Enzymes Beyond Traditional Applications in Dairy Science and Technology 9780323960106, 0323960103

Table of contents :
Cover
Front-matter
Copyright
List of contributors
Contents
1 Milk enzymes
1.1 Introduction
1.2 Enzymes in milk: significance, nomenclature, reaction catalyzed, and activity levels
1.3 Proteinases
1.3.1 Plasmin
1.3.2 Cathepsin D
1.4 Lipases and esterases
1.4.1 Lipase
1.4.2 Lipoprotein lipase (EC 3.1.1.34)
1.4.3 Bile salt–stimulated lipase
1.4.4 Esterases
1.5 Phosphohydrolases
1.5.1 Alkaline phosphatase
1.5.2 Acid phosphatase
1.5.3 Ribonuclease
1.6 Oxidases
1.6.1 Lactoperoxidase (EC 1.11.1.7)
1.6.2 Catalase (EC 1.11.1.6)
1.6.3 Xanthine oxidase (EC 1.17.3.2)
1.6.4 Superoxide dismutase
1.6.5 Sulfhydryl oxidase (EC 1.8.3--)
1.7 γ-glutamyl transpeptidase (EC 2.3.2.2)
1.8 N-Acetyl-β-d-glucosaminidase (EC 3.2.1.30)
1.9 Lysozyme (EC 3.1.2.17)
1.10 Enzymes from psychrotrophs origin in milk
1.11 Conclusion
References
2 Enzymes in mastitis milk
2.1 Introduction
2.2 Enzymes in mastitis
2.2.1 Proteases
2.2.1.1 Plasminogen and plasmin
2.2.1.2 Elastase, collagenase, and cathepsin
2.2.1.3 Caspases
2.2.2 Esterases
2.2.3 Antioxidant enzymes
2.2.3.1 Glutathione peroxidase (GSH-Px)
2.2.3.2 Catalase
2.2.3.3 Superoxide dismutase (SOD)
2.2.3.4 Xanthine oxidase
2.2.4 Antibacterial enzymes [lactoperoxidase (LPO) and myeloperoxidase (MPO)]
2.2.5 N-acetyl-d-glucosaminidase (NAGase)
2.2.6 Lactate dehydrogenase (LDH)
2.2.7 Phosphatases and aminotransferases
2.3 Efforts in diagnosing mastitis in dairy animals
2.4 Future developments and conclusion
Acknowledgments
References
3 Effect of high-pressure processing on milk enzymes
3.1 Introduction
3.2 Significance of milk enzymes
3.3 Need for alternate processing of milk
3.4 High-pressure processing technology
3.5 Effect of high pressure on the activity and structure of milk enzymes
3.6 Kinetics of high pressure on milk enzyme inactivation
3.7 Effect of high-pressure processing on milk enzyme system
3.7.1 Effect of high-pressure processing on alkaline phosphatase
3.7.2 Effect of high-pressure processing on plasmin
3.7.3 Effect of high–pressure processing on lipoprotein lipase, γ-glutamyltransferase, and lactoperoxidase
3.8 Milk enzymes as high–pressure processing indicator
3.9 Conclusion
References
4 Traditional applications of enzymes in dairy science and technology
4.1 Introduction
4.2 Alkaline phosphatase
4.2.1 Significance of alkaline phosphatase
4.2.2 Methods for estimation of alkaline phosphatase activity
4.2.2.1 Colorimetric methods
4.2.2.2 Fluorimetric methods
4.2.2.3 Immunochemical methods
4.2.2.4 AOAC method for cheese
4.2.3 Effect of mastitis
4.2.4 Alkaline phosphatase activity in nonbovine milk
4.2.5 Reactivation of alkaline phosphatase
4.3 Acid phosphatase
4.4 Milk lipoprotein lipase
4.4.1 Physicochemical characteristics
4.4.2 Concentration in bovine milk
4.4.3 Lipolysis
4.4.4 Significance in dairy industry
4.5 Plasmin
4.5.1 Inactivation of plasmin
4.5.2 Significance of plasmin in milk
4.5.3 Ultrahigh temperature milk
4.5.4 Cheese
4.5.5 Milk protein products
4.5.6 Milk powder products
4.6 Catalase
4.6.1 Physicochemical properties
4.6.2 Catalase activity in milk
4.6.3 Measurement of catalase activity
4.6.4 Significance in dairy industry
4.7 Lactoperoxidase
4.7.1 Physicochemical properties
4.7.2 Concentration in milk and colostrum
4.7.3 Significance of lactoperoxidase enzyme
4.7.4 Lactoperoxidase system in milk
4.8 Xanthine oxidoreductase
4.9 γ-Glutamyl transferase
4.9.1 Physicochemical properties
4.9.2 Significance in dairy industry
4.10 Conclusion
References
5 Methods for identification of bioactive peptides
5.1 Introduction
5.2 Methods of protein digestion
5.2.1 In vitro methods
5.2.1.1 Enzymatic method
5.2.1.2 Microbial method
5.2.2 In vivo methods
5.2.2.1 Aspiration of gut content
5.2.2.2 Measurement in the blood
5.2.2.3 Identification/characterization in the blood
5.3 Methods of isolation and identification/characterization of food-derived peptides
5.4 Methods of function assessment
5.4.1 Function assessment using in vitro methods
5.4.2 Function assessment using in vivo methods
5.5 The importance of quantifying bioactive peptides
5.6 Conclusion
References
6 In-silico methods for milk-derived bioactive peptide prediction
6.1 Introduction
6.2 Methods of milk-derived bioactive peptide prediction
6.2.1 Obtaining the amino acid sequence of milk proteins
6.2.2 In-silico digestion of milk proteins
6.2.3 Molecular docking simulation
6.3 In vitro confirmatory experiments after in silico prediction
6.4 Estimation of bioactive peptide content in food items using in-silico methods
6.5 Conclusion and future perspective
References
7 Production of bioactive peptides from bovine caseins
7.1 Introduction
7.2 Production of bioactive peptides from bovine casein
7.2.1 Hydrolysis by enzymes from plant or microorganism
7.2.2 Degradation by digestive enzymes
7.2.3 Proteolysis during fermentation
7.3 Bioactivities of bovine casein peptides
7.3.1 Antihypertensive activity
7.3.2 Antidiabetic activity
7.3.3 Antioxidant activity
7.3.4 Other bioactivities
7.4 Conclusion and further perspectives
References
8 Production of bioactive peptides from bovine whey proteins
8.1 Introduction
8.2 Generation of whey protein–derived bioactive peptides
8.2.1 Enzymatic hydrolysis
8.2.2 Hydrolysis during gastrointestinal digestion
8.2.3 Fermentation
8.2.4 In silico aided enzymatic release of bioactive peptides
8.3 Analytical techniques for the identification of bioactive peptides
8.3.1 Enrichment and fractionation of bioactive peptides
8.3.2 Peptide characterization
8.4 Biological effects of whey-derived bioactive peptides
8.4.1 Antidiabetic peptides
8.4.2 Antihypertensive peptides
8.4.3 Antimicrobial peptides
8.4.4 Antioxidant peptides
8.4.5 Anticancer peptides
8.4.6 Immunomodulatory peptides
8.4.7 Antiinflammatory peptides
8.4.8 Opioid-like peptides
8.4.9 Satiety hormone-inducing peptides
8.5 Conclusion and future prospects
Acknowledgments
References
9 Bioactive peptides derived from camel milk proteins
9.1 Introduction
9.2 Bioactive peptides from camel milk proteins
9.2.1 Antioxidant
9.2.1.1 Structural activity relationship of camel milk–derived antioxidant peptides
9.2.2 Antihypertensive
9.2.2.1 Structural activity relationship (SAR) of camel milk–derived antihypertensive peptides
9.2.3 Antimicrobial peptides from camel milk
9.2.3.1 Structural activity relationship of camel milk–derived antimicrobial peptides
9.2.4 Antidiabetic peptides derived from camel milk proteins
9.2.4.1 Dipeptidyl peptidase-IV inhibitory peptides from camel milk proteins
9.2.4.2 α-Amylase (AM) inhibitory peptides from camel milk proteins
9.2.4.3 α-Glucosidase (AG) inhibitory peptides from camel milk proteins
9.2.4.4 Structural activity relationship of camel milk–derived antidiabetic peptides
9.2.5 Antiobesity peptides from camel milk proteins and their structural activity relationship
9.2.6 Other biological properties of camel milk–derived hydrolysates
9.3 Future perceptions
References
10 Bioactive peptides from fermented milk products
10.1 Introduction
10.2 Bioactive peptides from fermented bovine milk products
10.2.1 Soful
10.2.2 Yogurt
10.2.3 Koumiss
10.2.4 Kefir
10.2.5 Others
10.3 Bioactive peptides from fermented goat milk products
10.3.1 Yogurt
10.3.2 Kefir
10.3.3 Dahi
10.4 Bioactive peptides from fermented camel milk products
10.4.1 Camel milk
10.4.2 Bioactive peptides from fermented camel’s milk
10.4.3 Bioactive peptides from fermented camel milk products
10.5 Bioactive peptides from fermented mare milk products
10.5.1 Koumiss
10.6 Bioactive peptides from fermented sheep milk products
10.6.1 Koopeh
10.6.2 Yogurt
10.7 Conclusion
References
11 Downstream processing of therapeutic bioactive peptide
11.1 Introduction
11.2 Production mechanisms of bioactive peptides
11.2.1 Enzymatic hydrolysis
11.2.2 Fermentation
11.2.3 Enzymes derived from proteolytic microorganisms
11.3 Downstream processing of bioactive peptides (isolation, purification, and characterization)
11.3.1 Fractionation methods
11.3.2 Membrane separation techniques
11.3.3 Chromatographic methods
11.3.3.1 Size-exclusion chromatography
11.3.3.2 Ion-exchange chromatography
11.3.3.3 Reversed-phase liquid chromatography
11.4 Conclusion
References
12 Enzyme actions during cheese ripening and production of bioactive compounds
12.1 Introduction
12.2 Bioactive compounds
12.2.1 Peptides
12.2.2 Conjugated linoleic acid
12.2.3 Gama aminobutyric acid and L-ornithine
12.2.4 Carotenoids
12.3 Conclusion
References
13 Immobilization of β-galactosidases
13.1 Introduction
13.2 Sources of β-galactosidase
13.3 Structure of β-galactosidase
13.4 Classification of β-galactosidases
13.5 Reactions of β-galactosidase
13.6 Immobilization of β-galactosidase
13.6.1 Functional enzyme aggregates
13.6.2 Gel beads and lattices
13.6.3 Chitosan
13.6.4 Nanoparticles
13.6.5 Metal affinity columns
13.6.6 Methacrylate and its variants
13.7 Conclusion
Acknowledgments
References
14 Low-lactose milk production using β-galactosidases
14.1 Introduction
14.2 Characteristics of β-galactosidases
14.2.1 Sources of β-galactosidases
14.2.2 Reactions catalyzed by β-galactosidases
14.2.3 Optimal reaction conditions for β-galactosidases
14.2.4 Production and purification of β-galactosidases
14.2.5 Sources of industrial β-galactosidase
14.2.6 Technologies for producing low-lactose milk
14.2.7 Future scope
14.3 Immobilized β-galactosidases
14.4 Column reactors with immobilized β-galactosidases
14.5 Conclusions and perspectives
References
15 Production of oligosaccharides, a prebiotic from lactose, using β-galactosidase
15.1 Introduction
15.2 Characteristics of β-galactosidases for the production of galactooligosaccharides
15.2.1 Sources of β-galactosidases
15.2.2 Reactions catalyzed by β-galactosidases for the production of galactooligosaccharides
15.2.3 Optimal reaction conditions for the production of galactooligosaccharides
15.2.4 Production and purification of galactooligosaccharides
15.2.5 Sources of industrial β-galactosidase and galactooligosaccharides
15.2.6 Future scope
15.3 Immobilized β-galactosidase for the production of galactooligosaccharides
15.4 Conclusions and perspectives
References
16 Production of lactulose from cheese whey
16.1 Introduction
16.2 Lactulose production
16.2.1 Isomerization-based lactulose synthesis
16.2.1.1 Chemical method
16.2.1.2 Electro-activation-based isomerization
16.2.1.3 Enzyme-based isomerization
16.2.2 Transgalactosylation-based lactulose synthesis
16.3 Separation of lactulose
16.4 Health benefits of lactulose
16.5 Conclusion
References
17 Determination of lactose in milk and milk-derived ingredients using biosensor-based techniques
17.1 Introduction
17.2 Importance of lactose in milk and dairy ingredients
17.3 Lactose quantification methods
17.4 Biosensors
17.4.1 Biosensors used in dairy foods
17.4.2 Biosensors used for lactose quantification
17.5 Blood glucose meter biosensors as an option for determination of lactose
17.5.1 Blood glucose meter operating principles
17.5.2 Potential issues with a blood glucose meter–based lactose assay
17.5.3 Practical applications reported in literature for use of blood glucose meter in measurement of lactose
17.5.3.1 Measurement of lactose in milk using a blood glucose meter
17.5.3.2 Measurement of lactose in dairy ingredients using a blood glucose meter
17.6 Conclusion
References
18 Enzyme-based analytical methods pertinent to dairy industry
18.1 Introduction
18.2 Urea estimation in milk
18.2.1 Monitoring pH change
18.2.2 Monitoring change in pressure
18.2.3 Potentiometric approach
18.2.4 Spectrophotometric measurement of ammonium ion concentration
18.2.5 Urea biosensor
18.3 Lactose estimation
18.3.1 Spectrophotometric method
18.3.2 By measuring the change in pH
18.4 Estimation of lactate or lactic acid in dairy products
18.5 Estimation of cholesterol in dairy products
18.6 Ascorbic acid estimation in dairy products
18.7 Detection of common adulterants
18.7.1 Detection and estimation of hydrogen peroxide in milk
18.7.2 Detection of glucose in milk
18.7.3 Detection and estimation of sucrose in milk and milk products
18.7.4 Detection of maltodextrin in milk
18.7.5 Paper strip for urea detection
18.7.6 Detection and estimation of starch in milk and milk products
18.8 Conclusion
References
19 Lactate biosensor for assessing milk microbiological load
19.1 Introduction
19.2 Lactic acid for assessing milk microbial load
19.3 Methods of detection
19.3.1 Analytical conventional techniques
19.3.1.1 High-performance liquid chromatography
19.3.1.2 Liquid chromatography–mass spectrometry
19.3.2 Lactate biosensors
19.3.2.1 Electrochemical methods
19.3.2.2 Optical spectroscopic methods
19.3.2.2.1 UV–vis spectroscopy
19.3.2.2.2 Colorimetric
19.3.2.2.3 Fourier transform infrared spectroscopy
19.3.3 Nanotechnology applications in sensors
19.4 Conclusion and future prospective
Acknowledgment
Conflicts of interest
Ethical approval
References
20 Enzymes for cleaning-in-place in the dairy industry
20.1 Introduction: fouling and cleaning-in-place in the dairy industry
20.2 Industrial enzymes and their use for cleaning-in-place in the dairy industry
20.3 Reported studies on the effectiveness of enzymes for cleaning-in-place in the dairy industry
20.3.1 Removal of Type A fouling deposits
20.3.2 Removal of biofilms
20.4 Considerations for the development of optimal enzyme-based cleaning solutions
20.5 Conclusions and future outlook
References
21 Regulatory policies on use of food enzymes
21.1 Introduction
21.2 Regulatory framework regarding food enzymes
21.3 Specific aspects of intellectual property right protection on enzymes
21.4 Government policies toward food in biotechnology
21.4.1 Enzyme regulation in Canada
21.4.2 Enzyme regulation in Australia and New Zealand
21.4.2.1 Proposed amendments
21.4.3 European Union regulation
21.4.4 Scope of enzyme regulation
21.4.5 Limitations
21.4.6 US regulations
21.4.6.1 Petitions for enzyme preparations
21.4.6.2 Generally Recognized as Safe notices for enzyme preparations
21.4.7 FAO/WHO
21.5 Policy and regulatory framework: lower middle income countries
21.6 Future prospect
References
Index