2021
DOI: 10.1016/j.btre.2021.e00637
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Investigating thermal stability based on the structural changes of lactase enzyme by several orthogonal methods

Abstract: Highlights The primary and secondary structure of lactase was not changed by thermal stress. The glycan structure of lactase showed significant alterations after heat stress. Changes in the glycosylation structure affected physico-chemical properties of lactase.

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Cited by 4 publications
(2 citation statements)
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“…Upon completion of manufacture, the activity of the finished dosage forms was compared to the starting material. In all cases, the end products retained more than 98% (Matrix: 98.22 ± 1.71%, Layered: 98.59 ± 0.86%, n = 10-10), of their original activity, confirming that the appropriate production conditions were chosen according to our preliminary measurements [27].…”
Section: Physical Characterization Of Particlessupporting
confidence: 61%
“…Upon completion of manufacture, the activity of the finished dosage forms was compared to the starting material. In all cases, the end products retained more than 98% (Matrix: 98.22 ± 1.71%, Layered: 98.59 ± 0.86%, n = 10-10), of their original activity, confirming that the appropriate production conditions were chosen according to our preliminary measurements [27].…”
Section: Physical Characterization Of Particlessupporting
confidence: 61%
“…Quantitative mass spectrometric analysis of the glycans shows a significant difference for some sugar moieties due to high temperature. We can assume that structural changes in the higher order structural levels of the protein or within the glycosylation structures might be responsible for decrease of activity [4].…”
Section: Resultsmentioning
confidence: 99%