• Food Science and Biotechnology
• /
• v.18 no.3
• /
• pp.732-738
• /
• 2009

An acidic polygalacturonase (PG) from Aspergillus kawachii was produced by solid state fermentation employing a polyurethane foam support. The conditions used for the production of acidic PG were particle size of support (0.6 or 500 $mm^3$) and fermentation time. From the factors studied, the particle size had important influence on enzyme production. The best conditions for acidic PG production were $0.6\;mm^3$ particle size, 18 hr at $30^{\circ}C$ and initial pH of 5.0. In addition, pectin was extracted from citrus pomaces (grapefruit, lime, and tangerine) by acidic PG at $50^{\circ}C$ for 24 hr with citric acid solution. Infrared spectroscopy showed that lime pomace had more high-methoxylated (65%) endogenous pectin than was obtained than from grapefruit or tangerine pomaces. The enzymatically extracted pectin yield in dry basis (d.b.) for grapefruit and lime pectins were 6.95 and 4.25%, respectively. The citric acid solution alone also contributed to pectin extraction from citrus pomaces (7-9%, d.b.). Limited pectin extraction by acidic PG from tangerine pomace was most likely due to the presence of low-methoxylated endogenous pectin. The enzymatic method for pectin extraction using acidic PG from A. kawachii is a promising technique for releasing highly polymerized pectic substances from high-methoxylated lime or grapefruit pomaces.

• Journal of Microbiology and Biotechnology
• /
• v.26 no.6
• /
• pp.989-998
• /
• 2016

Acidic endo-polygalacturonases are the major part of pectinase preparations and extensively applied in the clarification of fruits juice, vegetables extracts, and wines. However, most of the reported fungal endo-polygalacturonases are active and stable under narrow pH range and low temperatures. In this study, an acidic endo-polygalacturonase (EPG4) was purified and characterized from a mutant strain of Penicillium oxalicum. The N-terminal amino acid sequence of EPG4 (ATTCTFSGSNGAASASKSQT) was different from those of reported endo-polygalacturonases. EPG4 displayed optimal pH and temperature at 5.0 and 60-70℃ towards polygalacturonic acid (PGA), respectively, and was notably stable at pH 2.2-7.0. When tested against pectins, EPG4 showed enzyme activity over a broad acidic pH range (>15.0% activity at pH 2.2-6.0 towards citrus pectin; and >26.6% activity at pH 2.2-7.0 towards apple pectin). The K_m and V_max values were determined as 1.27 mg/ml and 5,504.6 U/mg, respectively. The enzyme hydrolyzed PGA in endo-manner, releasing oligo-galacturonates from PGA, as determined by TLC. Addition of EPG4 (3.6 U/ml) significantly reduced the viscosity (by 42.4%) and increased the light transmittance (by 29.5%) of the papaya pulp, and increased the recovery (by 24.4%) of the papaya extraction. All of these properties make the enzyme a potential application in the beverage industry.