Evidence map›Paper›PMID 22179540›Full record

ArticleJournal of industrial microbiology & biotechnology2012

Gene cloning, expression, and biochemical characterization of an alkali-tolerant β-mannanase from Humicola insolens Y1.

Huiying Luo, Kun Wang, Huoqing Huang, Pengjun Shi, Peilong Yang, Bin Yao

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Article in Journal of industrial microbiology & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

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0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Review
  2. Applications of Microbial β-Mannanases.Frontiers in bioengineering and biotechnology · 2020
    Review
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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Huiying LuoKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun South Street, Beijing 100081, People's Republic of China.
Kun Wang
Huoqing Huang
Pengjun Shi
Peilong Yang
Bin Yao

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this article, we firstly report a highly alkali-tolerant fungal β-mannanase from Humicola insolens Y1. The full-length cDNA of the β-mannanase, designated as man5A, has an open reading frame of 1,233 bp that encodes a 411-amino acid polypeptide (Man5A) with a calculated molecular mass of 42.3 kDa. The deduced sequence of Man5A comprises a putative 20-residue signal peptide and a catalytic domain belonging to glycoside hydrolase family 5, and displays 61-85% identities with hypothetical proteins and 32-39% with experimentally verified fungal β-mannanases. Purified recombinant Man5A produced by Pichia pastoris has a specific activity of 1,122 U mg⁻¹ and exhibits optimal activity at pH 5.5 and 70°C. Distinct from other reported fungal β-mannanases, Man5A is highly alkali tolerant, exhibiting 45 and 36% of the maximal activity at pH 8.0 and 9.0, respectively, and more than 10% activity even at pH 10.0. Moreover, Man5A has excellent pH stability at pH 5.0-12.0 and is highly thermostable at 50°C. The higher frequency of alkaline amino acids (Arg and Lys), greater pKa values of the catalytic residues, and more positively charged residues on the surface of Man5A might be the causes. Man5A has strong resistance to various neutral and alkaline proteases, retaining more than 97% of the activity after proteolytic treatment for 1 h. The superior characteristics of Man5A make it more advantageous for the application in the kraft pulp industry.

Indexed as

Industrial MicrobiologyAscomycotabeta-MannosidaseCloning, MolecularHydrogen-Ion ConcentrationPichiaProtein Sorting SignalsRecombinant Proteinsbeta-MannosidaseProtein Sorting SignalsRecombinant Proteins

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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.