{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T22:05:34Z","timestamp":1768514734647,"version":"3.49.0"},"reference-count":59,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2018,4,2]],"date-time":"2018-04-02T00:00:00Z","timestamp":1522627200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[2018,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>In this work, a new exploitation of the thermostable \u03b2\u2010glycosidase from <jats:italic>Sulfolobus solfataricus<\/jats:italic> expressed in <jats:italic>Saccharomyces cerevisiae<\/jats:italic> to create functional foods for low lactose diets was evaluated. For this purpose, the lactose hydrolysis reaction using immobilized and soluble enzymes was investigated. Activity and stability at different conditions of pH and temperature were tested. The immobilization process had a big impact on the catalysis performance, leading to an enhancement of the enzymatic reaction rate on lactose, as demonstrated by the increasing of 2 and 2.5 folds of <jats:italic>K<\/jats:italic><jats:sub>cat<\/jats:sub> and <jats:italic>K<\/jats:italic><jats:sub>cat<\/jats:sub>\/<jats:italic>K<\/jats:italic><jats:sub>M<\/jats:sub>, respectively. Moreover, the maximal activity for the immobilized form was referred at pH 6.5 instead of 7.0, leading to an improvement of the catalytic performance at milk pHs. Although the soluble enzyme was already weakly inhibited by the reaction products, the immobilization further reduced the inhibitory action of glucose increasing the <jats:italic>K<\/jats:italic><jats:sub>i<\/jats:sub> from 96.7 to 110.4 mM. Finally, the immobilized enzyme showed high hydrolysis rate in whole milk that yielded 99% of lactose breakdown in 10 and 30 min at 60 and 40\u00b0C, respectively. These results support the application of the immobilized \u03b2\u2010glycosidase for the development of new functional foods particularly suitable to the alleviation of lactose intolerance.<\/jats:p>","DOI":"10.1002\/bip.23118","type":"journal-article","created":{"date-parts":[[2018,4,2]],"date-time":"2018-04-02T12:11:36Z","timestamp":1522671096000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Improvement of functional properties of a thermostable \u03b2\u2010glycosidase for milk lactose hydrolysis"],"prefix":"10.1002","volume":"109","author":[{"given":"Elena","family":"Ionata","sequence":"first","affiliation":[{"name":"Institute of Agro\u2010Environmental and Forest Biology\u2014Consiglio Nazionale delle Ricerche (CNR), via P. 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