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Applied and Environmental Microbiology, July 2006, p. 4503-4514, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.01829-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Response of Lactobacillus helveticus PR4 to Heat Stress during Propagation in Cheese Whey with a Gradient of Decreasing Temperatures

Raffaella Di Cagno,1 Maria De Angelis,1* Antonio Limitone,1 Patrick F. Fox,2 and Marco Gobbetti1

Dipartimento di Protezione delle Piante e Microbiologia Applicata, Università degli Studi di Bari, Bari, Italy,1 Department of Food and Nutritional Sciences, University College Cork, Cork, Ireland2

Received 3 August 2005/ Accepted 16 March 2006

The heat stress response was studied in Lactobacillus helveticus PR4 during propagation in cheese whey with a gradient of naturally decreasing temperature (55 to 20°C). Growth under a gradient of decreasing temperature was compared to growth at a constant temperature of 42°C. Proteinase, peptidase, and acidification activities of L. helveticus PR4 were found to be higher in cells harvested when 40°C was reached by a gradient of decreasing temperature than in cells grown at constant temperature of 42°C. When cells grown under a temperature gradient were harvested after an initial exposure of 35 min to 55°C followed by decreases in temperature to 40 (3 h), 30 (5 h 30 min), or 20°C (13 h 30 min) and were then compared with cells grown for the same time at a constant temperature of 42°C, a frequently transient induction of the levels of expression of 48 proteins was found by two-dimensional electrophoresis analysis. Expression of most of these proteins increased following cooling from 55 to 40°C (3 h). Sixteen of these proteins were subjected to N-terminal and matrix-assisted laser desorption ionization-time of flight mass spectrometry analyses. They were identified as stress proteins (e.g., DnaK and GroEL), glycolysis-related machinery (e.g., enolase and glyceraldehyde-3-phosphate dehydrogenase), and other regulatory proteins or factors (e.g., DNA-binding protein II and ATP-dependent protease). Most of these proteins have been found to play a role in the mechanisms of heat stress adaptation in other bacteria.

* Corresponding author. Mailing address: Dipartimento di Protezione delle Piante e Microbiologia Applicata, Facoltà di Scienze Biotecnologiche di Bari, Via G. Amendola 165/a, 70126 Bari, Italy. Phone: 39 080 5442948. Fax: 39 080 5442911. E-mail: m.deangelis{at}agr.uniba.it.

Applied and Environmental Microbiology, July 2006, p. 4503-4514, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.01829-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gagnaire, V., Jardin, J., Jan, G., Lortal, S. (2009). Invited review: Proteomics of milk and bacteria used in fermented dairy products: From qualitative to quantitative advances. J DAIRY SCI 92: 811-825 [Abstract] [Full Text]  


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