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Methods"],"published-print":{"date-parts":[[2020,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>An assay-based method was developed to determine the residual activity of the maltogenic amylase from <jats:italic>Geobacillus stearothermophilus<\/jats:italic> in white bread. It was found that the important step for amylase extraction from the bread matrix was the addition of 10% (w\/v) maltodextrin in the extraction buffer. The endogenous amylase activity in dough was investigated, and its inactivation during bread baking was proven. Thus, all amylase activities measured after baking have an exogenous origin. The amylase activities in the loaf of self-baked white bread containing defined dosages of exogenous amylase (10\u2013100 \u03bcg per g flour) were reproducibly determined with 17.8 \u00b1 1.24% residual activity. Moreover, an amylase activity of 369 \u00b1 34.3 pkat g<jats:sub>bread<\/jats:sub><jats:sup>\u22121<\/jats:sup> was determined in three batches of a commercial white bread. The real temperature impact on the amylase during bread baking was investigated. The highest temperature in the crumb was 97 \u00b0C and, therefore, is significantly lower than the oven temperature (230 \u00b0C).<\/jats:p>","DOI":"10.1007\/s12161-019-01673-7","type":"journal-article","created":{"date-parts":[[2019,12,16]],"date-time":"2019-12-16T16:29:59Z","timestamp":1576513799000},"page":"496-502","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Determination of the Direct Activity of the Maltogenic Amylase from Geobacillus stearothermophilus in White Bread"],"prefix":"10.1007","volume":"13","author":[{"given":"Katrin","family":"Reichenberger","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anja","family":"Luz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ines","family":"Seitl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8307-7027","authenticated-orcid":false,"given":"Lutz","family":"Fischer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,11,21]]},"reference":[{"key":"1673_CR1","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1002\/(SICI)1521-379X(199801)50:1<39::AID-STAR39>3.0.CO;2-S","volume":"50","author":"C Christophersen","year":"1998","unstructured":"Christophersen C, Otzen DE, Noman BE et al (1998) Enzymatic characterisation of Novamyl\u00ae, a thermostable \u03b1-amylase. 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Anja Luz declares that she has no conflict of interest. Ines Seitl declares that she has no conflict of interest. Lutz Fischer declares that he has no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of Interest"}},{"value":"This study does not contain experiments that involve human or animals other than the authors who performed the work.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical Approval"}},{"value":"All authors have read the manuscript and agreed upon its submission to the journal.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Informed Consent"}}]}}