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.
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页码:394 / 406
页数:13
相关论文
共 152 条
[1]   Complete genome sequence of the probiotic lactic acid bacterium Lactobacillus acidophilus NCFM [J].
Altermann, E ;
Russell, WM ;
Azcarate-Peril, MA ;
Barrangou, R ;
Buck, BL ;
McAuliffe, O ;
Souther, N ;
Dobson, A ;
Duong, T ;
Callanan, M ;
Lick, S ;
Hamrick, A ;
Cano, R ;
Klaenhammer, TR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (11) :3906-3912
[2]   Cloning and sequencing of the gene encoding X-prolyl-dipeptidyl aminopeptidase (PepX) from Streptococcus thermophilus strain ACA-DC 4 [J].
Anastasiou, R ;
Papadelli, M ;
Georgalaki, MD ;
Kalantzopoulos, G ;
Tsakalidou, E .
JOURNAL OF APPLIED MICROBIOLOGY, 2002, 93 (01) :52-59
[3]   CLONING, SEQUENCING AND CHARACTERIZATION OF THE PEPIP GENE ENCODING A PROLINE IMINOPEPTIDASE FROM LACTOBACILLUS-DELBRUECKII SUBSP BULGARICUS CNRZ-397 [J].
ATLAN, D ;
GILBERT, C ;
BLANC, B ;
PORTALIER, R .
MICROBIOLOGY-UK, 1994, 140 :527-535
[4]   Microarray analysis of a two-component regulatory system involved in acid resistance and proteolytic activity in Lactobacillus acidophilus [J].
Azcarate-Peril, MA ;
McAuliffe, O ;
Altermann, E ;
Lick, S ;
Russell, WM ;
Klaenhammer, TR .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2005, 71 (10) :5794-5804
[5]   The complete genomes of Lactobacillus plantarum and Lactobacillus johnsonii reveal extensive differences in chromosome organization and gene content [J].
Boekhorst, J ;
Siezen, RJ ;
Zwahlen, MC ;
Vilanova, D ;
Pridmore, RD ;
Mercenier, A ;
Kleerebezem, M ;
de Vos, WM ;
Brüssow, H ;
Desiere, F .
MICROBIOLOGY-SGM, 2004, 150 :3601-3611
[6]   Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus [J].
Bolotin, A ;
Quinquis, B ;
Renault, P ;
Sorokin, A ;
Ehrlich, SD ;
Kulakauskas, S ;
Lapidus, A ;
Goltsman, E ;
Mazur, M ;
Pusch, GD ;
Fonstein, M ;
Overbeek, R ;
Kyprides, N ;
Purnelle, B ;
Prozzi, D ;
Ngui, K ;
Masuy, D ;
Hancy, F ;
Burteau, S ;
Boutry, M ;
Delcour, J ;
Goffeau, A ;
Hols, P .
NATURE BIOTECHNOLOGY, 2004, 22 (12) :1554-1558
[7]   The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp lactis IL1403 [J].
Bolotin, A ;
Wincker, P ;
Mauger, S ;
Jaillon, O ;
Malarme, K ;
Weissenbach, J ;
Ehrlich, SD ;
Sorokin, A .
GENOME RESEARCH, 2001, 11 (05) :731-753
[8]   Contribution of Lactococcus lactis cell envelope proteinase specificity to peptide accumulation and bitterness in reduced-fat cheddar cheese [J].
Broadbent, JR ;
Barnes, M ;
Brennand, C ;
Strickland, M ;
Houck, K ;
Johnson, ME ;
Steele, JL .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2002, 68 (04) :1778-1785
[9]   Autolysis of Lactococcus lactis caused by induced overproduction of its major autolysin, AcmA [J].
Buist, G ;
Karsens, H ;
Nauta, A ;
vanSinderen, D ;
Venema, G ;
Kok, J .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1997, 63 (07) :2722-2728
[10]   Autolysis of Lactococcus lactis is influenced by proteolysis [J].
Buist, G ;
Venema, G ;
Kok, J .
JOURNAL OF BACTERIOLOGY, 1998, 180 (22) :5947-5953