Editing Botulinum toxin (section)

===Organism and toxin susceptibilities===
{{Expand section|1=modern content and referencing on antibiotic susceptibilities |small=no|date=February 2015}}

Proper refrigeration at temperatures below {{convert|4.4|C|F}} slows the growth of ''C.&nbsp;botulinum''.<ref>{{Cite web |date=29 March 2011 |title=Clostridium botulinum Toxin Formation |url=https://www.fda.gov/files/food/published/Fish-and-Fishery-Products-Hazards-and-Controls-Guidance-Chapter-13-Download.pdf |access-date=12 March 2023 |website=U.S. [[Food and Drug Administration]] (FDA) |page=246 |archive-date=8 February 2021 |archive-url=https://web.archive.org/web/20210208183813/https://www.fda.gov/files/food/published/Fish-and-Fishery-Products-Hazards-and-Controls-Guidance-Chapter-13-Download.pdf |url-status=live }}</ref> The organism is also susceptible to high salt, high oxygen, and low pH levels.<ref name="WHO2018" />{{failed verification|date=December 2022}} The toxin itself is rapidly destroyed by heat, such as in thorough cooking.<ref>{{cite journal |vauthors = Licciardello JJ, Nickerson JT, Ribich CA, Goldblith SA |title = Thermal inactivation of type E botulinum toxin |journal = Applied Microbiology |volume = 15 |issue = 2 |pages = 249–256 |date = March 1967 |pmid = 5339838 |pmc = 546888 |doi = 10.1128/AEM.15.2.249-256.1967 }}</ref> The spores that produce the toxin are heat-tolerant and will survive boiling water for an extended period of time.<ref>{{cite journal |vauthors = Setlow P |title = I will survive: DNA protection in bacterial spores |journal = Trends in Microbiology |volume = 15 |issue = 4 |pages = 172–180 |date = April 2007 |pmid = 17336071 |doi = 10.1016/j.tim.2007.02.004 }}</ref>

The botulinum toxin is [[denaturation (biochemistry)|denatured]] and thus deactivated at temperatures greater than {{convert|85|C|F}} for five minutes.<ref name="WHO2018">{{cite web |title=Fact sheets - Botulism |url=https://www.who.int/news-room/fact-sheets/detail/botulism |work=World Health Organization |access-date=23 March 2019 |date=10 January 2018 |archive-date=23 March 2019 |archive-url=https://web.archive.org/web/20190323162924/https://www.who.int/news-room/fact-sheets/detail/botulism |url-status=live }}</ref> As a zinc [[metalloprotease]] (see below), the toxin's activity is also susceptible, post-exposure, to [[enzyme inhibition|inhibition]] by [[protease inhibitor (pharmacology)|protease inhibitors]], e.g., zinc-coordinating [[hydroxamate]]s.<ref name=Bowlin11>{{cite journal |vauthors = Li B, Peet NP, Butler MM, Burnett JC, Moir DT, Bowlin TL |title = Small molecule inhibitors as countermeasures for botulinum neurotoxin intoxication |journal = Molecules |volume = 16 |issue = 1 |pages = 202–220 |date = December 2010 |pmid = 21193845 |pmc = 6259422 |doi = 10.3390/molecules16010202 |doi-access = free |title-link = doi }}</ref><ref name=Janda0911>{{cite journal |vauthors = Capková K, Salzameda NT, Janda KD |title = Investigations into small molecule non-peptidic inhibitors of the botulinum neurotoxins |journal = Toxicon |volume = 54 |issue = 5 |pages = 575–582 |date = October 2009 |pmid = 19327377 |pmc = 2730986 |doi = 10.1016/j.toxicon.2009.03.016 |bibcode = 2009Txcn...54..575C }}</ref>