Proteolysis in sourdough fermentations: mechanisms and potential for improved bread quality

被引:263
作者
Gaenzle, Michael G. [1 ]
Loponen, Jussi [1 ,2 ]
Gobbetti, Marco [3 ]
机构
[1] Univ Alberta, Dept Agr Food & Nutr Sci, Edmonton, AB T6G 2P5, Canada
[2] Univ Helsinki, Dept Food Technol, Helsinki, Finland
[3] Univ Bari, Dept Plant Protect & Appl Microbiol, Bari, Italy
关键词
D O I
10.1016/j.tifs.2008.04.002
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The degradation of the cereal proteins in wheat and rye sourdough fermentations strongly affects the quality of bread. Acidification and the reduction of disulfide bonds of gluten by heterofermentative lactobacilli increase the activity of cereal proteases and substrate accessibility; amino acids are accumulated by strain-specific intracellular peptidases of lactobacilli. Germinated cereals or other proteases enable an extensive degradation of proteins in sourdoughs in fermentation protocols that may be used to develop new products for individuals with gluten intolerance. The increased knowledge on proteolysis in sourdoughs enables a directed optimization of fermentation to improve bread quality.
引用
收藏
页码:513 / 521
页数:9
相关论文
共 74 条
[1]  
[Anonymous], [No title captured]
[2]   The intestinal T cell response to α-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase [J].
Arentz-Hansen, H ;
Körner, R ;
Molberg, O ;
Quarsten, H ;
Vader, W ;
Kooy, YMC ;
Lundin, KEA ;
Koning, F ;
Roepstorff, P ;
Sollid, LM ;
McAdam, SN .
JOURNAL OF EXPERIMENTAL MEDICINE, 2000, 191 (04) :603-612
[3]   IDENTIFICATION OF A GROWTH STIMULANT FOR LACTOBACILLUS-SANFRANCISCO [J].
BERG, RW ;
SANDINE, WE ;
ANDERSON, AW .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1981, 42 (05) :786-788
[4]   Thiocalsin: A thioredoxin-linked, substrate-specific protease dependent on calcium [J].
Besse, I ;
Wong, JH ;
Kobrehel, K ;
Buchanan, BB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (08) :3169-3175
[5]   Heterologous expression, purification, refolding, and structural-functional characterization of EP-B2, a self-activating barley cysteine endoprotease [J].
Bethune, Michael T. ;
Strop, Pavel ;
Tang, Yinyan ;
Sollid, Ludvig M. ;
Khosla, Chaitan .
CHEMISTRY & BIOLOGY, 2006, 13 (06) :637-647
[6]   A second aspartic proteinase associated with wheat gluten [J].
Bleukx, W ;
Delcour, JA .
JOURNAL OF CEREAL SCIENCE, 2000, 32 (01) :31-42
[7]   Specificity of a wheat gluten aspartic proteinase [J].
Bleukx, W ;
Brijs, K ;
Torrekens, S ;
Van Leuven, F ;
Delcour, JA .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1998, 1387 (1-2) :317-324
[8]   Major proteinase hydrolysing gliadin during wheat germination [J].
Bottari, A ;
Capocchi, A ;
Fontanini, D ;
Galleschi, L .
PHYTOCHEMISTRY, 1996, 43 (01) :39-44
[9]   Proteolytic activities in dormant rye (Secale cereale L.) grain [J].
Brijs, K ;
Bleukx, W ;
Delcour, JA .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1999, 47 (09) :3572-3578
[10]   Degradation of gluten by proteases from dry and germinating wheat (Triticum durum) seeds:: An in vitro approach to storage protein mobilization [J].
Capocchi, A ;
Cinollo, M ;
Galleschi, L ;
Saviozzi, F ;
Calucci, L ;
Pinzino, C ;
Zandomeneghi, M .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2000, 48 (12) :6271-6279