sulphate Precipitation, Bio-Gel-P-100 Gel Filtration Chromatography and Reactive Blue-2-Agarose Affinity chromatography.
The specific activity of the enzyme was 0.22U/mg.
The presence of this enzyme could be exploited by including it in the diet of animals which would serve as a source of protein and 3-MST. Perhaps, these rhinoceros larva could be introduced on farmland with contaminated soil whereby they will process the dead roots and plants into soil thereby providing more space and manure for plants to grow healthy.

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