Functional Dipeptide Production by Immobilized Enzyme on Yeast Cell Surface.

Sejin Geum, Seoyoung Lee, Sunghee Kim, Grace Evelina, Hosam Ki, Peng-Fei Xia, Yong-Su Jin, Soo Rin Kim

Abstract read

In one paragraph

Article in Journal of microbiology and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Sejin GeumSchool of Food Science and Biotechnology, Kyungpook National University, Daegu 41566, Republic of Korea.

Seoyoung LeeSchool of Food Science and Biotechnology, Kyungpook National University, Daegu 41566, Republic of Korea.

Sunghee KimSchool of Food Science and Biotechnology, Kyungpook National University, Daegu 41566, Republic of Korea.

Grace EvelinaSchool of Food Science and Biotechnology, Kyungpook National University, Daegu 41566, Republic of Korea.

Hosam KiMaterials Science Research Institute, LABIO Co., Ltd., Seoul 08501, Republic of Korea.

Peng-Fei XiaSchool of Environmental Science and Engineering, Shandong University, Qingdao 266237, P.R. China.

Yong-Su JinDepartment of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Soo Rin KimSchool of Food Science and Biotechnology, Kyungpook National University, Daegu 41566, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-Alanyl-L-glutamine (Ala-Gln) is a high-value dipeptide with superior stability, solubility, and bioavailability, underscoring its potential for nutritional supplementation. Compared with conventional chemical catalysis, whole-cell biocatalysts offer a more efficient, simpler, and environmentally friendly alternative for peptide synthesis. Among these, enzyme cell-surface immobilization systems enable the stable display of target enzymes on yeast cells, thereby enhancing enzyme stability while simplifying catalyst recovery and reuse, which is particularly advantageous for large-scale industrial applications. In this study, an engineered

Indexed as

AcyltransferasesDipeptidesEnzymes, ImmobilizedSaccharomyces cerevisiaeBiocatalysisEnzyme StabilityHydrogen-Ion ConcentrationAcyltransferasesalanylglutamineDipeptidesEnzymes, ImmobilizedImmobilized enzymeL-alanyl-L-glutamineSaccharomyces cerevisiaeWhole-cell biocatalystsα-Amino acid ester acyltransferase

Identifiers

PMID41814588

DOI10.4014/jmb.2512.12032

PMCPMC12989794

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.