Evidence map›Paper›PMID 42159684›Full record

ArticleBioprocess and biosystems engineering2026

The optimization of thermostable recombinant α-amylase for efficient fabric desizing using response surface methodology and surface morphology analysis.

Krishnendu Mondal, Prayatna Sharma, Ishfaq Nabi Najar, Tanmoy Jana, Sudipta Samanta, Subhas Giri, Arijit Jana, Nagendra Thakur, Keshab Chandra Mondal

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Article in Bioprocess and biosystems engineering, 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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1 · What the graph read from it

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Krishnendu MondalDepartment of Microbiology, Vidyasagar University, Midnapore, West Bengal, 721102, India.
Prayatna SharmaDepartment of Microbiology, Sikkim University, Gangtok, Sikkim, 737102, India.
Ishfaq Nabi NajarSS Institute of Medical Science and Research Centre, Devanere, Karnataka, 577005, India.
Tanmoy JanaDepartment of Microbiology, Vidyasagar University, Midnapore, West Bengal, 721102, India.
Sudipta SamantaDepartment of Environmental Studies, Vidyasagar University, Midnapore, West Bengal, 721102, India.
Subhas GiriDepartment of Microbiology, Vidyasagar University, Midnapore, West Bengal, 721102, India.
Arijit JanaDepartment of Microbiology, Vidyasagar University, Midnapore, West Bengal, 721102, India.
Nagendra ThakurDepartment of Microbiology, Sikkim University, Gangtok, Sikkim, 737102, India.
Keshab Chandra MondalDepartment of Microbiology, Vidyasagar University, Midnapore, West Bengal, 721102, India. mondalkc@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A thermostable α-amylase gene (Amyk4) from Bacillus licheniformis k4cm (or similar thermophilic Bacillus), isolated from a Himalayan hot spring in Sikkim, India, was successfully cloned and expressed in Escherichia coli BL21(DE3). The purified recombinant α-amylase (Amyk4) exhibited maximal activity (153.2 ± 1.05 U/mL) at 80 °C and pH 6.0, with a half-life of 30.39 h and enhanced stability in the presence of Ca²⁺, indicating its suitability for high-temperature industrial applications. The cotton fabric desizing was optimized using Response Surface Methodology (Box-Behnken design). Optimal conditions (pH 6.9, 80 °C, enzyme dosage of 190 U/g, and treatment time of 95 min) achieved a TEGEWA rating of 8 and a weight loss of 6.6%. The quadratic model showed strong statistical validity (R² = 0.9205 for TEGEWA and 0.9168 for weight loss). Among the evaluated variables, pH, enzyme concentration, and reaction time significantly influenced desizing efficiency. Non-ionic surfactants slightly improved desizing efficiency compared to ionic surfactants. Scanning electron microscopy (SEM) analysis confirmed effective starch removal without fibre damage. These findings demonstrate the potential of recombinant Amyk4 as a thermostable, eco-friendly candidate for sustainable textile desizing applications.

Indexed as

alpha-AmylasesBacillus licheniformisBacterial ProteinsCotton FiberEnzyme StabilityEscherichia coliHydrogen-Ion ConcentrationRecombinant Proteinsalpha-AmylasesBacterial ProteinsRecombinant ProteinsBox–Behnken designCotton desizingRecombinant expressionResponse surface methodologyThermostable α-amylase

Identifiers

PMID42159684

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