Abstract
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.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call