کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4357483 | 1615869 | 2009 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and characterization of an exo-polygalacturonase from Pycnoporus sanguineus
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
علوم کشاورزی و بیولوژیک (عمومی)
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چکیده انگلیسی
The present work describes the purification and characterization of a novel extracellular polygalacturonase, PGase I, produced by Pycnoporus sanguineus when grown on citrus fruit pectin. This substrate gave enhanced enzyme production as compared to sucrose and lactose. PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product as determined by TLC and orcinol-sulphuric acid staining. Its capacity to hydrolyze digalacturonate identified PGase I as an exo-polygalacturonase. SDS-PAGE showed that PGase I is an N-glycosidated monomer. The enzyme has a molecular mass of 42 kDa, optimum pH 4.8 and stability between pH 3.8 and 8.0. A temperature optimum was observed at 50-60 °C, with some enzyme activity retained up to 80 °C. Its activation energy was 5.352 cal molâ1. PGase I showed a higher affinity towards PGA than citric pectin (Km = 0.55 ± 0.02 and 0.72 ± 0.02 mg mlâ1, respectively). Consequently, PGase I is an exo-PGase, EC 3.2.1.82.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Mycological Research - Volume 113, Issue 12, December 2009, Pages 1404-1410
Journal: Mycological Research - Volume 113, Issue 12, December 2009, Pages 1404-1410
نویسندگان
Emma N. Quiroga, Melina A. Sgariglia, César F. Molina, Diego A. Sampietro, José R. Soberón, Marta A. Vattuone,