Abstract
The pullulanase (EC 3.2.1.41) of Bacillus acidopullulyticus was purified using anion exchange chromatography and preparative isoelectric focusing. The purified preparation migrated as a single protein band upon SDS gel electrophoresis and its molecular weight was estimated to be 102,000. Two main activity bands having pl‐values 5.0 and 5.2 were detected by analytical isoelectric focusing. The enzyme was purified 4‐fold with the yield 38% by this two‐step purification procedure. The purified pullulanase showed maximal activity at 50°C and pH 5 and was slightly activated by Ca2+. It was stable at 50°C but totally lost its activity at 60ºC in one hour. This purified pullulanase efficiently hydrolyzed the α‐1,6‐glucosidic bonds of pullulan and gelatinized starch.
| Original language | English |
|---|---|
| Pages (from-to) | 477 - 482 |
| Number of pages | 6 |
| Journal | Stärke |
| Volume | 43 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 1991 |
| MoE publication type | A1 Journal article-refereed |
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Purification and characterization of Bacillus acidopullulyticus pullulanase for enzymatic starch modification. / Lappalainen, Arja (Corresponding Author); Niku-Paavola, Marja-Leena; Suortti, Tapani; Poutanen, Kaisa.
In: Stärke, Vol. 43, No. 12, 1991, p. 477 - 482.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Purification and characterization of Bacillus acidopullulyticus pullulanase for enzymatic starch modification
AU - Lappalainen, Arja
AU - Niku-Paavola, Marja-Leena
AU - Suortti, Tapani
AU - Poutanen, Kaisa
N1 - Project code: ELI40050
PY - 1991
Y1 - 1991
N2 - The pullulanase (EC 3.2.1.41) of Bacillus acidopullulyticus was purified using anion exchange chromatography and preparative isoelectric focusing. The purified preparation migrated as a single protein band upon SDS gel electrophoresis and its molecular weight was estimated to be 102,000. Two main activity bands having pl‐values 5.0 and 5.2 were detected by analytical isoelectric focusing. The enzyme was purified 4‐fold with the yield 38% by this two‐step purification procedure. The purified pullulanase showed maximal activity at 50°C and pH 5 and was slightly activated by Ca2+. It was stable at 50°C but totally lost its activity at 60ºC in one hour. This purified pullulanase efficiently hydrolyzed the α‐1,6‐glucosidic bonds of pullulan and gelatinized starch.
AB - The pullulanase (EC 3.2.1.41) of Bacillus acidopullulyticus was purified using anion exchange chromatography and preparative isoelectric focusing. The purified preparation migrated as a single protein band upon SDS gel electrophoresis and its molecular weight was estimated to be 102,000. Two main activity bands having pl‐values 5.0 and 5.2 were detected by analytical isoelectric focusing. The enzyme was purified 4‐fold with the yield 38% by this two‐step purification procedure. The purified pullulanase showed maximal activity at 50°C and pH 5 and was slightly activated by Ca2+. It was stable at 50°C but totally lost its activity at 60ºC in one hour. This purified pullulanase efficiently hydrolyzed the α‐1,6‐glucosidic bonds of pullulan and gelatinized starch.
U2 - 10.1002/star.19910431207
DO - 10.1002/star.19910431207
M3 - Article
VL - 43
SP - 477
EP - 482
JO - Starch
JF - Starch
SN - 2192-4236
IS - 12
ER -