2009_Book_FoodChemistry

1052 Index
–, isoionic point 059, 059(F)
–, legume 746, 748(T)
–, maleylation 066
–, microbial 008
–, microparticulated 463
–, modification 064, 079, 080(T)
–, molecular weight 056(T)
–, –, determination 041
–, muscle 571(T)
–, N,O-acyl migration 043, 044
–, N-terminus, determination 042
–, net charge 059
–, optical activity 060
–, optical rotatory dispersion (ORD) 060, 060(F)
–, overlapping cleavage 045(F)
–, oxidation with peroxidase/H 2 O 2 087
–, oxidative change 072
–, partial hydrolysis, chemical 043
–, –, enzymatic 043
–, phenylalanine free 086, 087(T)
–, photometric determination 016, 020
–, pK value of the side chain 059(T)
–, pleated-sheet structure 050, 050(T), 051(F)
–, primary structure 040
–, quaternary structure 056, 056(T)
–, reaction 064
–, reaction in food processing 070
–, reaction with aldehyde 214, 214(F)
–, reaction with amino acid ester 067
–, reaction with bifunctional reagent 070
–, reaction with diazoacetamide 067
–, reaction with malondialdehyde 214
–, reaction with monohydroperoxide 212, 213
–, reaction with pyridoxal phosphate 065
–, reductive alkylation 080(T)
–, reductive methylation 083(F)
–, regular structure element 049, 050(T)
–, –, frequency of amino acid 054(T)
–, rye flour 709(T)
–, S-sulfo derivative 067
–, salting-in effect 061
–, salting-out effect 061
–, secondary structure 049
–, selective cleavage at cysteine residue 067
–, selective cleavage at methionine residue 043, 044
–, sequence analysis 021, 041, 044
–, sequence analysis via nucleotide sequence 046
–, sheet, β - 050, 050(T), 051(F)
–, single cell 008
–, solubility 060, 061(F), 085, 086(F)
–, –, fish 634(T)
–, –, frozen fish 633(F)
–, source 008
–, spinning 088
–, structural domain 055, 055, 056(F)
–, structure, β -
–, –, frequenzy of amino acid 054(T)
–, subunit 041
–, succinylation 065, 081, 081(F)
–, super-secondary structure 052, 053(F)
–, surface denaturation 062, 063
–, sweet 436
–, swelling 061
–, technological property 080(T)
–, temperature of phase transition 006, 006(T)
–, terminal group 042
–, tertiary structure 053, 056(F)
–, texturization 088
–, texturized 087
–, titration curve 060(F)
–, total charge 059
–, turn, β -
–, –, frequenzy of amino acid 054(T)
–, turn, β -, 052, 052(T), 053(F)
–, tyrosine cross-linking with peroxidase/H 2 O 2 086
–, vegetable 770, 780(F)
–, water binding capacity 061
–, wheat, hydration 727, 728(F)
–, wheat flour 709(T)
–, X-ray analysis 048
Protein concentrate 008
–, fish 636
Protein content, type of bread 735(T)
Protein cross-link, fish 626
Protein denaturation, activation energy 132
Protein efficiency ratio 030
Protein film, dough 727, 728(F)
–, stability 062
Protein foam 062
Protein gel 062
Protein hydrolysate 602, 602(F)
–, debitterizing 085, 086(T)
–, production 602(F)
Protein hydrolysis, loss 023
Protein isolate 008
Protein modification, Maillard reaction 285, 285
Protein nature, enzyme 095
Protein radical, formation 214, 214
Protein strand, dough 729, 729(F)
Proteinase 074, 077(T)
–, active serine, detection 108
–, application in meat ripening 150
–, flour improvement 720, 720(F)
–, industrial application 150
–, industrial preparation 150, 151(T)
–, pH optimum 151(T)
–, stability, pH range 151(T)
–, wheat 696
Proteinase (see also endopeptidase)
Proteinase inhibitor 055, 055(F), 075
–, active center 756(T)
–, amount, legume 754