نتایج جستجو برای: pullulanase

تعداد نتایج: 277  

Journal: :International Journal of Biomedical Research 2011

Journal: :Journal of bacteriology 2009
Louise J Gourlay Isabella Santi Alfredo Pezzicoli Guido Grandi Marco Soriani Martino Bolognesi

The group B streptococcus type I pullulanase (SAP) is a class 13 glycoside hydrolase that is anchored to the bacterial cell surface via a conserved C-terminal anchoring motif and involved in alpha-glucan degradation. Recent in vitro functional studies have shown that SAP is immunogenic in humans and that anti-SAP sera derived from immunized animals impair both group A and group B streptococcus ...

Journal: :Journal of bacteriology 2007
Olivera Francetic Nienke Buddelmeijer Shawn Lewenza Carol A Kumamoto Anthony P Pugsley

The pseudopilin PulG is an essential component of the pullulanase-specific type II secretion system from Klebsiella oxytoca. PulG is the major subunit of a short, thin-filament pseudopilus, which presumably elongates and retracts in the periplasm, acting as a dynamic piston to promote pullulanase secretion. It has a signal sequence-like N-terminal segment that, according to studies with green a...

Journal: :IOP conference series 2023

Abstract Common enzymes used in starch modification include α-amylase, β-amylase, glucoamylase, isoamylase, and pullulanase. Botanical sources of are widely grains, beans, tubers. The is to change the lack native properties make desired physicochemical properties. Besides, can produce resistant (RS), which essential for health concerns. review aims provide information on enzymatic its effect ch...

Journal: :International Journal of Life-Sciences Scientific Research 2016

Journal: :Glycobiology 2011
Junji Noguchi Kimiko Chaen Nhuan Thi Vu Taiki Akasaka Hiroaki Shimada Takashi Nakashima Aiko Nishi Hikaru Satoh Toshiro Omori Yoshimitsu Kakuta Makoto Kimura

Starch-branching enzyme catalyzes the cleavage of α-1, 4-linkages and the subsequent transfer of α-1,4 glucan to form an α-1,6 branch point in amylopectin. Sequence analysis of the rice-branching enzyme I (BEI) indicated a modular structure in which the central α-amylase domain is flanked on each side by the N-terminal carbohydrate-binding module 48 and the α-amylase C-domain. We determined the...

Journal: :The Biochemical journal 1998
A Henker I Schindler A Renz E Beck

Purified pullulanase (starch-debranching enzyme, R-enzyme, EC 3.2.1. 41) from spinach (Spinacia oleracea L.) chloroplasts separated into at least seven individual enzymically active proteins (isomers, numbered 1-7) on isoelectric focusing or column chromatofocusing. At their isoelectric points (between pH 4.7 and 5.2) these forms were rather stable. At slightly alkaline pH, each converted into ...

Journal: :Applied and environmental microbiology 1985
H H Hyun J G Zeikus

Clostridium thermosulfurogenes, an anaerobic bacterium which ferments starch into ethanol at 62 degrees C, produced an active extracellular amylase and contained intracellular glucoamylase but not pullulanase activity. The extracellular amylase was purified 2.4-fold, and its general physicochemical and catalytic properties were examined. The extracellular amylase was characterized as a beta-amy...

Journal: :Applied and environmental microbiology 2006
Sinéad M Ryan Gerald F Fitzgerald Douwe van Sinderen

Forty-two bifidobacterial strains were screened for alpha-amylase and/or pullulanase activity by investigating their capacities to utilize starch, amylopectin, or pullulan. Of the 42 bifidobacterial strains tested, 19 were capable of degrading potato starch. Of these 19 strains, 11 were able to degrade starch and amylopectin, as well as pullulan. These 11 strains, which were shown to produce ex...

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