Proteolytic systems of lactic acid bacteria

被引:509
作者
Savijoki, Kirsi
Ingmer, Hanne
Varmanen, Pekka
机构
[1] Univ Helsinki, Inst Biotechnol, FIN-00014 Helsinki, Finland
[2] Univ Helsinki, Fac Vet Med, Dept Vet Basic Sci, FIN-00014 Helsinki, Finland
[3] Royal Vet & Agr Univ, Dept Vet Pathobiol, DK-1870 Frederiksberg C, Denmark
关键词
D O I
10.1007/s00253-006-0427-1
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Lactic acid bacteria (LAB) have a very long history of use in the manufacturing processes of fermented foods and a great deal of effort was made to investigate and manipulate the role of LAB in these processes. Today, the diverse group of LAB includes species that are among the best-studied microorganisms and proteolysis is one of the particular physiological traits of LAB of which detailed knowledge was obtained. The proteolytic system involved in casein utilization provides cells with essential amino acids during growth in milk and is also of industrial importance due to its contribution to the development of the organoleptic properties of fermented milk products. For the most extensively studied LAB, Lactococcus lactis, a model for casein proteolysis, transport, peptidolysis, and regulation thereof is now established. In addition to nutrient processing, cellular proteolysis plays a critical role in polypeptide quality control and in many regulatory circuits by keeping basal levels of regulatory proteins low and removing them when they are no longer needed. As part of the industrial processes, LAB are challenged by various stress conditions that are likely to affect metabolic activities, including proteolysis. While environmental stress responses of LAB have received increasing interest in recent years, our current knowledge on stress-related proteolysis in LAB is almost exclusively based on studies on L. lactis. This review provides the current status in the research of proteolytic systems of LAB with industrial relevance.
引用
收藏
页码:394 / 406
页数:13
相关论文
共 152 条
[61]  
HIGGINS CF, 1992, ANNU REV CELL BIOL, V8, P67, DOI 10.1146/annurev.cb.08.110192.000435
[62]   CLONING, SEQUENCING AND EXPRESSION OF THE GENE ENCODING THE CELL-ENVELOPE-ASSOCIATED PROTEINASE FROM LACTOBACILLUS-PARACASEI SUBSP PARACASEI NCDO-151 [J].
HOLCK, A ;
NAES, H .
JOURNAL OF GENERAL MICROBIOLOGY, 1992, 138 :1353-1364
[63]   A NONESSENTIAL GLUTAMYL AMINOPEPTIDASE IS REQUIRED FOR OPTIMAL-GROWTH OF LACTOCOCCUS-LACTIS MG1363 IN MILK [J].
IANSON, KJA ;
MOVAHEDI, S ;
GRIFFIN, HG ;
GASSON, MJ ;
MULHOLLAND, F .
MICROBIOLOGY-UK, 1995, 141 :2873-2881
[64]   Recombinant Lactococcus starters as a potential source of additional peptidolytic activity in cheese ripening [J].
Joutsjoki, V ;
Luoma, S ;
Tamminen, M ;
Kilpi, M ;
Johansen, E ;
Palva, A .
JOURNAL OF APPLIED MICROBIOLOGY, 2002, 92 (06) :1159-1166
[65]   THE EXTRACELLULAR P-I-TYPE PROTEINASE OF LACTOCOCCUS-LACTIS HYDROLYZES BETA-CASEIN INTO MORE THAN 100 DIFFERENT OLIGOPEPTIDES [J].
JUILLARD, V ;
LAAN, H ;
KUNJI, ERS ;
JERONIMUSSTRATINGH, CM ;
BRUINS, AP ;
KONINGS, WN .
JOURNAL OF BACTERIOLOGY, 1995, 177 (12) :3472-3478
[66]  
Juillard V, 1998, APPL ENVIRON MICROB, V64, P1230
[67]  
KATAYAMAFUJIMURA Y, 1987, J BIOL CHEM, V262, P4477
[68]   Genomic features of lactic acid bacteria effecting bioprocessing and health [J].
Klaenhammer, TR ;
Barrangou, R ;
Buck, BL ;
Azcarate-Peril, MA ;
Altermann, E .
FEMS MICROBIOLOGY REVIEWS, 2005, 29 (03) :393-409
[69]   Complete genome sequence of Lactobacillus plantarum WCFS1 [J].
Kleerebezem, M ;
Boekhorst, J ;
van Kranenburg, R ;
Molenaar, D ;
Kuipers, OP ;
Leer, R ;
Tarchini, R ;
Peters, SA ;
Sandbrink, HM ;
Fiers, MWEJ ;
Stiekema, W ;
Lankhorst, RMK ;
Bron, PA ;
Hoffer, SM ;
Groot, MNN ;
Kerkhoven, R ;
de Vries, M ;
Ursing, B ;
de Vos, WM ;
Siezen, RJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (04) :1990-1995
[70]   CLONING, DNA-SEQUENCE ANALYSIS AND PARTIAL CHARACTERIZATION OF PEPN, A LYSYL AMINOPEPTIDASE FROM LACTOBACILLUS-DELBRUCKII SSP LACTIS DSM7290 [J].
KLEIN, JR ;
KLEIN, U ;
SCHAD, M ;
PLAPP, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 217 (01) :105-114