Showing papers by "Tzi Bun Ng published in 2004"
TL;DR: The peptides and proteins secreted by fungi are reviewed in this article and various enzymes with applications in food industry, chemical production and the medical sector are reviewed.
148 citations
TL;DR: The peptide isolated from fruiting bodies of the mushroom Pleurotus eryngii inhibited mycelial growth in Fusarium oxysporum and Mycosphaerella arachidicola and demonstrated some similarity to the antifungal protein from the mushroom Lyophyllum shimeiji and little resemblance to thaumatin andThaumatin-like proteins.
124 citations
TL;DR: Out of the 12 species of bacteria tested, only Pseudomonas aeruginosa and Staphylococcus aureus were inhibited in growth by the ribonuclease.
83 citations
TL;DR: The peptide, designated as nartazin, was purified from the bulbs of the Chinese daffodil Narcissus tazetta var.
25 citations
TL;DR: A heterodimeric napin-like polypeptide with translation-inhibiting and antibacterial activities has been isolated from kale seeds but did not exert antifungal, ribonuclease, or protease activity.
Abstract: A heterodimeric napin-like polypeptide with translation-inhibiting and antibacterial activities has been isolated from kale seeds. The purification procedure entailed ion-exchange chromatography on dielthylaminoethyl (DEAE)-cellulose, affinity chromatography on Affi-gel blue gel, ion-exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S, and gel filtration by FPLC on Superdex 75. The napin-like polypeptide was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and Mono S. Its 7-kDa large subunit differs in N-terminal amino acid sequence from the 4-kDa small subunit. The polypeptide inhibited translation in the rabbit reticulocyte lysate system with an IC50 of 37.5 nM. This activity was preserved between pH 5 and pH 11, and between 10 and 40 degrees C. It fell to a low level at pH 3 and pH 13 and at 70 degrees C. Antibacterial activity against Bacillus, Megabacterium, and Pseudomonas species and antiproliferative activity against leukemia L1210 cells were observed. However, the polypeptide did not exert antifungal, ribonuclease, or protease activity.
14 citations
TL;DR: Two antifungal peptides (designated alpha- and beta-basrubrins) and a peptide and a protein with N-terminal sequences resembling heat shock protein (hsp) and serine-threonine kinase-like protein, respectively, were isolated from seeds of the Ceylon spinach Basella rubra and neither exhibited DNase, RNase, lectin or protease activity, indicating that their antif fungus action is not due to these activities.
12 citations
TL;DR: Comparison of the sequence of amino acids in the peptide fragment of MCoCI and the molecular mass with those of other protease inhibitors suggests that this inhibitor belongs to the potato I inhibitor family.
Abstract: A 7514-Da chymotrypsin inhibitor was isolated from the seed extract of Momordica cochinchinensis (Family Cucurbitaceae) by chromatography on chymotrypsin-Sepharose 4B and subsequently by C18 reversed-phase HPLC. This inhibitor, named MCoCI, possessed remarkable thermostability and was stable from pH 2 to 12. MCoCI also inhibited subtilisin, but had at least 50-fold lower inhibitory activity towards trypsin and elastase. Amino acid sequencing of a peptide fragment of MCoCI revealed a sequence of 23 amino acids. Comparison of this sequence and the molecular mass with those of other protease inhibitors suggests that MCoCI belongs to the potato I inhibitor family.
11 citations