Evidence map›Paper›PMID 41528997›Full record

ArticlePloS one2026

Genome-wide identification and functional characterization of alpha-amylase genes in Litopenaeus vannamei.

Jingxuan Liang, Hao Yang, Guiling Tan, Ting Chen, Lvping Zhang, Wenjie Pan, Jiayue Yin, Bo Ma, Jianfeng Xu, Jiquan Zhang and 4 more

Abstract read
In one paragraph

Article in PloS one, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

1 citing paper in PubMed.

  1. Article
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

14 authors.

Jingxuan LiangState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.
Hao YangLaboratory of Zoological Systematics and Application of Hebei Province, College of Life Sciences, Hebei University, Baoding, China.
Guiling TanLaboratory of Zoological Systematics and Application of Hebei Province, College of Life Sciences, Hebei University, Baoding, China.
Ting ChenState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.
Lvping ZhangState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.
Wenjie PanState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.
Jiayue YinState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.
Bo MaState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.
Jianfeng XuState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.
Jiquan ZhangLaboratory of Zoological Systematics and Application of Hebei Province, College of Life Sciences, Hebei University, Baoding, China.
Peng LuoState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.ORCID https://orcid.org/0000-0002-2106-6186
Peiming ZhengGuangdong Jinyang Biotechnology Co., Ltd, Maoming, China.
Chaoqun HuState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.
Chunhua RenState Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.ORCID https://orcid.org/0000-0002-7458-1923

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alpha-amylase is a key enzyme involved in carbohydrate hydrolysis and food digestion in animals. However, its molecular characteristics and functions remain poorly understood in the economically important Pacific white shrimp, Litopenaeus vannamei. Through comparative genomic analysis, this study revealed that the α-amylase (Amy) gene family has undergone an expansion in arthropods, particularly crustaceans, while retaining highly conserved catalytic domains. Six Amy genes were identified in L. vannamei. Their expression patterns across tissues and developmental stages revealed predominant transcription in the hepatopancreas, with significant upregulation during periods of high energy demand, such as zoeal feeding and pre-molting. Among these genes, Lv-Amy (XP_027225605.1) exhibited the highest expression level. Quantitative real-time PCR (qPCR) and fluorescence in situ hybridization (FISH) further characterized the tissue distribution and cellular localization of Lv-Amy. Structurally, Lv-Amy displays a typical (β/α)₈ TIM barrel conformation and two conserved calcium-binding sites. The recombinant Lv-Amy protein was produced in an E. coli expression system and its enzymatic properties were characterized. Maximal activity of the recombinant Lv-Amy protein was observed at pH 7.5 and 25°C, while activity remained above 50% of the maximum within pH 7.0-8.0 and 20-45°C, indicating that Lv-Amy can function efficiently under environmental conditions characteristic of the tropical marine habitat of L. vannamei. In summary, this study provides new insights into the molecular characteristics and functions of α-amylase in L. vannamei, suggesting that Lv-Amy plays an important role in digestion and offering a reference of stage-specific nutritional formulation for this species.

Indexed as

alpha-AmylasesPenaeidaeAmino Acid SequenceAnimalsCloning, MolecularGene Expression Regulation, EnzymologicMolecular Sequence DataPhylogenyalpha-Amylases

Identifiers

PMID41528997
PMCPMC12798967

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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.