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Is protein phosphorylation a control mechanism for the degradation of caseins by lactic acid bacteria? The detection of an extracellular acid phosphatase activity
Author(s) -
Kyriakidis S. M.,
Sakellaris G.,
Sotiroudis T. G.
Publication year - 1993
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1993.tb00361.x
Subject(s) - lactic acid , library science , foundation (evidence) , phosphorylation , bacteria , biochemistry , chemistry , biology , political science , computer science , law , genetics
The existence of an extracellular acid phosphatase activity in Lactobacillus delbrueckii subsp. bulgaricus ACADC235 and in Lactococcus lactis subsp. cremoris Wg2 is reported in the present work. Acid phosphatase ( p ‐nitrophenyl phosphatase, pNPPase) activity was detected both in whole cells and in crude cell‐wall extracts and coelutes from Sepharose 6B together with a fraction of proteinase activity and a high Mr phosphopolyanionic material. It represents a putative protein phosphatase as it efficiently dephosphorylates casein and phosvitin. This extracellular acid phosphatase activity seems to play a role in the control of casein proteolysis by lactic acid bacteria since dephosphorylation of casein enhances its degradation by the cell wall‐bound proteinase.