SCREENING, CHARACTERIZATION AND OPTIMIZATION OF ALKALINE PROTEASE PRODUCED FROM BACILLUS SUBTILIS ISOLATED FROM TRADITIONALLY FERMENTED FOOD

  • 0 Review(s)

Product Category: Projects

Product Code: 00007200

No of Pages: 130

No of Chapters: 1-5

File Format: Microsoft Word

Price :

₦5000

  • $

ABSTRACT

Enzymes are considered environmentally friendly (green) chemicals that have the potential to completely replace or reduce the use of hazardous chemicals in industrial processes, thereby promising sustainable production and manufacturing. Proteases derived from microbes have almost all of the properties required for biotechnological applications. This study was conducted with the aim of screening for potent protease-producing bacteria from Bacillus subtilis, determining optimal production conditions and partially characterizing the stability of the protease with regards to some physicochemical parameters. Hence, identification of Bacillus subtilis at a molecular level and purification as well as detailed characterization of the types of the proteases are recommended for effective utilization in different area of applications as the purification of the extract from the study yielded 71.3%-fold with high specific activity of 2787.1U/g. Based on optimization of physicochemical parameters and nutritional parameters for the optimum production of protease, the optimum temperature of protease production was 40°C with protease concentration of 32.9 ±1.60U/g. pH 9 was the optimum for production of protease with protease concentration of (14.1±1.40U/g and 22.7±2.1U/g) for both phosphate and carbonate buffers respectively. Among the metallic ions, media containing Mn2+ performed better than Cu2+, Mg2+, Fe2+, and Zn2+ with a protease concentration of 24.6±2.45U/g and 23.3±1.31U/g at 5mM and 1mM respectively. Studies on the effect of concentration of divalent ions revealed that both the activity and stability of protease was better in 5mM than in 1mM concentration. Furthermore, evaluation of some agro-industrial wastes as potential substrates for protease production indicated that wheat bran was better for carbon agro-residues (3.9±0.30U/g), whereas soybean meal was better for nitrogen agro-residues (4.0±0.23U/g). Since protease was produced from readily available complex substrates and agro-residues, Bacillus subtilis appear to have substantial potential for application in various proteolytic processes. Also, from the study, it was observed that immobilized alkaline protease from Bacillus subtilis was most compatible with the laboratory-based detergent Tween 20 and consequently showed highest protease activity of 6.3±0.62U/g, and also the enzyme showed highest compatibility with the commercial detergent omo and ariel and consequently showed highest protease activity of 5.8±0.55U/g and 5.0±0.10U/g respectively. Finally, in this study, stain removal was very efficient and haemolysis of blood occurred within a minute of enzyme action on the blood stain. An addition of purified alkaline protease from Bacillus subtilis effectively removed the stain. It could therefore be used as an additive in laundry detergents.




TABLE OF CONTENTS

                                                                                                                        Page

Title Page                                                                                                        i

Declaration                                                                                                      ii

Dedication                                                                                                     iii

Certification                                                                                                    iv

Acknowledgments                                                                                          v         

Table of Contents                                                                                           vi        

List of Tables                                                                                                  x

List of Figures                                                                                                 xi

Abstract                                                                                                          xii

 

CHAPTER 1: INTRODUCTION                                                                  1

1.1              Background of the Study                                                                   1

1.2              Statement of the Problem                                                                   2

1.3              Justification of the Study                                                                   3

1.4              Aim and Objectives of the Study                                                       5

 

CHAPTER 2: LITERATURE REVIEW                                    6

2.1       An Overview of Enzymes                                                                  6

2.2       Protease Enzymes                                                                               7

2.3       Sources of Protease                                                                             9

2.3.1    Animal proteases                                                                                 9

2.3.2    Plant proteases                                                                                    10

2.3.3    Microbial proteases                                                                             10

2.4       Classification of Microbial Proteases                                                  13

2.4.1    Glutamic acid proteases                                                                      15

2.4. 2    Serine proteases                                                                                 15

2.4.3    Cysteine proteases                                                                              15

2.4.4.   Aspartase proteases                                                                             16

2.4.5   Threonine proteases                                                                             16

2.4.6    Metalloproteases                                                                                 16

2.5       Bacillus Subtilis                                                                                   17

2.6       Utilization of African Oil Bean (Ugba) as Substrate for

Enzyme Production                                                                            19

2.7       Protease Production                                                                            19

2.8       Process Optimization                                                                          21

2.8.1    Optimization of protease parameters                                                  21

2.8.2    Optimization of physical parameters                                                  22

2.9       Purification and Characterization of Protease                                                23

2.10     Commercial Application of Protease Enzymes                                   24

2.10.1  Detergent additives                                                                            26

2.10.2  Proteases in leather industry                                                              28

2.10.3 Processing of keratin wastes                                                               29

2.10.4 Fibrinolytic proteases as thrombolytic agents                                     30

2.10.5  Proteases for biofilm removal                                                             31

2.10.6  Proteases for silk degumming                                                             33

2.10.7 Proteases in photographic industry                                                     35

2.10.8  Proteases in food industry                                                                  37

2.10.9  Proteases for contact lens cleansing                                                    38

2.10.10   Proteases for bio polishing of wool                                                 38

 

CHAPTER 3: MATERIALS AND METHODS                                           40

3.1       Materials                                                                                             40

3.1.1    Collection of materials                                                                        40

3.1. 2   Instrumentation and apparatus                                                           40

3.1.3    Chemicals and reagents                                                                      40

3.2       Methods                                                                                              41

3.2.1    Sterilization                                                                                         41

3.2.2    Media preparation                                                                               41

3.2.3    Sample preparation and inoculation                                                    41

3.2.4    Purification and storage of cultures                                                    42

3.2.5    Identification and characterization of proteolytic bacteria                 42

3.2.6    Screening for alkaline protease enzyme from bacterial isolates          48

3.2.7    Molecular characterization and identification of isolates                   49

3.2.8    Quantitative estimation of protease                                                    51

3.2.9    Enzyme purification                                                                            51

3.2.10  Ninhydrin test to detect hydrolysis of casein by enzyme     

alkaline protease                                                                                  53

3.2.11  Estimation of alkaline protease activity                                             54

3.2.12  Quantitative protein assay                                                                  56

3.2.13  Enzyme specific activity                                                                     58

3.2.14  Optimization of growth and physical parameters for

enzyme production                                                                             58

3.2.15  Enzyme immobilization                                                                      60

3.2.16  Detergent compatibility and alkaline protease activity                      

using immobilized enzyme                                                                  60

3.2.17  Efficacy of alkaline protease enzyme in stain removal                      61

3.2.18  Statistical analysis                                                                               61


CHAPTER 4: RESULTS AND DISCUSSION           63

4.1       Results                                                                                                63

4.1.1    Morphological and biochemical properties of isolates                        63

4.1.2    Screening and identification of protease producing organisms          65

4.1.3    Genotypic characterization of isolate                                                 68

4.1.4    Crude enzyme activity and purification                                             71

4.1.5    Optimization of physiological and nutritional parameters

on protease production                                                                       73

4.1.6    Compatibility of alkaline protease and detergents with their

protease activity                                                                                  83

4.1.7    Efficacy of enzyme on biological stain removal                                 85

4.2       Discussion                                                                                           87

 

CHAPTER 5: CONCLUSION AND RECOMMENDATIONS                 92

5.1       Conclusion                                                                                          92

5.2       Recommendations                                                                              92

References                                                                                                      93

Appendices                                                                                                     104

                                                                                                                       

 

 

 

 

 

 

LIST OF TABLES

                                                                                                                                    Page

2.1.      Microorganisms having protease activity                                                        12

2.2.      Protease general classification with enzyme code and specific

mechanism of action for each sub group                                                        14

4.1.      Phenotypic characterization of isolates                                                           64

4.2.      Purification steps of protease enzyme from Bacillus subtilis                          72

4.3.      Protease production at different pH values                                                    76

4.4.      Effect of divalent metal ions on protease production                                     78

 

 

  

 

 

LIST OF FIGURES

                                                                                                                                    Page

2.1       A representation of general industrial application of protease enzyme          25

2.2       Steps involved in biofilm formation                                                               32

2.3       Structure of silk fiber and degumming of silk.                                               34

2.4       Gelatin hydrolysis for release of silver for x-ray film                                     36

3.1       Tyrosine standard curve                                                                                  57

4.1       Representation of clearance zone for gelatin hydrolysis of the isolate           66

4.2       Representation of the zone of casein hydrolysis shown by test organism      67

4.3       Phylogenetic tree showing the evolutionary distance of the

bacterial isolates                                                                                              69

4.4       Agarose gel electrophoresis of the 16SrRNA gene selected

bacterial isolates                                                                                              70

4.5       Temperature effect on protease production                                                    74

4.6       Effect of carbon agro-residues on protease production                                  80

4.7       Effect of nitrogen agro-residues on protease production                               82

4.8       Detergent and alkaline protease compatibility and their protease activity    84

4.9       Wash test and efficacy of alkaline protease on stain removal                       86

 



 

 

CHAPTER 1

INTRODUCTION


             1.1              BACKGROUND OF THE STUDY

Advances in industries, agriculture, and biotechnological domains have recently driven the quest for microorganisms with innovative features that can be used to boost scientific and industrial output. Due to a number of factors, such as substrate selectivity and high catalytic activity, metabolic products such as enzymes generated by these microorganisms have a significant advantage over conventional chemical catalysts (Rai and Mukherjee, 2011). Proteases, lipases, and amylases, among other enzymes produced by these microbes, are widely used in medical, molecular, environmental biotechnology, and agricultural applications (Reddy et al., 2008).

Microbial proteases, which have a wide range of applications in bio-industries such as food, pharmaceuticals, textiles, photography, leather, and detergents, currently dominate the global enzyme industry (Singh and Bajaj, 2017). However, for successful industrial use, proteases must be robust enough to withstand the adverse process conditions. Proteases used in biotechnological processes must be resilient and capable of kinetic and structural adjustments in harsh industrial microenvironments, such as high temperatures, low pH, and the presence of inhibitors (Singh et al., 2014).

Bacillus spp. proteases have a specific significance among microbial proteases since they are renowned for their ability to create strong enzymes that may be suitable for industrial process conditions. Enzyme-based solutions promise effective raw material use, minimum or no waste formation, and avoid the use of harmful chemicals (Singh and Bajaj, 2017b). Enzymes are the basic molecules that govern a variety of metabolic processes in living systems, and they are essential for life to exist.

Proteases are one of the most important classes of industrial enzymes that have received a lot of attention in recent years (Sarouk et al., 2012). Proteases (EC 3.4) are a type of enzyme found in all living things that perform a wide range of complex physiological and metabolic tasks (Theron and Divol, 2014). These proteases could come from microbial sources, particularly extremophiles (microbes that live in severe biological niches) (Ali et al., 2016).

Bacillus spp. strains are used to make industrial enzymes and have grown in importance, accounting for 35% of total microbial enzyme sales (Jayakumar et al., 2012). This is due to Bacillus spp capacity to create enzymes that are well suited to industrial process settings (Rehman et al., 2017). Bacillus spp. enzymes are considered poly-extremotolerance, meaning they can function in a wide range of process conditions, including extremes in temperature, pH, the presence of solvents, detergents, and other potential enzyme inhibitors (Joshi and Satyanarayana, 2013).

For biotechnological operations involving protein production, numerous species of Bacillus, viz. Bacillus subtilis, Bacillus amyloliquefaciens and Bacillus licheniformis and others, have become the most popular due to their superior fermentation capabilities, high product yields and the complete lack of harmful by-products (Guleria et al., 2016).


            1.2              STATEMENT OF THE PROBLEM

Enzymes are obtained commercially from any biological source, including animals, plants, and microorganisms. These naturally occurring enzymes are frequently not easily available in sufficient numbers for commercial application, but the number of proteins generated via recombinant methods is rising at an exponential rate. The cost of manufacture, purification, yield, and stability to particular environmental conditions, which has notably influenced high quantity yield of proteases, are the key impediments to proteolytic application for industrial enzymes. In particular, there is an urgent need for the development of microbial strains from various sources capable of producing more protease enzymes at a more thermostable and moderate pH activity in industrial production. Given the wide range of applications for proteases, discovering incipient sources for protease production has piqued the interest of numerous scientific communities. Identifying substrates and optimizing their nutritional content for the generation of more proteolytic enzyme-producing microorganisms with a broad spectrum of activity has thus been a major issue in the manufacturing industry. The choice of substrate is a critical aspect in the production process. The most crucial factor to consider is that the substrate should be inexpensive and stimulating in nature, allowing the enzyme production to increase and the cost to drop. Solid state fermentation (SSF) is preferred over submerged fermentation because it offers various benefits, including highly concentrated products, the use of low-cost substrates, semi-sterile conditions, simplified downstream processing, and less pollution. The effect of agro-residue particle size and moisture content (humidity) on alkaline protease synthesis is significant. As a result, there has been a need to broaden the search for microorganisms with the potential and needed characteristics for protease synthesis.

            

            1.3              JUSTIFICATION OF THE STUDY

The use of protease enzyme in the manufacturing industry has skyrocketed in recent years. On account of their technological and economic contributions to many industrial production domains, these enzymes are currently considered important. These advantages and contributions can be realized by maximizing diverse substrates for production, such as low-cost agricultural residues, which are considered waste products. Ugba is a readily available substrate and a successful usage of enzyme from ugba fermentation isolates will create a new channel for ugba's utility value to be boosted in this regard. The cost of production in relation to the value of the end product is the most important issue when isolating enzymes on an industrial scale for commercial use. Alkaline proteases are commonly used in commercial applications as crude preparations. Nonetheless, alkaline protease purification is critical for gaining a better knowledge of the enzyme's action. Environmentally friendly approaches to the synthesis of fine chemicals have gotten a lot of attention in recent years, therefore the usage of agricultural waste for the production of various enzymes has skyrocketed. Various industries have concentrated on using agro-residues as the only source of carbon and nitrogen in large-scale fermentation medium. In terms of medium ingredients, these leftovers are readily available in big quantities at low cost and with minimal capital expenditure.  Enzyme production is based on the waste to energy principle, thus, the use of agro-waste for the manufacture of commercially essential compounds does not disrupt the food chain and reduces reliance on non-renewable resources. Screening methods are being used to quickly discover enzymes with potential industrial applications. Protease enzymes are intended to fill the gap between chemical and biological processes as a result of their peculiar features, and they have been widely used in industrial operations. The ability to recognize and optimize the spatial and temporal variation of microorganisms expressing different enzymes, as well as the factors militating their activities, is critical. This has necessitated the use of Bacillus subtilis as potential microorganism in production of protease despite the fact that it is pathogenic nature yet it has found its potential use in industrial production.

 

1.4       AIM AND OBJECTIVES OF THE STUDY

The aim of the research is to screen, characterize and optimize protease enzyme isolated from Bacillus subtilis. Specific objectives of the study include;

            i.                    Isolation, screening and identification of proteolytic Bacillus subtilis from traditionally fermented ugba for synthesis of protease enzyme.

             ii.                  Purification and characterization of alkaline protease.

          iii.                Optimization of physicochemical and nutritional parameters for maximum production of protease.

            iv.                Detergent compatibility and efficiency of alkaline protease in protenious stain removal: an empirical study.

 

 

Click “DOWNLOAD NOW” below to get the complete Projects

FOR QUICK HELP CHAT WITH US NOW!

+(234) 0814 780 1594

Buyers has the right to create dispute within seven (7) days of purchase for 100% refund request when you experience issue with the file received. 

Dispute can only be created when you receive a corrupt file, a wrong file or irregularities in the table of contents and content of the file you received. 

ProjectShelve.com shall either provide the appropriate file within 48hrs or send refund excluding your bank transaction charges. Term and Conditions are applied.

Buyers are expected to confirm that the material you are paying for is available on our website ProjectShelve.com and you have selected the right material, you have also gone through the preliminary pages and it interests you before payment. DO NOT MAKE BANK PAYMENT IF YOUR TOPIC IS NOT ON THE WEBSITE.

In case of payment for a material not available on ProjectShelve.com, the management of ProjectShelve.com has the right to keep your money until you send a topic that is available on our website within 48 hours.

You cannot change topic after receiving material of the topic you ordered and paid for.

Ratings & Reviews

0.0

No Review Found.


To Review


To Comment