کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8328435 1540205 2018 40 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Extraction, purification and characterization of low molecular weight Proline iminopeptidase from probiotic L. plantarum for meat tenderization
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Extraction, purification and characterization of low molecular weight Proline iminopeptidase from probiotic L. plantarum for meat tenderization
چکیده انگلیسی
Membrane bound proline iminopeptidase (PIP) from lactic acid bacteria (LAB) L. plantarum was extracted and purified using CM-sephadex, Sephadex G-100 and Q-sepharose column chromatography. PIP was purified with purification fold 7.13 and 33.5% yield. SDS-PAGE and MALDI-TOF revealed it as homodimer with molecular weight of 37.9 kDa and subunit of mass 18.9 kDa. Purified enzyme exhibited maximum activity at 45 °C and pH 7.0. Km and Vmax of purified PIP were 65 μM and 25.9 nm/min/ml respectively. Inhibition by PMSF confirmed it a serine protease. Metal ions and EDTA showed no effect on enzyme activity. The enzyme mainly hydrolysed Pro-4mβNA. The effectiveness of enzyme in purified form, membrane bound form and in combination with other enzymes to degrade collagen resulting in pharmaceutically significant collagen hydrolysates and in meat tenderization marks its industrial importance. There are very few PIPs are characterized from LAB, and therefore this study is industrially significant and brings some new knowledge into this area.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 109, 1 April 2018, Pages 651-663
نویسندگان
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