کد مقاله کد نشریه سال انتشار مقاله انگلیسی ترجمه فارسی نسخه تمام متن
1172678 1491340 2016 6 صفحه PDF سفارش دهید دانلود کنید
عنوان انگلیسی مقاله ISI
Adding an appropriate amino acid during crosslinking results in more stable crosslinked enzyme aggregates
ترجمه فارسی عنوان
افزودن یک اسید آمینه مناسب در طول اتصال به اسید، باعث افزایش پایدارتر آنزیم های متصل به یکدیگر می شود
کلمات کلیدی
آنزیم Crosslinked aggregates (CLEAs)؛ تثبیت آنزیم؛ آنزیم ها در حلال های آلی؛ آنزیم ها در مواد شوینده؛ لیپازها؛ SubtilisinCLEA، مجموعه ای از آنزیم crosslinked؛ BTEE، بنزویل تریروزین اتیل استر؛ TLL، Thermomyces lanuginosus لیپاز؛ HPLC، high-per
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی

Carrier free immobilization, especially crosslinked enzyme aggregates (CLEAs), has become an important design for biocatalysis in several areas. Adding amino acids during formation of CLEAs was found to give biocatalysts more stable at 55 °C and in the presence of 60% acetonitrile. The half-lives of CLEAs prepared with and without Arg addition were 21 and 15 h (subtilisin) and 4 and 1.6 h (α-chymotrypsin) at 55 °C, respectively. The corresponding half-lives during acetonitrile presence were 4.1 and 3.0 h (subtilisin) and 39 and 22 min (α-chymotrypsin), respectively. CLEAs made with Arg had higher percentages of alpha helix. CLEAs made by adding Lys, Ala, or Asp also were more stable. In the case of Thermomyces lanuginosus lipase (TLL), CLEA with Ala was even more stable than CLEA with Arg. The addition of a suitable amino acid, thus, enhances CLEA stabilities. The results are discussed in the light of earlier results on chemical modification of proteins and the observation that the Arg/Lys ratio is invariably high in the case of enzymes from thermophiles.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Analytical Biochemistry - Volume 507, 15 August 2016, Pages 27–32
نویسندگان
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