Bioprocessing and Screening of Indigenous Wastes for Hyper Production of Fungal Lipase

Author:

Ali Usman1,Anwar Zahid1,Hasan Shoaib1ORCID,Zafar Muddassar1,Ain Noor ul1,Afzal Fareed2,Khalid Waseem3ORCID,Rahim Muhammad Abdul2ORCID,Mrabti Hanae Naceiri4,AL-Farga Ammar5ORCID,Eljeam Hamdi Abdel Rasool Abdelsamad6

Affiliation:

1. Department of Biochemistry and Biotechnology, University of Gujrat, Gujrat 50700, Pakistan

2. Department of Food Science, Faculty of Life Sciences, Government College University, Faisalabad 38000, Pakistan

3. University Institute of Food Science and Technology, The University of Lahore, Lahore 54000, Pakistan

4. High Institute of Nursing Professions and Health Techniques of Casablanca, Casablanca 20260, Morocco

5. Department of Biochemistry, College of Science, University of Jeddah, Jeddah 21577, Saudi Arabia

6. Department of English, College of Science and Arts, King Khalid University, Abha 61421, Saudi Arabia

Abstract

Background: Lipase is one of the most important enzymes produced from microbial fermentation. Agricultural wastes are a good source of enzyme production because they are cost-effective and production rates are also higher. Method: In this study, eight lignolitic substrates were screened for lipase production. Results: Out of these substrates, guava leaves showed maximum activity of 9.1 U/mL from Aspergillus niger by using the solid-state fermentation method. Various factors such as temperature, pH, incubation period, moisture content, inoculum size, and substrate size that influence the growth of fungi were optimized by response surface methodology (RSM), and then characterization was performed. When all physical and nutritional parameters were optimized by RSM, the maximum lipase activity obtained was 12.52 U/mL after 4 days of incubation, at pH 8, 40 °C temperature, 3 mL inoculum size, 20% moisture content, and 6 g substrate concentration. The enzyme was partially purified through 70% ammonium sulfate precipitation. After purification, it showed 34.291 U/mg enzyme activity, increasing the purification fold to 1.3. The enzyme was then further purified by dialysis, and the purification fold increased to 1.83 having enzyme activity of 48.03 U/mg. Furthermore, activity was increased to 132.72 U/mg after column chromatography. A purification fold of 5.07 was obtained after all purification steps.

Funder

King Khalid University

Publisher

MDPI AG

Subject

Physical and Theoretical Chemistry,Catalysis,General Environmental Science

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