Tag: Heat inactivation

Scientific research has established that heat, including high-temperature baking, is a primary method for deactivating lectins in many foods. However, the effectiveness hinges on specific variables like temperature, moisture, and cooking time. So, does baking remove lectins completely and reliably?

In the early 1900s, researchers discovered that excessive consumption of raw egg whites could cause "egg-white injury syndrome," a condition caused by the protein avidin binding tightly to biotin. Knowing how to neutralize avidin is therefore crucial for both nutritional safety and for achieving reliable results in a wide array of laboratory techniques.

Raw egg whites contain a protein called avidin, which has a remarkable affinity for binding with biotin, a crucial B-vitamin. This tight bond can prevent the body from absorbing biotin, but fortunately, the process of destroying this protein is both simple and effective. By understanding the properties of avidin, you can easily prepare eggs to unlock their full nutritional potential without concern for biotin deficiency.

Did you know that the stinging or tingling sensation from eating fresh pineapple is caused by the protein-digesting enzyme, bromelain? Getting bromelain out of pineapple is a straightforward process, relying on either heat to deactivate the enzyme or mechanical methods to separate it, and is essential for preventing the characteristic mouth burn and enabling certain recipes.

According to the CDC, improperly canned home vegetables, including green beans, are the most common source of botulism outbreaks in the United States. The question of whether you can remove botulism from canned green beans is a serious one, with the simple and direct answer being: no, not reliably enough to be safe.