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Table 1 Identification of peptides in purified enzymes

From: Identification and characterization of core cellulolytic enzymes from Talaromyces cellulolyticus (formerly Acremonium cellulolyticus) critical for hydrolysis of lignocellulosic biomass

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.Ma

[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.Na

[HV540856]

[20]

K.TGTLTEIR.R

Xyl10A

10

43.4

Endo-1,4-β-xylanase, putative (GI:242803213)

Talaromyces stipitatus ATCC 10500

K.GQCYAWDVVNEALNEDGTYR.Q

[AB796434]

[26]

R.MTLPDTSALQTQQSTDYQTTTTACVQTK.G

  1. 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.