A highly active esterase from Lactobacillus helveticus hydrolyzes chlorogenic acid in sunflower meal to prevent chlorogenic acid induced greening in sunflower protein isolates
A highly active esterase from Lactobacillus helveticus hydrolyzes chlorogenic acid in sunflower meal to prevent chlorogenic acid induced greening in sunflower protein isolates
复制标题
来自瑞士乳杆菌的高活性酯酶水解向日葵粕中的绿原酸,以防止向日葵分离蛋白中绿原酸引起的绿化
DOI:
10.1016/j.foodres.2022.111996
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发表时间:
2022
影响因子:
8.1
通讯作者:
Owens, Cedric P.
中科院分区:
文献类型:
--
作者:
Lo Verde, Christine;Pepra-Ameyaw, Nana Baah;Drucker, Charles T.;Okumura, Tracie L.S.;Lyon, Katherine A.;Muniz, Julia C.;Sermet, Chloe S.;Were Senger, Lilian;Owens, Cedric P.
Chlorogenic acid (CGA) is an ester between caffeic and quinic acid. It is found in many foods and reacts with free amino groups in proteins at alkaline pH, leading to the formation of an undesirable green pigment in sunflower seed-derived ingredients. This paper presents the biochemical characterization and application of a highly active chlorogenic acid esterase fromLactobacillus helveticus. The enzyme is one of the most active CGA esterases known to date with aKmof 0.090 mM and akcatof 82.1 s−1. The CGA esterase is easily expressed recombinantly inE. coliin large yields and is stable over a wide range of pH and temperatures. We characterized CGA esterase’s kinetic properties in sunflower meal and demonstrated that the enzyme completely hydrolyzes CGA in the meal. Finally, we showed that CGA esterase treatment of sunflower seed meal enables the production of pale brown sunflower protein isolates using alkaline extraction. This work will allow for more widespread use of sunflower-derived products in applications where neutrally-colored food products are desired.