PMID- 21696390
OWN - NLM
STAT- MEDLINE
DCOM- 20120816
LR  - 20181201
IS  - 1750-3841 (Electronic)
IS  - 0022-1147 (Linking)
VI  - 76
IP  - 6
DP  - 2011 Aug
TI  - Enzyme stability of microencapsulated Bifidobacterium animalis ssp. lactis Bb12 
      after freeze drying and during storage in low water activity at room temperature.
PG  - M463-71
LID - 10.1111/j.1750-3841.2011.02246.x [doi]
AB  - Stability of enzymes such as beta-galactosidase (beta-gal), beta-glucosidase (beta-glu), 
      lactate dehydrogenase (LDH), pyruvate kinase (PK), hexokinase (HK), and ATPase of 
      microencapsulated Bifidobacterium animalis ssp. lactis Bb12 after freeze-drying 
      and after 10 wk of storage at low water activity (a(w)) at room temperature was 
      studied. Bacteria were microencapsulated using alginate formulation with or 
      without mannitol fortification (sodium alginate and mannitol [SAM] and sodium 
      alginate [SA], respectively) by creating gel beads followed by freeze drying. Two 
      types of dried gel beads were then stored at low a(w), such as 0.07, 0.1, and 
      0.2; storage in an aluminum foil was used as control. All storage was carried out 
      at room temperature of 25  degrees C for 10 wk. Measurement of beta-gal, beta-glu, LDH, PK, HK, 
      and ATPase (with or without exposure to pH 2.0 for 2 h) activities was carried 
      out before freeze drying, after freeze drying, and after 10 wk of storage. There 
      was a significant decrease in almost all enzyme activities, except that of PK. 
      SAM and SA showed no different effect on maintaining enzyme activities during 
      freeze drying. Storage for 10 wk at room temperature at various low a(w) using 
      SAM and SA system had a significant effect on retention of most enzymes studied, 
      except that of PK and LDH. Storage at a(w) of 0.07 and 0.1 was more effective in 
      maintaining enzyme activities than storage at a(w) of 0.2 and in an aluminum 
      foil. However, mannitol fortification into alginate system did not significantly 
      improve retention of enzymes during 10 wk of storage.
CI  - (c) 2011 Institute of Food Technologists(R)
FAU - Dianawati, Dianawati
AU  - Dianawati D
AD  - School of Biomedical and Health Sciences, Victoria Univ., Werribee Campus, P.O. 
      Box 14428, Melbourne, Victoria 8001, Australia.
FAU - Shah, Nagendra P
AU  - Shah NP
LA  - eng
PT  - Comparative Study
PT  - Journal Article
DEP - 20110622
PL  - United States
TA  - J Food Sci
JT  - Journal of food science
JID - 0014052
RN  - 0 (Alginates)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Emulsions)
RN  - 0 (Gels)
RN  - 0 (Hexuronic Acids)
RN  - 059QF0KO0R (Water)
RN  - 3OWL53L36A (Mannitol)
RN  - 8A5D83Q4RW (Glucuronic Acid)
RN  - EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor))
RN  - EC 3.2.1.- (Glycoside Hydrolases)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
SB  - IM
MH  - Adenosine Triphosphatases/chemistry/metabolism
MH  - Alginates/chemistry
MH  - Bacterial Proteins/chemistry/*metabolism
MH  - Bifidobacterium/*enzymology
MH  - Emulsions
MH  - Enzyme Stability
MH  - *Food Technology
MH  - Freeze Drying
MH  - Gels
MH  - Glucuronic Acid/chemistry
MH  - Glycoside Hydrolases/chemistry/metabolism
MH  - Hexuronic Acids/chemistry
MH  - Hydrogen-Ion Concentration
MH  - Mannitol/chemistry
MH  - Microspheres
MH  - Phosphotransferases (Alcohol Group Acceptor)/chemistry/metabolism
MH  - Probiotics/chemistry/*metabolism
MH  - Temperature
MH  - Time Factors
MH  - Water/analysis
EDAT- 2011/06/24 06:00
MHDA- 2012/08/17 06:00
CRDT- 2011/06/24 06:00
PHST- 2011/06/24 06:00 [entrez]
PHST- 2011/06/24 06:00 [pubmed]
PHST- 2012/08/17 06:00 [medline]
AID - 10.1111/j.1750-3841.2011.02246.x [doi]
PST - ppublish
SO  - J Food Sci. 2011 Aug;76(6):M463-71. doi: 10.1111/j.1750-3841.2011.02246.x. Epub 
      2011 Jun 22.