From jeans to orange juice to laundry detergent: None would be possible without the activity of enzymes. Currently, enzymes used in industry are produced through an expensive, laborious fermentation process, requiring cold storage. However, an innovative new approach, ushered in by Penn Dental Medicine biochemist Dr. Henry Daniell‘s research, is opening up a whole new way of making these valuable proteins.
Two new studies in Plant Biotechnology Journal reveal that enzymes made in plants can be as effective as the traditional microbial-derived enzyme at accomplishing a number of industrial tasks, from juice clarification, cleaning laundry stains, dyeing textiles, or de-pilling fabric. Such plant-grown enzymes have the added benefit of being cheaper to produce and shelf-stable in a powdered form, requiring no refrigeration. The technology has led to the launch of startup-company PhylloZyme.
“I’m excited to have pioneered the production of technology that can make a major difference in affordability of everyday products,” says Daniell.
The first paper examined pectinases – enzymes that break down pectin, a natural component of fruits, an additive to certain foods, and a component of cotton fiber. Using equipment normally leveraged in the textile industry, the Penn-led team showed that the plant-made enzymes could more effectively break down pectin in cotton fabric, allowing water absorption, in a process called bioscouring, a necessary step in fabric dyeing as well.
They also tested the leaf-derived enzymes in clarifying orange juice, a step that releases flavor and nutrients from the pulp. Here, too, the plant-derived enzymes were equal to or better than the commercial microbial-derived productions.
In the second study, researchers produced five new plant-derived enzymes commonly used in the textile or detergent industry and compared them to 15 commercial enzyme products, now derived from microbes, usually yeast.
In comparing the plant-made products to the others, one major difference was staying power. The commercially available enzymes needed refrigeration and their activity declined at higher pH or higher temperatures. In contrast, the plant-made products were shelf stable at room temperature for up to16 months, and remained effective across a range of pH values and temperatures.
Daniell is enthusiastic about the potential of these products to reshape 50-year-old industrial processes. The plant-made enzymes also serve as a milestone in the genetic-engineering field, as the first protein product made in leaves for commercial use.
The studies were supported by the NIH (grants EY024564, HL107904, HL109442, HL133191).
Contact: Beth Adams, firstname.lastname@example.org, 215-573-8224
SOURCE Penn Dental Medicine