The Anatomy of this project write-up encompasses the ordinary look of enzymes as organic molecules, rather it sheds more light into the comprehensive view and determination of the catalytic and specific activity enzymes particularly – DIASTASE, MALTASE & ZYMASE can exploit in industrial application; also critically important is the selectively ways of providing fundamental data which allows the society – particularly small-scale brewers to understand and exploit the chemistry of fermentation by enzymes. The method employed in this project involves three processes namely:

1. The preparation of the enzymes by fermentation

2. The preparation of the starch substrate from maize

3. The Overall process Development involving both the products of the 1^st and 2^nd processes.

The results of the method and procedures employed in this project are:

i. That enzyme activities in biochemical processes involves catalysis – through binding of the enzyme molecule and the substrate.

ii. The remarkable specifically for substrates.

Finally, all enzymes in fermentation of starch whose catalytic properties rely on their molecular structure and arrangement are stabilized by interactions between their constituents. This is conclusively evident in the chemistry of the fermentation process in starch, which is later discussed and highlighted in this write-up.

TABLE OF CONTENTS

Title page

Certification

Dedication

Acknowledgement

Abstract

Table of contents

CHAPTER ONE

1.0 INTRODUCTION

1.1 Background Information

1.2 Aim of the Study

1.3 Objectives of the Study

1.4 Limitation of the Study

1.5 Significance of the Study

1.6 Statement of Problem

CHAPTER TWO

2.0 LITERATURE REVIEW

2.1 Chemistry of Fermentation

2.2 The role of the Enzymes

CHAPTER THREE

3.0 MATERIALS AND METHODOLOGY

3.1 Materials and Equipments

3.2 Methodology and Procedures

3.3 The Process Development

3.4 Preparation of the Enzymes by Fermentation

3.5 Preparation of the Starch Substrate from Maize

3.6 Flowchart Representing the Overall Process Development

CHAPTER FOUR

4.0 RESULTS

4.1 Conclusion

CHAPTER FIVE

5.0 RECOMMENDATION

REFERENCES

CHAPTER ONE

1.1 BACKGROUND INFORMATION

The primary aim of this project is centered on the determination of the catalytic and specific activities of enzymes in fermentation of starch from maize. These enzymes are DIASTASE, MALTASE and ZYMASE. This determination study is made possible through certain unique properties which these collection of enzymes posses.

Speaking in concrete terms, ENZYMES serve as biocatalysts, speeding up chemical reactions. Like those involved with fermentation of starch. Enzyme molecules accelerate the rate of reactions, often by many orders of magnitude, thereby allowing the substance involved undergo a chemical breakdown.

Enzymes in fermentation of starch go about their work in an ASSEMBLY-LINE fashion, each enzyme performing a specific task at a particular stage of the fermentation process. For instance, the enzyme – MALTASE, breaks down MALTOSE into two isomeric fermentable sugars namely - Glucose and Fructose; thereby preparing another stage for another enzyme to act during the fermentation process. Enzymes in fermentation process, especially in starch; perform their work at blinding speed.

A single molecule of enzyme can catalyze thousands of chemical reactions per second. This is because enzymes in fermentation reaction particularly in starch have a marked ability to accelerate the reaction and also to promote the specific processes involved under the chemically mild conditions, which prevails in the fermentation process.

In all ways, these enzymes readily make essential physiochemical contributions to the fermentation process by virtue of their organized and involved three-dimensional structure, which reveals certain regions on the enzyme surface where small solute molecules or ions can bind reversibly. Such solutes are called LIGANDS; a term borrowed from ORGANOMETALLIC CHEMISTRY.

There may be many ligard-binding sites on the surface of an enzyme. But each site usually possesses the power to bind only a limited range of ligards, by virtue of the character of the site. The term “CHARACTER” is here used to cover not only the three-dimensional shape of the site but also its charge characteristics and to what degree it is hydrophobic or hydrophitic.

The character of a binding site is clearly a function of the amino acid side chains that are brought together there by the folding of the polypeptide chain. Enzymes are distinguished from other protein molecules by having ACTIVE SITES. The substrate binds at the active site of its enzyme in much the same way as other ligards might do, but once bound there, a chemical reaction ensures because of the special nature of the enzyme active site in respect to their catalysis and specificity in fermentation bio-process.