. 2014 Oct 9;7:151. doi: 10.1186/s13068-014-0151-5

Table 1.

Identification of peptides in purified enzymes

Enzyme	GH family	Molecular mass (theoretical, kDa)	Similar protein (NCBI GI number)	Species	Peptide sequences	Accession number	Reference
Bgl3A	3	84.5	β-d-Glucoside glucohydrolase (GI:210068788)	Talaromyces marneffei ATCC 18224	K.GPCVGNTAAPSGISFPSLCIQDSPLGVR.Y	[FZ427523]	[31]
					R.YANPVTAFPAGTNAGMTWDR.T
					K.GLGVHVQLGPVAGPLGK.I
					K.HYIGNEQELNR.E
					R.TLHELYLWPFADAVR.A
					R.GCDTGTLAMGWGSGTCQFPYLTDPLTAIK.T
					K.LSLAAGASGTATFDLTRR.D
Cel5A	5	42.6	Endoglucanase, putative (GI:218723193)	Talaromyces stipitatus ATCC 10500	R.IPFAMER.M^a	[HV540858]	[20]
					K.VIFDTNNEYHDMDETLVFNLNQAAIDGIR.G
					R.VEGATAWLQANKK.L
Cel6A	6	47.8	Cellobiohydrolase, putative (GI:242804399)	Talaromyces stipitatus ATCC 10500	K.AAEIPSFVWLDTAAK.V	[AB022429]	[23]
					K.VPTMGTYLANIEAANK.A
					K.AGASPPIAGIFVVYDLPDR.D
					R.DCAAAASNGEYTVANNGVANYK.A
					K.AYPDVHTILIIEPDSLANMVTNLSTAK.C
Cel7A	7	55.0	1,4-β-d-Glucan-cellobiohydrolyase, putative (GI:212538337)	Talaromyces marneffei ATCC 18224	K.SGGSCTTNSGAITLDANWR.W	[E39854]	[25]
					K.AGAQYGVGYCDSQCPR.D
					R.YAGTCDPDGCDFNPYR.L
					R.LGVTDFYGSGK.T
					R.YYVQNGVVIPQPSSK.I
Cel7B	7	50.9	Endoglucanase, putative (GI:210064489)	Talaromyces marneffei ATCC 18224	R.VYLLDPAGK.N^a	[HV540856]	[20]
Cel7B	7	50.9	Endoglucanase, putative (GI:210064489)	Talaromyces marneffei ATCC 18224	K.TGTLTEIR.R	[HV540856]	[20]
Xyl10A	10	43.4	Endo-1,4-β-xylanase, putative (GI:242803213)	Talaromyces stipitatus ATCC 10500	K.GQCYAWDVVNEALNEDGTYR.Q	[AB796434]	[26]
Xyl10A	10	43.4	Endo-1,4-β-xylanase, putative (GI:242803213)	Talaromyces stipitatus ATCC 10500	R.MTLPDTSALQTQQSTDYQTTTTACVQTK.G	[AB796434]	[26]

Theoretical molecular mass of the identified protein was based on the putative amino acid sequence including a signal sequence. Tryptic peptide fragments were identified by matching MS/MS spectra to Aspergillus, Talaromyces, and Hypocrea peptide sequences in the NCBI database. Cel5A and Cel7B peptides were identified by matching MALDI-TOF MS spectra with amino acid sequence translations of open reading frames in the T. cellulolyticus draft genome. ^aFragments were identified by both MS/MS spectra and MALDI-TOF MS spectra. GH, glycosyl hydrolase; MALDI-TOF MS, matrix-assisted laser desorption ionization time-of-flight mass spectrometry; MS/MS, tandem mass spectrometry.