Research Article Production of Glucoamylase from Novel Strain of Alternaria Alternata under Solid State Fermentation Durr-e- Nayab , 1 Shamim Akhtar , 1 Nazneen Bangash , 2 Waqar-un- Nisa, 3 Malik Tahir Hayat , 4 Awais Zulfiqar , 5 Mubashar Niaz , 6 Abdul Qayyum , 7 Asad Syed , 8 Ali H. Bahkali, 8 and Abdallah M. Elgorban 8 1 Department of Botany, University of Gujrat, Pakistan 2 Department of Biosciences, COMSATS University, Islamabad, Pakistan 3 International Islamic University, H-10 Islamabad, Pakistan 4 Department of Environmental Sciences, COMSATS University, Abbottabad Campus, Islamabad, Pakistan 5 Brimbank City Council, P.O. Box 70 Sunshine, Victoria 3020, Australia 6 Atlas Environmental Laboratories, Suite 1503, Street 36 West, Manhattan, New York 10018, USA 7 Department of Agronomy, The University of Haripur, Haripur 22620, Pakistan 8 Department of Botany and Microbiology, College of Science, King Saud University, P.O. 2455, Riyadh 11451, Saudi Arabia Correspondence should be addressed to Shamim Akhtar; shamim2bot@gmail.com Received 5 April 2022; Revised 11 August 2022; Accepted 24 September 2022; Published 27 October 2022 Academic Editor: Aqeel Ahmad Copyright © 2022 Durr-e- Nayab et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Glucoamylase has an essential role as biocatalyst in various important industries of Pakistan. It is synthesized by using various fungal and bacterial strains, and different ecocultural conditions are applied under solid substrate fermentation method (SSF) to get the highest yield of glucoamylase. Alternaria alternata is an important fungus that can grow on industrial raw material like wheat bran, dried potato powder, tea leaves, rice husk, and sugar cane peel which are used as substrate. Among all, dried potato powder (10g) proved the best fermentation media for growth of fungal strain as well as maximum glucoamylase producer. Moreover, several chemical and physical states were also explored through solid substrate fermentation technique on glucoamylase yield. The highest glucoamylase production was recorded after 72 hours incubation in incubation chamber with 10g raw substrate, 1ml inoculum spore solution, 30 ° C temperature, and 5 pH. Further, phosphate buffer (5 pH) as moistening agent, 5% starch concentration and media additive as nitrogen (yeast extract), and carbon source (maltose) were screened for maximum glucoamylase titer (17:3±0:05 a° U/ml/min) and the highest specific activity (39.2U/mg). These cultural conditions were most appropriate for growth of A. alternata on solid media and production of highest glucoamylase under solid state fermentation procedure that could be utilized for commercial synthesis of glucoamylase. 1. Introduction Enzymes are globular proteins that are used to speed up the various biochemical reactions. All the metabolic reactions are catalyzed due to the presence of enzymes in the body. There are a lot of enzymes that have attributes at industrial levels, such as in paper sizing, fabric, pharmaceutical, soap, and fermentation industry. Glucoamylase (α-1,4-glucan glucohydrolase, amyloglucosidase, EC 3.2.1.3) as a catalyst is used in food industry, textile industry, and detergent industry to mediate the industrial process without being used in the whole practice [1]. Glucoamylase has the ability to convert starch into the end product of β-D-glucose by breaking 1-4 glycosidic or 1-6 glycosidic linkages from non-reducing ends of oligo and polysaccharides chains. This multidomain glycoprotein comprises of about 640 amino acids. The larger catalytic domain (CD), that is, the N- terminal part of the enzyme, contains 1-470 amino acids while the starch binding domain, that is, C-terminal part, having 509-640 amino acids. Both domains of glucoamylase Hindawi BioMed Research International Volume 2022, Article ID 2943790, 9 pages https://doi.org/10.1155/2022/2943790