Abstract

UV fluorescence and absorption spectroscopy from Bacillus subtilis spores detected proteins and dipicolinic acid (DPA) released into the supernatant after heat treatments ranging from 20° to 90°C. The protein and DPA concentration in the supernatant was greater with higher heat treatment temperatures, undergoing a substantial increase for T60°C, and supporting the theory that spores undergo a phase transition from a glassylike to a rubberylike state at 56°C. Gel electrophoresis detected several small proteins with molecular weights between 6  and   11   kDa. These proteins may be small acid-soluble spore proteins that are present in spores but break down during germination. A 30 kDa protein extracted above 60°C is related to the rubber–glass phase transition.

© 2006 Optical Society of America

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