Literature summary for 3.4.14.11 extracted from

Uestuen-Aytekin, O.e.; Arisoy, S.; Aytekin, A.O.e.; Yildiz, E.
Statistical optimization of cell disruption techniques for releasing intracellular X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis spp. lactis (2016), Ultrason. Sonochem., 29, 163-171 .

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Application

Application	Comment	Organism
synthesis	comparison of the effects of cell disruption methods on the activity of PepX. The optimized values of high-pressure homogenization are one cycle at 130 MPa providing activity of 114.47 mU/ml, while sonication gives an activity of 145.09 mU/ml at 28 min with 91% power and three cycles	Lactococcus lactis ssp. lactis

Inhibitors

Inhibitors	Comment	Organism
chloroform	reduced the enzyme activity during purification	Lactococcus lactis ssp. lactis
EDTA	reduces the enzyme activity during purification	Lactococcus lactis ssp. lactis
SDS	reduces the enzyme activity during purification	Lactococcus lactis ssp. lactis
Triton X-100	reduces the enzyme activity during purification	Lactococcus lactis ssp. lactis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
intracellular	-	Lactococcus lactis ssp. lactis	5622	-

Organism

Organism	UniProt	Comment	Textmining
Lactococcus lactis ssp. lactis	-	-	-
Lactococcus lactis ssp. lactis	A0A1V0NIQ5	-	-
Lactococcus lactis ssp. lactis NRRL B-1821	-	-	-
Lactococcus lactis ssp. lactis NRRL B-1821	A0A1V0NIQ5	-	-

Purification (Commentary)

Purification (Comment)	Organism
native enzyme, comparison of the effects of several cell disruption methods on the activity of PepX, detailed overview. Statistical optimization methods are performed for two cavitation methods, hydrodynamic (high-pressure homogenization) and acoustic (sonication), to determine the more appropriate disruption method. Two level factorial design (2FI), with the parameters of number of cycles and pressure, and Box-Behnken design (BBD), with the parameters of cycle, sonication time, and power, are used for the optimization of the high-pressure homogenization and sonication methods, respectively. In addition, disruption methods, consisting of lysozyme, bead milling, heat treatment, freeze-thawing, liquid nitrogen, EDTA, Triton-X, SDS, chloroform, and antibiotics, are performed and compared with the high-pressure homogenization and sonication methods. The optimized values of high-pressure homogenization are one cycle at 130 MPa providing activity of 114.47 mU/ml, while sonication afforded an activity of 145.09 mU/ml at 28 min with 91% power and three cycles	Lactococcus lactis ssp. lactis

Purification (Comment)

Organism

native enzyme, comparison of the effects of several cell disruption methods on the activity of PepX, detailed overview. Statistical optimization methods are performed for two cavitation methods, hydrodynamic (high-pressure homogenization) and acoustic (sonication), to determine the more appropriate disruption method. Two level factorial design (2FI), with the parameters of number of cycles and pressure, and Box-Behnken design (BBD), with the parameters of cycle, sonication time, and power, are used for the optimization of the high-pressure homogenization and sonication methods, respectively. In addition, disruption methods, consisting of lysozyme, bead milling, heat treatment, freeze-thawing, liquid nitrogen, EDTA, Triton-X, SDS, chloroform, and antibiotics, are performed and compared with the high-pressure homogenization and sonication methods. The optimized values of high-pressure homogenization are one cycle at 130 MPa providing activity of 114.47 mU/ml, while sonication afforded an activity of 145.09 mU/ml at 28 min with 91% power and three cycles

Lactococcus lactis ssp. lactis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Gly-Pro-4-nitroanilide + H2O	-	Lactococcus lactis ssp. lactis	Gly + Pro-4-nitroanilide	-	?
Gly-Pro-4-nitroanilide + H2O	-	Lactococcus lactis ssp. lactis NRRL B-1821	Gly + Pro-4-nitroanilide	-	?

Synonyms

Synonyms	Comment	Organism
PepX	-	Lactococcus lactis ssp. lactis
X-prolyl dipeptidyl aminopeptidase	-	Lactococcus lactis ssp. lactis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
45	65	the enzyme is thermolabile during purification	Lactococcus lactis ssp. lactis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Lactococcus lactis ssp. lactis