Purification and characterization of Bacillus acidopullulyticus pullulanase for enzymatic starch modification

Arja Lappalainen (Corresponding Author), Marja-Leena Niku-Paavola, Tapani Suortti, Kaisa Poutanen

Research output: Contribution to journalArticleScientificpeer-review

8 Citations (Scopus)

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 languageEnglish
Pages (from-to)477 - 482
Number of pages6
JournalStärke
Volume43
Issue number12
DOIs
Publication statusPublished - 1991
MoE publication typeA1 Journal article-refereed

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Bacillus acidopullulyticus
pullulanase
Bacilli
Starch
Bacillus
Purification
Isoelectric Focusing
starch
isoelectric focusing
pullulan
Chromatography
Electrophoresis
Anions
Molecular Weight
Gels
Molecular weight
gel electrophoresis
Enzymes
molecular weight
calcium

Cite this

Lappalainen, Arja ; Niku-Paavola, Marja-Leena ; Suortti, Tapani ; Poutanen, Kaisa. / Purification and characterization of Bacillus acidopullulyticus pullulanase for enzymatic starch modification. In: Stärke. 1991 ; Vol. 43, No. 12. pp. 477 - 482.
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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.",
author = "Arja Lappalainen and Marja-Leena Niku-Paavola and Tapani Suortti and Kaisa Poutanen",
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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 journalArticleScientificpeer-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

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VL - 43

SP - 477

EP - 482

JO - Starch

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SN - 2192-4236

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