Isolation of Sp. A5.3 Strain with Keratinolytic Activity

Overview

Journal Biology (Basel)

Publisher MDPI

Specialty Biology

Date 2022 Feb 25

PMID 35205110

Authors

Saniya Aktayeva

Kairat Baltin

Assel Kiribayeva

Zhiger Akishev

Dmitriy Silayev

Yerlan Ramankulov

Bekbolat Khassenov

Affiliations

Soon will be listed here.

Abstract

Environmental safety and economic factors necessitate a search for new ways of processing poultry farm feathers, which are 90% β-keratin and can be used as a cheap source of amino acids and peptones. In this study, feather-decomposing bacteria were isolated from a site of accumulation of rotten feathers and identified as . Among them, the sp. A5.3 isolate showed the best keratinolytic properties. Scanning electron microscopy indicated that sp. A5.3 cells closely adhere to the feather surface while degrading the feather. It was found that sp. A5.3 secretes thermostable alkaline proteolytic and keratinolytic enzymes. Zymographic analysis of the enzymatic extract toward bovine serum albumin, casein, gelatin, and β-keratin revealed the presence of proteases and keratinases with molecular weights 20-250 kDa. The proteolytic and keratinolytic enzymes predominantly belong to the serine protease family. Proteome analysis of the secreted proteins by nano-HPLC coupled with Q-TOF mass spectrometry identified 154 proteins, 13 of which are proteases and peptidases. Thus, strain sp. A5.3 holds great promise for use in feather-processing technologies and as a source of proteases and keratinases.

Citing Articles

High keratinase and other types of hydrolase activity of the new strain of Bacillus paralicheniformis.

Aktayeva S, Khassenov B PLoS One. 2024; 19(10):e0312679.

PMID: 39453952 PMC: 11508186. DOI: 10.1371/journal.pone.0312679.

A Comparative Transcriptome Analysis Unveils the Mechanisms of Response in Feather Degradation by Gxun-7.

Song C, Liu R, Yin D, Xie C, Liang Y, Yang D Microorganisms. 2024; 12(4).

PMID: 38674785 PMC: 11052024. DOI: 10.3390/microorganisms12040841.

An impact of N-glycosylation on biochemical properties of a recombinant α-amylase from .

Kiribayeva A, Silayev D, Akishev Z, Baltin K, Aktayeva S, Ramankulov Y Heliyon. 2024; 10(6):e28064.

PMID: 38515717 PMC: 10956057. DOI: 10.1016/j.heliyon.2024.e28064.

Genome sequence and assembly of the amylolytic Bacillus licheniformis T5 strain isolated from Kazakhstan soil.

Mussakhmetov A, Kiribayeva A, Daniyarov A, Bulashev A, Kairov U, Khassenov B BMC Genom Data. 2024; 25(1):3.

PMID: 38166625 PMC: 10759562. DOI: 10.1186/s12863-023-01177-8.

Insights into the keratin efficient degradation mechanism mediated by Bacillus sp. CN2 based on integrating functional degradomics.

Lai Y, Wu X, Zheng X, Li W, Wang L Biotechnol Biofuels Bioprod. 2023; 16(1):59.

PMID: 37016453 PMC: 10071666. DOI: 10.1186/s13068-023-02308-0.

References

Taskin M, Kurbanoglu E . Evaluation of waste chicken feathers as peptone source for bacterial growth. J Appl Microbiol. 2011; 111(4):826-34. DOI: 10.1111/j.1365-2672.2011.05103.x. View

Schallmey M, Singh A, Ward O . Developments in the use of Bacillus species for industrial production. Can J Microbiol. 2004; 50(1):1-17. DOI: 10.1139/w03-076. View

Khardenavis A, Kapley A, Purohit H . Processing of poultry feathers by alkaline keratin hydrolyzing enzyme from Serratia sp. HPC 1383. Waste Manag. 2008; 29(4):1409-15. DOI: 10.1016/j.wasman.2008.10.009. View

Gupta R, Ramnani P . Microbial keratinases and their prospective applications: an overview. Appl Microbiol Biotechnol. 2006; 70(1):21-33. DOI: 10.1007/s00253-005-0239-8. View

Prakash P, Jayalakshmi S, Sreeramulu K . Purification and characterization of extreme alkaline, thermostable keratinase, and keratin disulfide reductase produced by Bacillus halodurans PPKS-2. Appl Microbiol Biotechnol. 2010; 87(2):625-33. DOI: 10.1007/s00253-010-2499-1. View

Ganesh Kumar A, Swarnalatha S, Gayathri S, Nagesh N, Sekaran G . Characterization of an alkaline active-thiol forming extracellular serine keratinase by the newly isolated Bacillus pumilus. J Appl Microbiol. 2007; 104(2):411-9. DOI: 10.1111/j.1365-2672.2007.03564.x. View

Moridshahi R, Bahreini M, Sharifmoghaddam M, Asoodeh A . Biochemical characterization of an alkaline surfactant-stable keratinase from a new keratinase producer, Bacillus zhangzhouensis. Extremophiles. 2020; 24(5):693-704. DOI: 10.1007/s00792-020-01187-9. View

Mitsuiki S, Sakai M, Moriyama Y, Goto M, Furukawa K . Purification and some properties of a keratinolytic enzyme from an alkaliphilic Nocardiopsis sp. TOA-1. Biosci Biotechnol Biochem. 2002; 66(1):164-7. DOI: 10.1271/bbb.66.164. View

Lin X, Lee C, Casale E, Shih J . Purification and Characterization of a Keratinase from a Feather-Degrading Bacillus licheniformis Strain. Appl Environ Microbiol. 1992; 58(10):3271-5. PMC: 183090. DOI: 10.1128/aem.58.10.3271-3275.1992. View

10.

Verma A, Singh H, Anwar S, Chattopadhyay A, Tiwari K, Kaur S . Microbial keratinases: industrial enzymes with waste management potential. Crit Rev Biotechnol. 2016; 37(4):476-491. DOI: 10.1080/07388551.2016.1185388. View

11.

Gupta R, Sharma R, Beg Q . Revisiting microbial keratinases: next generation proteases for sustainable biotechnology. Crit Rev Biotechnol. 2012; 33(2):216-28. DOI: 10.3109/07388551.2012.685051. View

12.

Dalmaso G, Lage C, Mazotto A, de Souza Dias E, Caldas L, Ferreira D . Extracellular peptidases from Deinococcus radiodurans. Extremophiles. 2015; 19(5):989-99. DOI: 10.1007/s00792-015-0773-y. View

13.

TOMARELLI R, CHARNEY J, HARDING M . The use of azoalbumin as a substrate in the colorimetric determination or peptic and tryptic activity. J Lab Clin Med. 1949; 34(3):428-33. View

14.

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

15.

Tork S, Shahein Y, El-Hakim A, Abdel-Aty A, Aly M . Production and characterization of thermostable metallo-keratinase from newly isolated Bacillus subtilis NRC 3. Int J Biol Macromol. 2013; 55:169-75. DOI: 10.1016/j.ijbiomac.2013.01.002. View

16.

Gopinath S, Anbu P, Lakshmipriya T, Tang T, Chen Y, Hashim U . Biotechnological Aspects and Perspective of Microbial Keratinase Production. Biomed Res Int. 2015; 2015:140726. PMC: 4477050. DOI: 10.1155/2015/140726. View

17.

Akpor O, Odesola D, Thomas R, Oluba O . Chicken feather hydrolysate as alternative peptone source for microbial cultivation. F1000Res. 2019; 7:1918. PMC: 6707403. DOI: 10.12688/f1000research.17134.3. View

18.

Bandegan A, Kiarie E, Payne R, Crow G, Guenter W, Nyachoti C . Standardized ileal amino acid digestibility in dry-extruded expelled soybean meal, extruded canola seed-pea, feather meal, and poultry by-product meal for broiler chickens. Poult Sci. 2010; 89(12):2626-33. DOI: 10.3382/ps.2010-00757. View

19.

Wani Lako J, Yengkopiong J, Stafford W, Tuffin M, Cowan D . Cloning, expression and characterization of thermostable YdaP from Bacillus licheniformis 9A. Acta Biochim Pol. 2018; 65(1):59-66. DOI: 10.18388/abp.2017_1499. View

20.

Bhari R, Kaur M, Singh R . Thermostable and halotolerant keratinase from Bacillus aerius NSMk2 with remarkable dehairing and laundary applications. J Basic Microbiol. 2019; 59(6):555-568. DOI: 10.1002/jobm.201900001. View