Page 250 - Advances in Textile Biotechnology

Functionalisation of wool and silk fi bres using enzymes 231

structure of pork meat, LWT – Food Sci Technol, 39, 1117–1124. doi: 10.1016/j.
lwt.2005.07.008.
lantto r, puolanne e, kalkkinen n, buchert j and autio k (2005a), Enzyme-aided

modification of chicken-breast myofibril proteins: effect of laccase and transglu-
taminase on gelation and thermal stability, J Agric Food Chem, 53, 9231–9237. doi:
10.1021/jf051602a.
lantto r, schoenberg c, buchert j and heine e (2004), Effects of laccase-mediator
combinations on wool, Text Res J, 74, 713–717. doi: 10.1177/004051750407400809.
lantto r, puolanne e, katina k, niemistö m, buchert j and autio k (2007a), Effect
of laccase and transglutaminase on the textural and water-binding properties of
cooked chicken breast meat gels, Eur Food Res Technol, 225, 75–83. doi: 10.1007/
s00217-006-0384-z.
lantto r, puolanne e, kruus k, buchert j and autio k (2007b), Tyrosinase-aided
protein cross-linking: effects on gel formation of chicken breast myofi brils and
texture and water-holding of chicken breast meat homogenate gels, J Agric Food
Chem, 55, 1248–1255. doi: 10.1021/jf0623485.
lee sg, hong sp and sung mh (1999), Development of an enzymatic system for the
production of dopamine from catechol, pyruvate and ammonia, Enzyme Microb
Technol, 25, 298–302. doi: 10.1016/S0141-0229(99)00071-X.
lewandowski at, small da, chen t, payne gf and bentley we (2006), Tyrosine-
based activatable Pro-Tag: enzyme-catalyzed protein capture and release, Bio-
technol Bioeng, 93, 1207–1215. doi: 10.1002/bit.20840.
lewandowski at, yi h, luo x, payne gf, ghodssi r, rubloff gw and bentley we
(2008), Protein assembly onto microfabricated devices through enzymatic activa-
tion of fusion Pro-Tag, Biotechnol Bioeng, 99, 499–507. doi: 10.1002/bit.21580.
lindley h (1977), The chemical composition and structure of wool, in: Chemistry of
natural protein fi bres, Asquith RS Ed., Plenum Press, New York and London,
147–191.
lorand l and graham rm (2003), Transglutaminases: crosslinking enzymes with
pleiotropic functions, Nat Rev Mol Cell Biol, 4, 140–156. doi: 10.1038/nrm1014.
maclaren ja and milligan b (1981), The structure and composition of wool, in: Wool
science. The chemical reactivity of the wool fi bre, Science Press, Marrikville,
Australia, 1–16.
martin lb, nikodinovic j, mcmahon am, vijgenboom e and o’connor ke (2008),
Assessing the catalytic activity of three different sources of tyrosinases: a study
of the oxidation of mono- and difl uorinated monophenols, Enzyme Microb
Technol, 43, 297–301. doi: 10.1016/j.enzmictec.2008.03.010.
mattinen m-l, lantto r, selinheimo e, kruus k and buchert j (2008), Oxidation of
peptides and proteins by Trichoderma reesei and Agaricus bisporus tyrosinases, J
Biotechnol, 133, 395–402. doi: 10.1016/j.jbiotec.2007.10.009.
mero a, spolaore b, veronese f and fontana a (2009), Transglutaminase-mediated

PEGylation of proteins: direct identification of the sites of protein modifi cation
by mass spectrometry using a novel monodisperse PEG, Bioconjug Chem, 20,
384–389. doi: 10.1021/bc800427n.
michon t, chenu m, kellershon n, desmadril m and guéguen j (1997), Horseradish
peroxidase oxidation of tyrosine-containing peptides and their subsequent poly-
merisation: a kinetic study, Biochemistry, 36, 8504–8513. doi: 10.1021/bi963168z.
munteanu f-d, basto c, guebitz gm and cavaco-paulo a (2007), Staining of wool
using the reaction products of ABTS oxidation by laccase: synergetic effects of

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