Role in Flavor Development in Cheese. lactis subsp. cremoris B78 and Its Possible Cystathionine (beta)-Lyase from Lactococcus Purification and Characterization of

[1]  R. Baankreis,et al.  The occurrence of two intracellular oligoendopeptidases in Lactococcus lactis and their significance for peptide conversion in cheese , 1995, Applied Microbiology and Biotechnology.

[2]  G. Stauffer,et al.  DNA sequence of the metC gene and its flanking regions from Salmonella typhimurium LT2 and homology with the corresponding sequence of Escherichia coli , 1989, Molecular and General Genetics MGG.

[3]  W. D. de Vos,et al.  Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering , 1995, Applied and environmental microbiology.

[4]  G. G. Pritchard,et al.  Occurrence of arginine deiminase pathway enzymes in arginine catabolism by wine lactic Acid bacteria , 1995, Applied and environmental microbiology.

[5]  A. Alting,et al.  The role of starter peptidases in the initial proteolytic events leading to amino acids in Gouda cheese , 1995 .

[6]  A. Alting,et al.  Conversion of αS1-casein-(24-199)-fragment and β-casein under cheese conditions by chymosin and starter peptidases , 1995 .

[7]  S. Visser,et al.  Isolation and comparative characterization of components that contribute to the flavour of different types of cheese , 1994 .

[8]  A. Chopin.  Organization and regulation of genes for amino acid biosynthesis in lactic acid bacteria. , 1993, FEMS microbiology reviews.

[9]  P. Renault,et al.  Gene inactivation in Lactococcus lactis: histidine biosynthesis , 1993, Journal of bacteriology.

[10]  P. Renault,et al.  Gene inactivation in Lactococcus lactis: branched-chain amino acid biosynthesis , 1993, Journal of bacteriology.

[11]  A. Alting,et al.  The Conversion of the α-s1-Casein-(1-23)-Fragment by the Free and Bound Form of the Cell-Envelope Proteinase of Lactococcus lactis subsp. cremoris Under Conditions Prevailing in Cheese , 1993 .

[12]  T. Morishita,et al.  Nutritional Requirements in Multiple Auxotrophic Lactic Acid Bacteria: Genetic Lesions Affecting Amino Acid Biosynthetic Pathways in Lactococcus lactis, Enterococcus faecium, and Pediococcus acidilactici. , 1992, Bioscience, biotechnology, and biochemistry.

[13]  R. Simard,et al.  Bitter flavour in dairy products. II. A review of bitter peptides from caseins: their formation, isolation and identification structure masking and inhibition , 1992 .

[14]  G. G. Pritchard,et al.  Proteolytic enzymes of dairy starter cultures , 1987 .

[15]  K. Soda,et al.  l-Methionine γ-lyase from Pseudomonas putida and Aeromonas , 1987 .

[16]  J. K. Rippe,et al.  Enzymic Generation of Methanethiol To Assist in the Flavor Development of Cheddar Cheese and Other Foods , 1986 .

[17]  G N Cohen,et al.  Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[18]  H. Yamada,et al.  Cystathionine gamma-lyase of Streptomyces phaeochromogenes. The occurrence of cystathionine gamma-lyase in filamentous bacteria and its purification and characterization. , 1984, The Journal of biological chemistry.

[19]  F. Exterkate.  Location of Peptidases Outside and Inside the Membrane of Streptococcus cremoris , 1984, Applied and environmental microbiology.

[20]  C. Dwivedi,et al.  Cloning, purification, and characterization of beta-cystathionase from Escherichia coli. , 1982, Biochemistry.

[21]  K. W. Turner,et al.  Lactose fermentation in Cheddar cheese and the effect of salt. , 1980 .

[22]  B. Law,et al.  Formation of methanethiol by bacteria isolated from raw milk and Cheddar cheese , 1978, Journal of Dairy Research.

[23]  Yasushi Sato,et al.  Direct observation of fine structures of bacteria in ripened Cheddar cheese by electron microscopy. , 1978 .

[24]  Y. Yamasaki,et al.  A Peptide With Delicious Taste , 1978 .

[25]  J. Uren,et al.  Modulation of cysteine metabolism in mice--effects of propargylglycine and L-cyst(e)ine-degrading enzymes. , 1978, Biochemical pharmacology.

[26]  J. Burnell,et al.  Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase. , 1977, Biochimica et biophysica acta.

[27]  M. M. Bradford.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[28]  S. Guggenheim.  [195f] β-Cystathionase (Salmonella): l-Cystathionine + H2O → l-homocysteine + pyruvic acid + NH3 , 1971 .