Evidence map›Paper›PMID 40232580›Full record

ArticleWorld journal of microbiology & biotechnology2025

Surface display of aspartate ammonia-lyase from Lactobacillus paracasei on Pichia pastoris.

Chen-Chi Chang, Yi-Hao Huang, Hua-Kun Fu, Kai-Wei Chang, Shih-Hsuan Chen, Yu-Ting Yu, Xin-Ying Lau, Jhih-Ying Ciou, He-Yuan Hsieh, Yung-Ju Chen and 1 more

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Article in World journal of microbiology & biotechnology, 2025. 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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0citing papers in PubMed
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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Chen-Chi ChangDepartment of Laboratory Medicine, Taipei City Hospital Heping Fuyou Branch, Taipei, 100027, Taiwan.
Yi-Hao HuangDepartment of Food Science, College of Agriculture and Health, Tunghai University, Taichung, 407224, Taiwan.
Hua-Kun FuDepartment of Food Science, College of Agriculture and Health, Tunghai University, Taichung, 407224, Taiwan.
Kai-Wei ChangDepartment of Food Science, College of Agriculture and Health, Tunghai University, Taichung, 407224, Taiwan.
Shih-Hsuan ChenDepartment of Food Science, College of Agriculture and Health, Tunghai University, Taichung, 407224, Taiwan.
Yu-Ting YuDepartment of Food Science, College of Agriculture and Health, Tunghai University, Taichung, 407224, Taiwan.
Xin-Ying LauDepartment of Biotechnology, UCSI University, 56000, Kuala Lumpur, Malaysia.
Jhih-Ying CiouDepartment of Food Science, College of Agriculture and Health, Tunghai University, Taichung, 407224, Taiwan.
He-Yuan HsiehDepartment of Radiation Oncology, Taichung Veteran General Hospital, Taichung, 407219, Taiwan.
Yung-Ju ChenDepartment of Food Science, College of Agriculture and Health, Tunghai University, Taichung, 407224, Taiwan.
Lu-Sheng HsiehDepartment of Food Science, College of Agriculture and Health, Tunghai University, Taichung, 407224, Taiwan. lshsieh@thu.edu.tw.

Funding

National Science and Technology Council, Taiwan NSTC 113-2313-B-029-002-MY3National Science and Technology Council, Taiwan NSTC 113-2622-E-029-005Taipei City Hospital Heping-Fuyou Branch TPCH-113-28
6 · The paper itself

Abstract

This study explores the surface display of Lactobacillus paracasei aspartate ammonia-lyase (LpAAL) on Pichia pastoris using glycosylphosphatidylinositol (GPI) anchoring technology. LpAAL, an enzyme with broad substrate specificity, has significant potential in various industries, including food, pharmaceuticals, and cosmetics, due to its ability to catalyze the conversion of L-aspartate into fumarate and other related reactions. The surface-displayed LpAAL on yeast (yLpAAL) demonstrated improved stability, especially under high temperature and alkaline conditions, making it suitable for industrial processes that demand robust and stable enzymes. Kinetic analysis revealed a slight increase in K

Indexed as

Aspartate Ammonia-LyaseCell Surface Display TechniquesLacticaseibacillus paracaseiPichiaAspartic AcidEnzyme StabilityKineticsRecombinant ProteinsSaccharomycetalesSubstrate SpecificityTemperatureAspartate Ammonia-LyaseAspartic AcidRecombinant ProteinsAspartate ammonia-lyaseGlycosylphosphatidylinositol (GPI) anchorLactobacillus paracaseiPichia pastorisSurface display

Identifiers

PMID40232580

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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.