Abstract：
:A polygalacturonase with a molecular mass of 74 kDa, an isoelectric point around pH 4.2 and pH--and temperature optima of 3.9 and 50 degrees C, respectively, was purified from a culture fluid of Penicillium frequentans. The enzyme was characterized as an exo-alpha-1,4-polygalacturonase (exo-PG I). Km and Vmax for sodium polypectate hydrolysis were 0.68 g/l and 596.8 U x mg(-1), respectively. The enzyme, a glycoprotein with a carbohydrate content of 81%, is probably the main pectinase of Penicillium frequentans responsible for cleaving monomer units from the non-reducing end of pectin.
journal_name
Microbiol Resjournal_title
Microbiological researchauthors
dos Santos Cunha Chellegatti MA,Fonseca MJ,Said Sdoi
10.1078/0944-5013-00127subject
Has Abstractpub_date
2002-01-01 00:00:00pages
19-24issue
1eissn
0944-5013issn
1618-0623journal_volume
157pub_type
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