Limonin-D-ring-lactonase

Limonin-D-ring-lactonase is an enzyme that plays a crucial role in the metabolism of limonoids, a class of terpenoids found in citrus fruits. This enzyme specifically catalyzes the hydrolysis of the D-ring lactone in limonin, a bitter compound in citrus fruits, to produce non-bitter compounds.

Function[edit | edit source]

Limonin-D-ring-lactonase is responsible for the conversion of limonin into non-bitter compounds. This enzymatic process is essential in the citrus industry, as it helps to reduce the bitterness of citrus products. The enzyme achieves this by catalyzing the hydrolysis of the D-ring lactone in limonin.

Structure[edit | edit source]

The structure of Limonin-D-ring-lactonase is complex and is composed of several amino acids. The enzyme's active site, where the hydrolysis of limonin occurs, is typically composed of a catalytic triad of amino acids. These amino acids work together to facilitate the hydrolysis reaction.

Role in Citrus Industry[edit | edit source]

In the citrus industry, Limonin-D-ring-lactonase is of significant importance. The enzyme's ability to convert limonin, a bitter compound, into non-bitter compounds helps to improve the taste of citrus products. This enzymatic process is therefore crucial in the production of citrus juices and other citrus-based products.

Research and Future Applications[edit | edit source]

Research into Limonin-D-ring-lactonase and its potential applications is ongoing. The enzyme's ability to reduce bitterness in citrus products has significant implications for the food industry. Furthermore, understanding the enzyme's structure and function could lead to the development of new methods for bitterness reduction in other food products.