@article{mbs:/content/journal/micro/10.1099/00221287-136-5-913, author = "Fagerström, Richard and Vainio, Arja and Suoranta, Kari and Pakula, Tiina and Kalkkinen, Nisse and Torkkeli, Helena", title = "Comparison of two glucoamylases from Hormoconis resinae", journal= "Microbiology", year = "1990", volume = "136", number = "5", pages = "913-920", doi = "https://doi.org/10.1099/00221287-136-5-913", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-136-5-913", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Two extracellular glucoamylases (EC 3.2.1.3), glucoamylase P and glucoamylase S, were purified to homogeneity from the culture medium of Hormoconis resinae (ATCC 20495; formerly Cladosporium resinae) by a new method. Their apparent molecular masses (71 kDa glucoamylase P; 78 kDa glucoamylase S) and catalytic properties agreed well with those previously reported in the literature. Heat inactivation studies suggested that the high debranching (1,6-glycosidic) activity of glucoamylase P preparations (measured with pullulan) may reside in the same protein molecule as its 1,4-glycosidic activity (measured with soluble starch). Although glucoamylase S had virtually no debranching activity, it cross-reacted with polyclonal antibodies raised against glucoamylase P, and the two enzymes had very similar amino acid compositions. However, peptide mapping and amino-terminal sequencing studies of the peptides showed that the two enzymes have different sequences and must be encoded by different genes.", }