Improvement of fermentation conditions for the production of X-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis

被引:12
作者
Pérez-Guzmán, AE
Victoria, TCY
Cruz-Camarillo, R
Hernández-Sánchez, H
机构
[1] Inst Politecn Nacl, Escuela Nacl Ciencias Biol, Dept Grad & Invest Alimentos, Mexico City 11340, DF, Mexico
[2] IPN, ENCB, Dept Microbiol, Mexico City 07738, DF, Mexico
关键词
culture medium; enzymes; Lactococcus lactis; peptidases; PepXP; X-prolyl-dipeptidyl aminopeptidase;
D O I
10.1023/B:WIBI.0000033066.86658.34
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 [微生物学]; 0836 [生物工程]; 090102 [作物遗传育种]; 100705 [微生物与生化药学];
摘要
The quantitative effects of some fermentation conditions on the production of the enzyme X-prolyl-dipeptidyl aminopeptidase (PepXP) (EC 3.4.14.5) of Lactococcus lactis subsp. lactis and cremoris were studied. The PepXP activity was found both in the membrane and in the cytoplasm, suggesting the presence of multiple molecular forms. Both microorganisms showed higher PepXP activities when glucose (5 g/l) was used as the carbon source and the yeast extract in the culture medium was increased to 3.5 g/l. In these conditions, 226 mU/ml of PepXP activity were obtained with L. lactis subsp. lactis and 235 mU/ml with the subsp. cremoris after 6 h. The best fermentation temperature was in the 30-32degreesC range. The enzyme activity remained stable even during the stationary phase.
引用
收藏
页码:413 / 417
页数:5
相关论文
共 23 条
[1]
X-PROLYL-DIPEPTIDYL AMINOPEPTIDASE OF LACTOBACILLUS-DELBRUECKII SUBSP BULGARICUS - CHARACTERIZATION OF THE ENZYME AND ISOLATION OF DEFICIENT MUTANTS [J].
ATLAN, D ;
LALOI, P ;
PORTALIER, R .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1990, 56 (07) :2174-2179
[2]
BERGMEYER H.U., 1974, METHODS ENZYMATIC AN, P574, DOI DOI 10.1016/B978-0-12-091302-2.50010-4
[3]
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
[4]
Purification and characterization of a prolyl aminopeptidase from Debaryomyces hansenii [J].
Bolumar, T ;
Sanz, Y ;
Aristoy, MC ;
Toldrá, F .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2003, 69 (01) :227-232
[5]
PROLINE-SPECIFIC PEPTIDASES OF STREPTOCOCCUS-CREMORIS AM2 [J].
BOOTH, M ;
DONNELLY, WJ ;
FHAOLAIN, IN ;
JENNINGS, PV ;
OCUINN, G .
JOURNAL OF DAIRY RESEARCH, 1990, 57 (01) :79-88
[6]
CHAVEZCAMARILLO G, 1994, THESIS ENCB IPN MEXI
[7]
Purification and partial characterisation of X-prolyl dipeptidyl aminopeptidase of Lactobacillus helveticus ITG LH1 [J].
Degraeve, P ;
Martial-Gros, A .
INTERNATIONAL DAIRY JOURNAL, 2003, 13 (07) :497-507
[8]
Purification and characterization of X-prolyl dipeptidyl aminopeptidase from Propionibacterium shermanii NCDO 853 [J].
FernandezEspla, MD ;
Fox, PF .
INTERNATIONAL DAIRY JOURNAL, 1997, 7 (01) :23-29
[9]
GARCIA RC, 1983, J GEN MICROBIOL, V129, P3519
[10]
Bacterial aminopeptidases: Properties and functions [J].
Gonzales, T ;
RobertBaudouy, J .
FEMS MICROBIOLOGY REVIEWS, 1996, 18 (04) :319-344