Utilization of wild Cressa cretica biomass for pectinase production from a halo‐thermotolerant bacterium

Author:

Hassan Masooma1,Ejaz Uroosa2,Rashid Rozina3,Moin Syed Faraz4,Gulzar Salman5,Sohail Muhammad1ORCID,Hasan Khwaja Ali6,Alswat Amal S.7,El‐Bahy Zeinhom M.8

Affiliation:

1. Department of Microbiology University of Karachi Karachi Pakistan

2. Department of Biosciences, Faculty of Life Sciences Shaheed Zulfikar Ali Bhutto Institute of Science and Technology (SZABIST) Karachi Pakistan

3. Department of Microbiology University of Balochistan Balochistan Pakistan

4. Dr. Zafar H Zaidi Center for Proteomics (Formely National Center for Proteomics) University of Karachi Karach Pakistan

5. Dr Muhammad Ajmal Khan Institute of Sustainable of Halophytes Utilization University of Karachi Karachi Pakistan

6. Molecular and Structural Biology Research Unit, Department of Biochemistry University of Karachi Karachi Pakistan

7. Department of Biotechnology, College of Science Taif University Taif Saudi Arabia

8. Department of Chemistry, Faculty of Science Al‐Azhar University, Nasr City Cairo Egypt

Abstract

AbstractHalophytes are the native inhabitants of saline environment. Their biomass can be considered as a potential substrate for the production of microbial enzymes. This study was intended at feasible utilization of a halophytic biomass, Cressia cretica, for pectinase production using a halo‐ and thermo‐tolerant bacterium, Bacillus vallismortis MH 10. The data from fractionation of the C. cretica biomass revealed presence of 17% pectin in this wild biomass. Seven different factors (temperature, agitation, pH, inoculum size, peptone concentration, substrate concentration, and incubation time) affecting pectinase production using C. cretica were assessed through a statistical tool, Plackett–Burman design. Consequently, two significant factors (incubation time and peptone concentration) were optimized using the central composite design. The strain produced 20 IU mL−1 of pectinase after 24 h under optimized conditions. The enzyme production kinetics data also confirmed that 24 h is the most suitable cultivation period for pectinase production. Fourier transform infrared spectroscopy and scanning electron microscopy of C. cretica biomass ascertained utilization of pectin and structural changes after fermentation. The purification of pectinase by using DEAE column yielded specific activity and purification fold of 88.26 IU mg−1 and 3.2, respectively. The purified pectinase had a molecular weight of >65 kDa. This study offers prospects of large‐scale production of pectinase by halotolerant strain in the presence of economical and locally grown substrate that makes the enzyme valuable for various industrial operations.

Publisher

Wiley

Subject

Molecular Medicine,Applied Microbiology and Biotechnology,General Medicine

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