<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>23(1)</volume><submitter>Bechtel A</submitter><funding>Universität Hohenheim</funding><pubmed_abstract>&lt;h4>Background&lt;/h4>The β-galactosidase from Paenibacillus wynnii (β-gal-Pw) is a promising candidate for lactose hydrolysis in milk and dairy products, as it has a higher affinity for the substrate lactose (low K&lt;sub>M&lt;/sub> value) compared to industrially used β-galactosidases and is not inhibited by the hydrolysis-generated product D-galactose. However, β-gal-Pw must firstly be produced cost-effectively for any potential industrial application. Accordingly, the yeast Komagataella phaffii was chosen to investigate its feasibility to recombinantly produce β-gal-Pw since it is approved for the regulated production of food enzymes. The aim of this study was to find the most suitable way to produce the β-gal-Pw in K. phaffii either extracellularly or intracellularly.&lt;h4>Results&lt;/h4>Firstly, 1</pubmed_abstract><journal>Microbial cell factories</journal><pagination>263</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11452983</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Recombinant production of Paenibacillus wynnii β-galactosidase with Komagataella phaffii.</pubmed_title><pmcid>PMC11452983</pmcid><pubmed_authors>Hetzel F</pubmed_authors><pubmed_authors>Seitl I</pubmed_authors><pubmed_authors>Fischer L</pubmed_authors><pubmed_authors>Bechtel A</pubmed_authors><pubmed_authors>Keutgen M</pubmed_authors><pubmed_authors>Pross E</pubmed_authors></additional><is_claimable>false</is_claimable><name>Recombinant production of Paenibacillus wynnii β-galactosidase with Komagataella phaffii.</name><description>&lt;h4>Background&lt;/h4>The β-galactosidase from Paenibacillus wynnii (β-gal-Pw) is a promising candidate for lactose hydrolysis in milk and dairy products, as it has a higher affinity for the substrate lactose (low K&lt;sub>M&lt;/sub> value) compared to industrially used β-galactosidases and is not inhibited by the hydrolysis-generated product D-galactose. However, β-gal-Pw must firstly be produced cost-effectively for any potential industrial application. Accordingly, the yeast Komagataella phaffii was chosen to investigate its feasibility to recombinantly produce β-gal-Pw since it is approved for the regulated production of food enzymes. The aim of this study was to find the most suitable way to produce the β-gal-Pw in K. phaffii either extracellularly or intracellularly.&lt;h4>Results&lt;/h4>Firstly, 1</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Oct</publication><modification>2026-06-03T03:43:19.835Z</modification><creation>2025-04-06T22:28:35.785Z</creation></dates><accession>S-EPMC11452983</accession><cross_references><pubmed>39367390</pubmed><doi>10.1186/s12934-024-02544-5</doi></cross_references></HashMap>