Food Biochemistry and Food Processing (2 edition)

(Wang) #1

BLBS102-c10 BLBS102-Simpson March 21, 2012 13:7 Trim: 276mm X 219mm Printer Name: Yet to Come


218 Part 2: Biotechnology and Enzymology

Cross-linking using chemical reagents remains challenging,
both in terms of controlling the chemistry and gaining con-
sumer acceptance. However, as the extensive recent use of trans-
glutaminase dramatically illustrates, protein cross-linking using
enzymes has huge potential for the improvement of traditional
products and the creation of new ones. Transglutaminase itself
will no doubt find yet more application as its precise mode of
action becomes better understood, especially if variants of the
enzyme are found with a broader substrate specificity.
Whether other enzymes, which cross-link by different mech-
anisms, can find equal applicability remains open to debate. The
thiol exchange enzymes, such as PDI, may offer advantages
to food processors if their mechanisms can be unravelled, and
then controlled within a foodstuff. Other enzymes, such as lysyl
oxidase, have not yet been used, but have potential to improve
foods (Dickinson 1997), especially in the light of recent work
characterising this class of enzymes (Buffoni and Ignesti 2000),
which may allow their currently unpredictable effects to be
better understood.

ACKNOWLEDGEMENTS


We thank all the postgraduates and postdoctoral fellows who
have worked with us on the Maillard reaction and protein cross-
linking of food, in particular Dr Sian Fayle, Paula Brown,ˆ
Dr Indira Rasiah, Dr Susie Meade, Dr Antonia Miller and
Dr Suhaimi Yasir.

REFERENCES


Aalami M, Leelavathi K. 2008. Effect of microbial transglutaminase
on spaghetti quality.J Food Sci73: C306–C312.
Ahmed N. 2005. Advanced glycation endproducts – role in pathol-
ogy of diabetic complications.Diabetes Res Clin Pract67: 3–21.
Al-Abed Y, Bucala R. 2000. Structure of a synthetic glucose de-
rived advanced glycation end product that is immunologically
cross-reactive with its naturally occurring counterparts.Biocon-
jug Chem11: 39–45.
Ames JM. 1992. The Maillard reaction in foods. In: BJF Hudson
(ed.)Biochemistry of Food Proteins.Elsevier Applied Science,
London, pp. 99–153.
Ames JM. 2007. Evidence against dietary advanced glycation end-
products being a risk to human health.Mol Nutr Food Res51:
1085–1090.
Ames JM. 2009. Dietary Maillard reaction products: implication for
human health and disease.Czech J Food Sci27( SI): S66–S68.
An HJ et al. 1996. Roles of endogeneous enzymes in surimi gelation.
Trends Food Sci Technol7: 321–327.
Ando H et al. 1989. Purification and characteristics of a novel trans-
glutaminase derived from microorganisms.Agric Biol Chem53:
2613–2617.
Aoki T et al. 1999. Improvement of heat stability and emulsify-
ing activity of ovalbumin by conjugation with glucuronic acid
through the Maillard reaction.Food Res Intern32: 129–133.
Aoki T et al. 2001. Modification of ovalbumin with oligogalactur-
onic acids through the Maillard reaction.Food Res Intern34:
127–132.

Benjakul S et al. 2004a. Cross-linking activity of sarcoplasmic frac-
tion from bigeye snapper (Priacanthus tayenus) muscle.Food Sci
Technol37: 79–85.
Benjakul S et al. 2004b. Effect of porcine plasma protein and setting
on gel properties of surimi produced from fish caught in Thailand.
Food Sci Technol37: 177–185.
Bergmann R et al. 2001. Radio fluorination and positron emis-
sion tomography (PET) as a new approach to study the in
vivo distribution and elimination of the advanced glycation end-
productsN-epsilon-carboxymethyllysine (CML) andN-epsilon-
carboxyethyllysine (CEL).Nahrung45: 182–188.
Biemel KM et al. 2001. Identification and quantitative evaluation
of the lysine-arginine crosslinks GODIC, MODIC, DODIC, and
glucosepan in foods.Nahrung45: 210–214.
Biemel KM et al. 2002. Identification and quantification of major
Maillard-crosslinks in human serum albumin and lens protein: ev-
idence for glucosepane as the dominant compound.J Biol Chem
277: 24907–24915.
Bordas M et al. 2004. Formation and stability of heterocycloc
amines in a meat flavour model system – Effect of temperature,
time and precursors.J Chromatogr B802: 11–17.
Bouhallab S et al. 1999. Formation of stable covalent dimer explains
the high solubility at pH 4.6 of lactose-β-lactoglobulin conjugates
heated near neutral pH.J Agric Food Chem47: 1489–1494.
Brady JD, Robins SP. 2001. Structural characterization of pyrrolic
cross-links in collagen using a biotinylated Ehrlich’s reagent.J
Biol Chem276: 18812–18818.
Brands CMJ et al. 2002. Quantification of melanoidin concentration
in sugar-casein systems.J Agric Food Chem50: 1178–1183.
Brinkmann-Frye E et al. 1998. Role of the Maillard reaction in aging
of tissue proteins.J Biol Chem273: 18714–18719.
Buffoni F, Ignesti G. 2000. The copper-containing amine oxidases:
biochemical aspects and functional role.Mol Genet Metab71:
559–564.
Cabrera-Chavez F et al. 2008. Transglutaminase treatment of wheat
and maize prolamins of bread increases the serum IgA reactivity
of celiac disease patients.J Agric Food Chem56: 1387–1391.
Caillard R et al. 2008. Characterization of amino cross-linked soy
protein hydrogels.J Food Chem73: C283–C291.
Caillard R et al. 2009. Physiochemical properties and microstruc-
ture of soy protein hydrogels co-induced by Maillard-type cross-
linking and salts.Food Res Int42: 90–106.
Chellan P, Nagaraj RH. 2001. Early glycation products produce
pentosidine cross-links on native proteins: novel mechanism of
pentosidine formation and propagation of glycation.J Biol Chem
276: 3895–3903.
Chen HH. 2000. Effect of non muscle protein on the thermogelation
of horse mackerel surimi and the resultant cooking tolerance of
kamaboko.Fish Sci66: 783–788.
Chevalier F et al. 2001. Improvement of functional properties of
β-lactoglobulin glycated through the Maillard reaction is related
to the nature of the sugar.Int Dairy J11: 145–152.
Chevalier F et al. 2002. Maillard glycation ofβ-lactoglobulin in-
duces conformation changes.Nahrung46: 58–63.
Cho RK et al. 1984. Chemical properties and polymerizing ability
of the lysozyme monomer isolated after storage with glucose.
Agric Biol Chem48: 3081–3089.
Cho RK et al. 1986a. Polymerization of acetylated lysozyme and
impairment of their amino acid residues due toα-dicarbonyl
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